{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SDX8","uniProtkbId":"A0A9P5SDX8_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-09-13","entryVersion":14,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326566.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00081752"}],"value":"Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013008"}],"value":"2.1.3.2"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012918"}],"value":"3.5.1.2"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044063"}],"value":"6.3.4.16"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012738"}],"value":"6.3.5.5"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326566.1"}],"value":"BG006_010024"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00058513"}],"value":"Multifunctional protein that encodes the first 2 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5) and aspartate transcarbamylase (ATCase; EC 2.1.3.2). The CPSase-function is accomplished in 2 steps, by a glutamine-dependent amidotransferase activity (GATase) that binds and cleaves glutamine to produce ammonia, followed by an ammonium-dependent carbamoyl phosphate synthetase, which reacts with the ammonia, hydrogencarbonate and ATP to form carbamoyl phosphate. The endogenously produced carbamoyl phosphate is sequestered and channeled to the ATCase active site. ATCase then catalyzes the formation of carbamoyl-L-aspartate from L-aspartate and carbamoyl phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"ecNumber":"3.5.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049534"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20013"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29991"},{"database":"ChEBI","id":"CHEBI:32814"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"}],"ecNumber":"2.1.3.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048859"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18633"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048816"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + NH4(+) + 2 ATP = carbamoyl phosphate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18029"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047359"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001947"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004812"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004852"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043998"}],"value":"In the 2nd section; belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043968"}],"value":"In the 3rd section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043979"}],"value":"In the C-terminal section; belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043984"}],"value":"In the N-terminal section; belongs to the CarA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326566.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":575,"modifier":"EXACT"},"end":{"value":767,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":1110,"modifier":"EXACT"},"end":{"value":1301,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":1368,"modifier":"EXACT"},"end":{"value":1520,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Active site","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":399,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":401,"modifier":"EXACT"},"end":{"value":401,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00409"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00409"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326566.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326566.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000766","properties":[{"key":"ProteinId","value":"KAF9326566.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016597","properties":[{"key":"GoTerm","value":"F:amino acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004070","properties":[{"key":"GoTerm","value":"F:aspartate carbamoyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004151","properties":[{"key":"GoTerm","value":"F:dihydroorotase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006207","properties":[{"key":"GoTerm","value":"P:'de novo' pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019240","properties":[{"key":"GoTerm","value":"P:L-citrulline biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006228","properties":[{"key":"GoTerm","value":"P:UTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01744","properties":[{"key":"EntryName","value":"GATase1_CPSase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01423","properties":[{"key":"EntryName","value":"MGS_CPS_I_III"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1370:FF:000002","properties":[{"key":"EntryName","value":"Aspartate carbamoyltransferase 2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000025","properties":[{"key":"EntryName","value":"Bifunctional pyrimidine biosynthesis protein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000011","properties":[{"key":"EntryName","value":"CAD protein-like isoform X1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000004","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase (glutamine-hydrolyzing)"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.50.30.20:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase 1, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.140:FF:000036","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1380:FF:000009","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase, large subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1370","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.50.30.20","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase small subunit, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.140","properties":[{"key":"EntryName","value":"Metal-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01209","properties":[{"key":"EntryName","value":"CPSase_S_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006132","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoyltranf_P-bd"}]},{"database":"InterPro","id":"IPR006130","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase"}]},{"database":"InterPro","id":"IPR036901","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase_sf"}]},{"database":"InterPro","id":"IPR002082","properties":[{"key":"EntryName","value":"Asp_carbamoyltransf"}]},{"database":"InterPro","id":"IPR006131","properties":[{"key":"EntryName","value":"Asp_carbamoyltransf_Asp/Orn-bd"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR006274","properties":[{"key":"EntryName","value":"CarbamoylP_synth_ssu"}]},{"database":"InterPro","id":"IPR002474","properties":[{"key":"EntryName","value":"CarbamoylP_synth_ssu_N"}]},{"database":"InterPro","id":"IPR036480","properties":[{"key":"EntryName","value":"CarbP_synth_ssu_N_sf"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR035686","properties":[{"key":"EntryName","value":"CPSase_GATase1"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR032466","properties":[{"key":"EntryName","value":"Metal_Hydrolase"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00670","properties":[{"key":"EntryName","value":"asp_carb_tr"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01368","properties":[{"key":"EntryName","value":"CPSaseIIsmall"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009475","properties":[{"key":"EntryName","value":"PRK12838.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF5","properties":[{"key":"EntryName","value":"CAD PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00988","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00185","properties":[{"key":"EntryName","value":"OTCace"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02729","properties":[{"key":"EntryName","value":"OTCace_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00101","properties":[{"key":"EntryName","value":"ATCASE"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"PRINTS","id":"PR00099","properties":[{"key":"EntryName","value":"CPSGATASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01097","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53671","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52021","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, small subunit N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF51556","properties":[{"key":"EntryName","value":"Metallo-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00097","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPAQVRASTTKAPVAVYPMPPVTAAPCDQAEASTVATLVLQDGSSYQGISFGAETKSISGECVFQTGMVGYPESLTDPSYRGQILVLTFPLVGNYGVPSRETMDPLLKDLPKHFESNEIHIAGLIVGQYSQDFSHFLATSSLGAWLKEFNIPAIYGIDTRAMTKKIRSQGVMLGKILFPTSIVGPTVIPASEEWMAAYQNVEYVDPNARNLVAEVSLKEPKIYSPEPATAVLGPNGKPLRILAVDVGMKFNQIRCFVARGVEVKVVPWDYDFNADTDYDGLFISNGPGDPTMTKVTIGHLTKALQIARTPIFGICLGHQLLALASGATTKKMKFGNRGHNIPCTDMISGRCYISSQNHGYAVDVATLPENFMELFVNANDGSNEGIMHKTLPIFSVQFHPESTPGPRDTEYLFDVFIKAVDDFRKTGTLKAITMPGGTKEAAAALNPRVSVRKVLVLGSGGLSIGQAGEFDYSGSQAIKALKEEGIYTVLINPNIATIQTSKGLADKVYFLPVTPEFVRKVILREKPDGIYVTFGGQTALSVGIKMKDEFAGLGVRVLGTPIETIIATEDREIFAQRMLSIGEKIAQAQTAVNIQEAIDAANQIGYPVICRAAFALGGLGSGFANNDEELTELVSRAFATSPQVLIERSMKGWKEIEYEVVRDCRDNCITVCNMENFDPLGIHTGDSIVVAPSQTLSDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPFSKEYCIIEVNARLSRSSALASKATGYPLAFVAAKLGLNIPLNEISNSVTKVTCACFEPSLDYVVVKMPRWDLAKFDRVSKALSSSMKSVGEVMAIGRTFEETIQKAIRAIDPSLVGFAPKESYPVIDDELMNPNDQRVFAIANAMNQGYSVDRIWELTKIDKWFLNKLQNIVRLDKTLGNFTASDVPASMLRSAKQLGFSDRQIATAISSNELSVRRLRTDAGIVPFVKQIDTVAAEFPAFTNYLYMTYNAVEHDVTFEDKGVMVLGSGVYRIGSSVEFDWCAVRAIRTLRGRGVKTVMVNYNPETVSTDYDEADRLYFENINLERILDIYEAETSSGVVIAMGGQTPNNIALPLHRQNVKILGTSPEMIDTAENRYKFSRMLDQINVDQPLWKELTSFDEAGEFCEKVGYPVLVRPSYVLSGAAMNVVYSPDDLSNYLGQATAVSRDHPVVISKYIEDAKEIEMDAIAVNGKMVMHVVSEHVENAGVHSGDATLILPPQDLDPETIRKIEVATAKIGQALDVTGCYNIQFIAKDNDIKVIECNLRASRSMPFVSKVMEVDLIEMATNAMLGFPVEAYPESPIPKSGYVGIKVPQFSFSRLSGADPILGVEMASTGEVACFGKDKYEAYIKALVSTGFTLPKKNVLLSIGSFKEKQEMLPAVKRLRALGYNLFATSGTADFMSEHGVAVKYLETLEDDNDSQKSEYSLNQHLANNLIDLYINLPSKNRYRRPASYVSKGYRTRRMAVDFSVPLITNVKCAKLFVEALARHKDFEIEVVDYKDSNRTVTLPGLVNIQTLVPGISTAASKDFDNVSKTAISSGFTMIGAMATGIPKGVEDKATLAIATTNTRNHAHCDFFLSQNANVDNANDRLKETSALFIPFAPMSGRAVANVAEAAKHFSSWPASSPIVTDAKGTDLASILLLASLHNRPVHITGVSSADDMALIMMSKDKELQVTCDIEVYSLFLTSEETGSKLLPTKAEQDAFWNSLHVFDCFTVGSLPYRLAAEKGTPLAHAGIEETLPLLVDAVNKGRLTMADVIAKLYTNPRKIFSLPEQKDSYVEIETDRACVLSSTSGPFAGKALSGTVHRVVLHGQTAYLDGAWYTTGSEGQDVSSVAQAITKAVEKVVHPAAVSTGAVMHSPRLGPSPDAAEARRSSVQLEAAPANIPQAISNVVKEMPSSIARIINNSPFSHRHILSSKQFDRNELHALFSLAHEMRTQVERNGSIDLLRGKVMCSMFYEPSTRTSCSFAAAMARLGGSVGETLADTVRTLGCYGDLIVLRHPDPGSAAIAAKFSKVPVINAGDGIGEHPTQAFLDVYTIREELGTVNGLTITLVGDLKNGRTVHSLVKLLAYYHVTLNFVSPPSLRMPESVKAELSQAGVIVNEYTDLNDVIAESDVVYVTRVQKERFSDLNEYERVKSAYIEPEVDFDQRAAYFRQMRYGLYVRMALLALLSLVID","length":2189,"molWeight":239123,"crc64":"44246FF0B64AAC81","md5":"1A87D733EC8DDBFA14F3427C799C8B82"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"PATHWAY":2,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Domain":3,"Active site":3},"uniParcId":"UPI001D40288A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SI19","uniProtkbId":"A0A9P5SI19_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-09-13","entryVersion":14,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326989.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00068309"}],"value":"Fatty acid synthase subunit beta"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012948"}],"value":"1.1.1.100"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012996"}],"value":"1.3.1.9"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013256"}],"value":"2.3.1.38"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013258"}],"value":"2.3.1.39"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013191"}],"value":"2.3.1.41"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012878"}],"value":"2.3.1.86"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012480"}],"value":"3.1.2.14"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013167"}],"value":"4.2.1.59"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326989.1"}],"value":"FAS2"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326989.1"}],"value":"BG006_009655"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + holo-[ACP] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15057"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"Rhea","id":"RHEA-COMP:9924"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30823"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78783"}],"ecNumber":"3.1.2.14","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048536"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17397"},{"database":"Rhea","id":"RHEA-COMP:9916"},{"database":"Rhea","id":"RHEA-COMP:9945"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:78776"},{"database":"ChEBI","id":"CHEBI:78827"}],"ecNumber":"1.1.1.100","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048508"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13097"},{"database":"Rhea","id":"RHEA-COMP:9925"},{"database":"Rhea","id":"RHEA-COMP:9945"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:78784"},{"database":"ChEBI","id":"CHEBI:78827"}],"ecNumber":"4.2.1.59","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001055"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10240"},{"database":"Rhea","id":"RHEA-COMP:9925"},{"database":"Rhea","id":"RHEA-COMP:9926"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:78784"},{"database":"ChEBI","id":"CHEBI:78785"}],"ecNumber":"1.3.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048572"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a fatty acyl-[ACP] + malonyl-[ACP] + H(+) = a 3-oxoacyl-[ACP] + holo-[ACP] + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22836"},{"database":"Rhea","id":"RHEA-COMP:9623"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"Rhea","id":"RHEA-COMP:9916"},{"database":"Rhea","id":"RHEA-COMP:14125"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78449"},{"database":"ChEBI","id":"CHEBI:78776"},{"database":"ChEBI","id":"CHEBI:138651"}],"ecNumber":"2.3.1.41","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049541"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H(+) = a long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP(+).","ecNumber":"2.3.1.86","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048237"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"holo-[ACP] + acetyl-CoA = acetyl-[ACP] + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:41788"},{"database":"Rhea","id":"RHEA-COMP:9621"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78446"}],"ecNumber":"2.3.1.38","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048835"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"holo-[ACP] + malonyl-CoA = malonyl-[ACP] + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:41792"},{"database":"Rhea","id":"RHEA-COMP:9623"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57384"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78449"}],"ecNumber":"2.3.1.39","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048462"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pantetheine 4'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00258"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:47942"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00033756"}],"value":"[Alpha(6)beta(6)] hexamers of two multifunctional subunits (alpha and beta)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010009"}],"value":"Belongs to the fungal fatty acid synthetase subunit beta family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007485"}],"value":"Belongs to the thiolase-like superfamily. Fungal fatty acid synthetase subunit alpha family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326989.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":2064,"modifier":"EXACT"},"end":{"value":2141,"modifier":"EXACT"}},"description":"Carrier","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50075"}]},{"type":"Domain","location":{"start":{"value":2255,"modifier":"EXACT"},"end":{"value":2332,"modifier":"EXACT"}},"description":"Carrier","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50075"}]},{"type":"Domain","location":{"start":{"value":3215,"modifier":"EXACT"},"end":{"value":3752,"modifier":"EXACT"}},"description":"Ketosynthase family 3 (KS3)","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS52004"}]},{"type":"Region","location":{"start":{"value":2700,"modifier":"EXACT"},"end":{"value":2720,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":3444,"modifier":"EXACT"},"end":{"value":3467,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":3397,"modifier":"EXACT"},"end":{"value":3397,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10022"}]},{"type":"Modified residue","location":{"start":{"value":2099,"modifier":"EXACT"},"end":{"value":2099,"modifier":"EXACT"}},"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00258"}]},{"type":"Modified residue","location":{"start":{"value":2290,"modifier":"EXACT"},"end":{"value":2290,"modifier":"EXACT"}},"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00258"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022450"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00258"}],"id":"KW-0596","category":"PTM","name":"Phosphopantetheine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326989.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326989.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000713","properties":[{"key":"ProteinId","value":"KAF9326989.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005835","properties":[{"key":"GoTerm","value":"C:fatty acid synthase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019171","properties":[{"key":"GoTerm","value":"F:(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004316","properties":[{"key":"GoTerm","value":"F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004315","properties":[{"key":"GoTerm","value":"F:3-oxoacyl-[acyl-carrier-protein] synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004318","properties":[{"key":"GoTerm","value":"F:enoyl-[acyl-carrier-protein] reductase (NADH) activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004312","properties":[{"key":"GoTerm","value":"F:fatty acid synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004321","properties":[{"key":"GoTerm","value":"F:fatty-acyl-CoA synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008897","properties":[{"key":"GoTerm","value":"F:holo-[acyl-carrier-protein] synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006633","properties":[{"key":"GoTerm","value":"P:fatty acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00828","properties":[{"key":"EntryName","value":"elong_cond_enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03447","properties":[{"key":"EntryName","value":"FAS_MaoC"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08950","properties":[{"key":"EntryName","value":"KR_fFAS_SDR_c_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.470.20:FF:000005","properties":[{"key":"EntryName","value":"Fatty acid synthase alpha subunit FasA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.930.70:FF:000001","properties":[{"key":"EntryName","value":"Fatty acid synthase beta subunit dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000078","properties":[{"key":"EntryName","value":"Fatty acid synthase beta subunit dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.366.10:FF:000007","properties":[{"key":"EntryName","value":"Fatty acid synthase beta subunit dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000168","properties":[{"key":"EntryName","value":"Fatty acid synthase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.25.70:FF:000001","properties":[{"key":"EntryName","value":"Fatty acid synthase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.3330:FF:000001","properties":[{"key":"EntryName","value":"Fatty acid synthase subunit beta dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.366.10:FF:000003","properties":[{"key":"EntryName","value":"Fatty acid synthase subunit beta dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.930.70","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1120.100","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.3330","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.47.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.90.25.70","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.140.1390","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.140.1400","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.140.1410","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.250.1930","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.250.1940","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.60.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.20.240.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.470.20","properties":[{"key":"EntryName","value":"4'-phosphopantetheinyl transferase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.10.129.10","properties":[{"key":"EntryName","value":"Hotdog Thioesterase"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.366.10","properties":[{"key":"EntryName","value":"Malonyl-Coenzyme A Acyl Carrier Protein, domain 2"},{"key":"MatchStatus","value":"3"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR008278","properties":[{"key":"EntryName","value":"4-PPantetheinyl_Trfase_dom"}]},{"database":"InterPro","id":"IPR037143","properties":[{"key":"EntryName","value":"4-PPantetheinyl_Trfase_dom_sf"}]},{"database":"InterPro","id":"IPR001227","properties":[{"key":"EntryName","value":"Ac_transferase_dom_sf"}]},{"database":"InterPro","id":"IPR014043","properties":[{"key":"EntryName","value":"Acyl_transferase_dom"}]},{"database":"InterPro","id":"IPR016035","properties":[{"key":"EntryName","value":"Acyl_Trfase/lysoPLipase"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR039569","properties":[{"key":"EntryName","value":"FAS1-like_DH_region"}]},{"database":"InterPro","id":"IPR013565","properties":[{"key":"EntryName","value":"Fas1/AflB-like_central"}]},{"database":"InterPro","id":"IPR040899","properties":[{"key":"EntryName","value":"Fas_alpha_ACP"}]},{"database":"InterPro","id":"IPR047224","properties":[{"key":"EntryName","value":"FAS_alpha_su_C"}]},{"database":"InterPro","id":"IPR040883","properties":[{"key":"EntryName","value":"FAS_meander"}]},{"database":"InterPro","id":"IPR041550","properties":[{"key":"EntryName","value":"FASI_helical"}]},{"database":"InterPro","id":"IPR003965","properties":[{"key":"EntryName","value":"Fatty_acid_synthase"}]},{"database":"InterPro","id":"IPR050830","properties":[{"key":"EntryName","value":"Fungal_FAS"}]},{"database":"InterPro","id":"IPR029069","properties":[{"key":"EntryName","value":"HotDog_dom_sf"}]},{"database":"InterPro","id":"IPR014031","properties":[{"key":"EntryName","value":"KAS_C"}]},{"database":"InterPro","id":"IPR014030","properties":[{"key":"EntryName","value":"KAS_N"}]},{"database":"InterPro","id":"IPR018201","properties":[{"key":"EntryName","value":"Ketoacyl_synth_AS"}]},{"database":"InterPro","id":"IPR002539","properties":[{"key":"EntryName","value":"MaoC-like_dom"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR020841","properties":[{"key":"EntryName","value":"PKS_Beta-ketoAc_synthase_dom"}]},{"database":"InterPro","id":"IPR009081","properties":[{"key":"EntryName","value":"PP-bd_ACP"}]},{"database":"InterPro","id":"IPR004568","properties":[{"key":"EntryName","value":"Ppantetheine-prot_Trfase_dom"}]},{"database":"InterPro","id":"IPR032088","properties":[{"key":"EntryName","value":"SAT"}]},{"database":"InterPro","id":"IPR016039","properties":[{"key":"EntryName","value":"Thiolase-like"}]},{"database":"NCBIfam","id":"TIGR00556","properties":[{"key":"EntryName","value":"pantethn_trn"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10982:SF21","properties":[{"key":"EntryName","value":"FATTY ACID SYNTHASE SUBUNIT BETA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10982","properties":[{"key":"EntryName","value":"MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01648","properties":[{"key":"EntryName","value":"ACPS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00698","properties":[{"key":"EntryName","value":"Acyl_transf_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08354","properties":[{"key":"EntryName","value":"Fas1-AflB-like_hel"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13452","properties":[{"key":"EntryName","value":"FAS1_DH_region"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22235","properties":[{"key":"EntryName","value":"FAS1_thioest_ins"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF18325","properties":[{"key":"EntryName","value":"Fas_alpha_ACP"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF18314","properties":[{"key":"EntryName","value":"FAS_I_H"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17951","properties":[{"key":"EntryName","value":"FAS_meander"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00109","properties":[{"key":"EntryName","value":"ketoacyl-synt"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02801","properties":[{"key":"EntryName","value":"Ketoacyl-synt_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01575","properties":[{"key":"EntryName","value":"MaoC_dehydratas"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16073","properties":[{"key":"EntryName","value":"SAT"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01483","properties":[{"key":"EntryName","value":"FASYNTHASE"}]},{"database":"SMART","id":"SM00827","properties":[{"key":"EntryName","value":"PKS_AT"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56214","properties":[{"key":"EntryName","value":"4'-phosphopantetheinyl transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52151","properties":[{"key":"EntryName","value":"FabD/lysophospholipase-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF51412","properties":[{"key":"EntryName","value":"Inosine monophosphate dehydrogenase (IMPDH)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54637","properties":[{"key":"EntryName","value":"Thioesterase/thiol ester dehydrase-isomerase"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF53901","properties":[{"key":"EntryName","value":"Thiolase-like"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50075","properties":[{"key":"EntryName","value":"CARRIER"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00606","properties":[{"key":"EntryName","value":"KS3_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS52004","properties":[{"key":"EntryName","value":"KS3_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFGGQGNIEEYFDELAEIYTTYTTLVQDYVEDMAAVLREHAKSDDASVFHSKGLDVMAWLRNPDSKPDVAYLVSAPVSLPLIGLVQLMHYYAMLKILDQTPIQLRDVILGSTGHSQGIISSVVISASATFEDFFANSRKALGLLFWIGTRSQQVYPQTTLNPAILQDSLSNNEGNPTPMLVVNSLRASEVQKYVEATNLHLPEDRKIKIALINGPRSSICTGPPQSLYGLNLALRKLKAPTGLEQGRVPFSQRKVKFSSRFLPITAPFHSSYLDGVSTLVAEDITRYDLAFDHTKMTVPVFSTDSGKDISGSATVTMDLVDQICSLPVHWEKATAMAGLTHVIDFGPGGSSGVGSLTARNKDGTGVQVILAGATEGVNRELSYKSDLFDANPASLRYAPNWVSEFQPKLVRSVNGEIHIDTRMSRLLAKPPLMVAGMTPSTVHEGFVSAVMNAGYHVELAGGGHYNEEAVRTKVKKIMQLTTPGAGITLNTLFINVRQWGFQAPLVPKLRREGLPMEGFCCAAGVPSLEVANEFISDMHEAGIRHVSFKPGSADAIRQVLAIAAAHPEMPIILQWTGGRAGGHHSFEDFHAPIFETYSAIRRHANVILVAGSGFGGAEDTLPYLTGDWSVEFDYPPMPFDGMLFGSRVMVAKEGMASLGVKQAIVDAPGVGDSEWEKTYKGPTGGVMTVRSELGEPIHKIATRGVKLWKEMDDTIFALPKDKRPAALLAKKDYIIKRLNADFQKVWFGKKSDGSVADLQDMTYEEVINRLIELLFIKHEERWIDHSHRNLLGDILRRIEERFVGVEKNSIVQTFSQIQVPFDFAQEFINTYPLTKTQLLTTEDVGYFLFLMQRRGQKPVPFIPVLDKDFEVWFKKDSLWQAEDLSAVVDQDVQRTCILQGPTAVRYATKVDEPVKDILDGIFHSHIASLKERYYNNDDASIPQVEYFGGKPGRFESATKAISPLVKISTDAEGRVALVETSTLESSLPQTEDWLEFLAGQDPSWFRALLTAPAVIQGKKFLNNPLARIFRPRVSQTVQFEYKDEKLHTVTVYDRRSWSASSKSNDLSPSLRARMQPNELIEVVLVEKNGERLIPFPLLFHYTPEKGYAPIHEVMEGRNERIKEFYYKLWFPTEEDQFTNCLATNAFTEKFICNGESVNTPEIKEFCQAVGNQAELYVERRQKVVYAPMDFAIVVGWKSIIKAIFPKSIDGDLLKLVHLSNGFRMLDGAESLKEGDIVDTVAEINAVVNNDSGKLVQVKGVVLRDGKRVMEVTSEFLYRGTFTDYHNTFQKTVETPMQVQLASAKDVAVLKSKEWIQWAEGEHTVAPGASLVFRLNTVVRFKNKQTFSHVETTGTVSMQISTKEHVEIATVQYTNEELSHGNPVLAYLKRNGSPIEQAVHFENGGYSVMPEGSFSSEVISPFSNEPYAKVSGDFNPIHVNPYFADLAELPGTITHGMWTSASTRKFVEIFAADNHPQRVTSYEVSFLSMVLPQDRLSTKLSHIGMINGKKIIKVETVNQNGTKVVEGTAEIDQPTIAYVFTGQGSQEQGMGMALYDSSPVAKAIWQKADRHFLENYGFSILDIVRNNPLKKTIHFGGPKGNAIRQNYMSMRYDLVEQDGSIKSLPLFPGINETTHFYTFQSPNGLLAATQFTQPALTLMEKAAFEDMRAKGLIQGNCAFAGHSLGEYSALASIGDVLPIESLVDVVFYRGMTMQVAVPRDEVGRSNYGMVAINPSRVSPTFNDSALRYVVDAIARQSNGLLEIVNENVENWQYVAAGELSNLDALSTVLNYLKVQKIDLQKLMETMPLEEVKKHLSQIIAGALEKVAEKLAKDGLIKPERGVATIPLAGIDVPFHSSFLLSGVAPFRTYLAKKINPTNINVPLLTAKYIPNLTAKPFSIEKSYVEGVYSLTSSPRLAKVLKNWVDTKLTAKQQQRLGYTLLVELLAYQFASPVRWIETQDRLFKEFNIVRLIEVGPSPTLCGMAQRTLKFKYEAYDDALTFQRSTLCTSKDAKEIYYAMDNVESSSPAPAAAAASAPKAAAPVVVAAPAPIASAGPAAAVADAPIKAVEILHVIVAQKVKKTLEEVPLSKAIKDLVGGKSTLQNEILGDLQKEFGGSGFPEKGEEAPLEELANALQGNFNGALGKQTTSLIAKMIGSKMPGGFSLSTAKGYLNKTHGLGPVRADAALLVGLTMEPAARLGAAPEANAWLDTVAQAYARRAGVTLGAGAPAGAASVQMMAAAPAGAGAPAAVADAPIKAIDILHVIVAQKIKKTVDEVPLSKAIKDLVGGKSTLQNEILGDLQKEFGGSGFPEKGEEAPLEDLGNALQANFNGSLGKQTTSLIAKMIGSKMPGGFTQSSAKGYLASAYGLGSLRADGALLLGLTMEPAARLGAEPEAKAWLDTVAQAYARRAGISLGGGGGGAVAGGAVGGAMMNSEEFNQFQAKQNAMMYQHLEIYARYLEKDLRAGEKQYEEEKIATLRLQADIDQWMAEHGDYYAEGIKPNFSVKKARKYDSHWNWVRQDALSLLYDMIFGRLTVVDREIVAQCIHVMNRANPQLLQFMIYHIDNTAADRGKTYALAKEFGNMLIQNCREVLEAAPVYKDVGVPTGPSTSIDNKGNILYEEVQRAGVRKLDHYVKDMAAGGKMSEFSNRQKVQKNLAQIYKIIKAQNNMKSSSKLAIKSLYGEVIHAMNMSNTIIREEKNRRASRVRRASAVPTDRPKKEAKKETIPFLHLKKKNPHSESGWEFSQRLTAVYLDVLTNMAKDGVTYENRMVLMTGAGKDSIGSAILKGLLSGGAKVIVTTSRFSRDVTEYYQSIYQRHGSKNSSLVVVPFNGGSKQDVDALVNYIYDKDPKKGLGWDLDYIIPFAAISVQGKEIDNIDSQSELAHRIMLTNVLRLLGNVKTKKMENGYDTRPAQVILPLSPNHGTFGADGLYGESKVALETLFNRWTSESWSAYLTITGAVIGWTRGTGLMSGNNIVAEGLEKYGVRTFSAQEMAFNILGLMHPSITNLCQIEPVWADLNGGLQYLVNVNEVSANLRAEYRQTSEIRKAIVAENTLDFKEVHGAEAERKHQPHKVTPRANMKFPFPELKNYKDLSHAHKLRGMLDLENVVVVTGFSEVGPWGNSRTRWEMEAKGQFSLEGCIEMAWIMGFIKHHNGNLKSGAPYSGWVDAKTGEPVKDKDVKSKYEKQILEHTGIRLIEPELFGGYDPKRKGLLQEVLIDHDLEAFEVSKEEAQMFKLEHGDKVDIYEEESGQWAVKFKKGANMYIPKALKFDRLVAGQIPTGWDAARYGVPKDIIDQVDTITLYVLVSTVEALVASGITDPYEFYQYVHVSEVGNTAGSGVGGMLSLRGMYRDRVLDKPVQKDILQESFINTMPAWVNMLLLSSSGPIKTPVGACATAVESVEIGVDTIQSGKAKIVIVGGYDDFQEEGSYEFANMKATSNTEEEFAHGRTPQEMSRPATSTRSGFMESHGAGIEILMQAKLAIEMGVPIYGIVGLTNTATDKEGRSVPAPGQGVLTTAREVKSKMPSRLLDIKYRKRQIDQRRAQIKQWVENEYTELGHELEELKAAGELTVSEEEYLAAETERIQKEAKRQHREALNLWGNEFYKQDPQIAPLRGALASFGLTIDDIGVGSFHGTSTKANDKNESEVVNKQMEHLGRSKGNALPSIWQKYLTGHPKGAAAAWMMNGVLQVLQTGLIPGNRNADNIDNTMRQFEHVLYTSRSIQTDGVKAGLLKSFGFGQVGGEVLLIHADYILGALEEHEYEAYKAKQQARQAKSYRYLHDSMTGGPALVQVKNAPPYTPELESPVYLNPSARAQYNNATKSWAFNAKALVPTSAKVDVGMTRAILETSAAESLGESSPRGVGVDVEMVSAINIENETFLERNFTAQEIEYCLSRPDPQASFAGRWSAKEAVVKAVSSFSLGTEKVWTQGAGAGLKEIEIVMAESGAPSVVFAGAAQEAAAKAGVKEMKVSISHSGAYAVAVANAL","length":3990,"molWeight":438469,"crc64":"FF189B4A0C60A16D","md5":"22158EF41E1F3A84FABCFE18BFE9711F"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":8,"COFACTOR":1,"SUBUNIT":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":3,"Region":2,"Active site":1,"Modified residue":2},"uniParcId":"UPI001DBF9C2F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SQV5","uniProtkbId":"A0A9P5SQV5_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-09-13","entryVersion":11,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335765.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Pentafunctional AROM polypeptide"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-dehydroquinate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"DHQS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"4.2.3.4"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-phosphoshikimate 1-carboxyvinyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"2.5.1.19"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"5-enolpyruvylshikimate-3-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"EPSP synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"EPSPS"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Shikimate kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"SK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"2.7.1.71"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-dehydroquinate dehydratase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-dehydroquinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"4.2.1.10"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Shikimate dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"1.1.1.25"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335765.1"}],"value":"ARO1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335765.1"}],"value":"BG006_010655"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054455"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-dehydroquinate = 3-dehydroshikimate + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21096"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16630"},{"database":"ChEBI","id":"CHEBI:32364"}],"ecNumber":"4.2.1.10","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21256"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57701"},{"database":"ChEBI","id":"CHEBI:58702"},{"database":"ChEBI","id":"CHEBI:145989"}],"ecNumber":"2.5.1.19","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044633"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:21257"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044633"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21968"},{"database":"ChEBI","id":"CHEBI:32364"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58394"}],"ecNumber":"4.2.3.4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"shikimate + ATP = 3-phosphoshikimate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13121"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:36208"},{"database":"ChEBI","id":"CHEBI:145989"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.71","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048567"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"shikimate + NADP(+) = 3-dehydroshikimate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17737"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16630"},{"database":"ChEBI","id":"CHEBI:36208"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.1.1.25","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Binds 2 Zn(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004811"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009948"}],"value":"Belongs to the EPSP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the 2nd section; belongs to the EPSP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006477"}],"value":"In the 2nd section; belongs to the type-I 3-dehydroquinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the 3rd section; belongs to the shikimate kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the 4th section; belongs to the type-I 3-dehydroquinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the C-terminal section; belongs to the shikimate dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the N-terminal section; belongs to the dehydroquinate synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009349"}],"value":"In the N-terminal section; belongs to the shikimate kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335765.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01761"}]},{"type":"Domain","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":367,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF24621"}]},{"type":"Domain","location":{"start":{"value":417,"modifier":"EXACT"},"end":{"value":849,"modifier":"EXACT"}},"description":"Enolpyruvate transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00275"}]},{"type":"Domain","location":{"start":{"value":1329,"modifier":"EXACT"},"end":{"value":1410,"modifier":"EXACT"}},"description":"Shikimate dehydrogenase substrate binding N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08501"}]},{"type":"Domain","location":{"start":{"value":1447,"modifier":"EXACT"},"end":{"value":1508,"modifier":"EXACT"}},"description":"Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01488"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":393,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Region","location":{"start":{"value":1091,"modifier":"EXACT"},"end":{"value":1311,"modifier":"EXACT"}},"description":"3-dehydroquinase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Region","location":{"start":{"value":1324,"modifier":"EXACT"},"end":{"value":1610,"modifier":"EXACT"}},"description":"Shikimate dehydrogenase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"Proton acceptor; for 3-dehydroquinate synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"Proton acceptor; for 3-dehydroquinate synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":837,"modifier":"EXACT"},"end":{"value":837,"modifier":"EXACT"}},"description":"For EPSP synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":1213,"modifier":"EXACT"},"end":{"value":1213,"modifier":"EXACT"}},"description":"Proton acceptor; for 3-dehydroquinate dehydratase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":1242,"modifier":"EXACT"},"end":{"value":1242,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Binding site","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":89,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":365,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":894,"modifier":"EXACT"},"end":{"value":901,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0057","category":"Biological process","name":"Aromatic amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335765.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335765.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000086","properties":[{"key":"ProteinId","value":"KAF9335765.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003855","properties":[{"key":"GoTerm","value":"F:3-dehydroquinate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003856","properties":[{"key":"GoTerm","value":"F:3-dehydroquinate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003866","properties":[{"key":"GoTerm","value":"F:3-phosphoshikimate 1-carboxyvinyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004764","properties":[{"key":"GoTerm","value":"F:shikimate 3-dehydrogenase (NADP+) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004765","properties":[{"key":"GoTerm","value":"F:shikimate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009073","properties":[{"key":"GoTerm","value":"P:aromatic amino acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009423","properties":[{"key":"GoTerm","value":"P:chorismate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00502","properties":[{"key":"EntryName","value":"DHQase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08195","properties":[{"key":"EntryName","value":"DHQS"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01556","properties":[{"key":"EntryName","value":"EPSP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01065","properties":[{"key":"EntryName","value":"NAD_bind_Shikimate_DH"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00464","properties":[{"key":"EntryName","value":"SK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000135","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1970:FF:000007","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:001256","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.65.10.10:FF:000007","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.65.10.10:FF:000008","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1090.10","properties":[{"key":"EntryName","value":"Dehydroquinate synthase-like - alpha domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.65.10.10","properties":[{"key":"EntryName","value":"Enolpyruvate transferase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.10860","properties":[{"key":"EntryName","value":"Leucine Dehydrogenase, chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00210","properties":[{"key":"EntryName","value":"EPSP_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03143","properties":[{"key":"EntryName","value":"Pentafunct_AroM"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00109","properties":[{"key":"EntryName","value":"Shikimate_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR046346","properties":[{"key":"EntryName","value":"Aminoacid_DH-like_N_sf"}]},{"database":"InterPro","id":"IPR016037","properties":[{"key":"EntryName","value":"DHQ_synth_AroB"}]},{"database":"InterPro","id":"IPR030960","properties":[{"key":"EntryName","value":"DHQS/DOIS_N"}]},{"database":"InterPro","id":"IPR056179","properties":[{"key":"EntryName","value":"DHQS_C"}]},{"database":"InterPro","id":"IPR001381","properties":[{"key":"EntryName","value":"DHquinase_I"}]},{"database":"InterPro","id":"IPR001986","properties":[{"key":"EntryName","value":"Enolpyruvate_Tfrase_dom"}]},{"database":"InterPro","id":"IPR036968","properties":[{"key":"EntryName","value":"Enolpyruvate_Tfrase_sf"}]},{"database":"InterPro","id":"IPR006264","properties":[{"key":"EntryName","value":"EPSP_synthase"}]},{"database":"InterPro","id":"IPR023193","properties":[{"key":"EntryName","value":"EPSP_synthase_CS"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR008289","properties":[{"key":"EntryName","value":"Pentafunct_AroM"}]},{"database":"InterPro","id":"IPR013792","properties":[{"key":"EntryName","value":"RNA3'P_cycl/enolpyr_Trfase_a/b"}]},{"database":"InterPro","id":"IPR031322","properties":[{"key":"EntryName","value":"Shikimate/glucono_kinase"}]},{"database":"InterPro","id":"IPR013708","properties":[{"key":"EntryName","value":"Shikimate_DH-bd_N"}]},{"database":"InterPro","id":"IPR010110","properties":[{"key":"EntryName","value":"Shikimate_DH_AroM-type"}]},{"database":"InterPro","id":"IPR000623","properties":[{"key":"EntryName","value":"Shikimate_kinase/TSH1"}]},{"database":"InterPro","id":"IPR023000","properties":[{"key":"EntryName","value":"Shikimate_kinase_CS"}]},{"database":"InterPro","id":"IPR006151","properties":[{"key":"EntryName","value":"Shikm_DH/Glu-tRNA_Rdtase"}]},{"database":"NCBIfam","id":"TIGR01356","properties":[{"key":"EntryName","value":"aroA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01357","properties":[{"key":"EntryName","value":"aroB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01093","properties":[{"key":"EntryName","value":"aroD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01809","properties":[{"key":"EntryName","value":"Shik-DH-AROM"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21090","properties":[{"key":"EntryName","value":"AROM/DEHYDROQUINATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21090:SF5","properties":[{"key":"EntryName","value":"PENTAFUNCTIONAL AROM POLYPEPTIDE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01761","properties":[{"key":"EntryName","value":"DHQ_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF24621","properties":[{"key":"EntryName","value":"DHQS_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01487","properties":[{"key":"EntryName","value":"DHquinase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00275","properties":[{"key":"EntryName","value":"EPSP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01488","properties":[{"key":"EntryName","value":"Shikimate_DH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08501","properties":[{"key":"EntryName","value":"Shikimate_dh_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01202","properties":[{"key":"EntryName","value":"SKI"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000514","properties":[{"key":"EntryName","value":"Pentafunct_AroM"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01100","properties":[{"key":"EntryName","value":"SHIKIMTKNASE"}]},{"database":"SUPFAM","id":"SSF51569","properties":[{"key":"EntryName","value":"Aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53223","properties":[{"key":"EntryName","value":"Aminoacid dehydrogenase-like, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56796","properties":[{"key":"EntryName","value":"Dehydroquinate synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55205","properties":[{"key":"EntryName","value":"EPT/RTPC-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00104","properties":[{"key":"EntryName","value":"EPSP_SYNTHASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00885","properties":[{"key":"EntryName","value":"EPSP_SYNTHASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01128","properties":[{"key":"EntryName","value":"SHIKIMATE_KINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSHPNPHIQKVSILGSETIILGFHIFDYLLRDTLSNFKASTYVVVTDTNLQKLYLDRFLASFHRISQELSSGTLPRLLTYVIPPGEESKSRAVKAEIEDYFLAQGCTRDTLVFAMGGGVIGDLVGFVAATFMRGIPFVQVPTTLLAMVDSSIGGKTAIDTPMAKNPIGAFWQPKRIFIDLAVLETLPEREFVNGMAEVIKTAAIWNHDDFVLLENGAEAIRDAVLKPVRNVEFQGAILESRTAAQQLLLQVVMASVAVKSYVVTHDERETGMRGLLNFGHSIGHAIEGLVTPKLLHGECVAIGMIKEAEIARHCGYLSQVAVGRLTRCIQAYGLPVTMEDKFVKNHIGNQYCSVDELMQVLRVDKKNMGSQKRIVMLSGIGQTLEQKPSNISDDIIRKVLAASTVVHPRPINQPAVTLSPPGSKSISNRALVLAALGQGTCRLTGLLHSDDTQVMLTALTKLGAATFEWENNGDTLVVHGNGGKMHIPDSELYLGNAGTAARFLTTVSVLVPPSSISGQKTILTGNARMKQRPIAPLIDALTANGSELKYMEGQGCLPLEVTPFSHGLAGGEIQLAASISSQYVSSILLCAPYATKEPVTLVLTGGQVISQPYIDMTIAMMKSFGVNVEALPNNTYRIPQVHYVNPAAYLVEADASSATYPLAIAAITGTTCTVPNIGSASLQGDAGFAVNVLRPMGCTVVQTETSTTVIGPAIGTLKPLAHIDMETMTDAFLTASVLAAVTQPATPGAENITRISGIANQRVKECNRIAAMMHELGKFGVTTSETPDGIIVHGHDIASLTPPKDGVKCYDDHRVAMSFSVLASVVPGGTIIREKKCVEKTWPTWWDDLESKLNGRITDADLGVPSDHHDYEVKSSSSKKSAGAKSDATIVVIGMRGAGKTSMGRFAARTLKRPFEDVDHYFEKTLSTTIPEFIKEHGWPAFREQEAKMLTELLAKYPTKHVISCGGGIVETASSREAFKQYITQGGVVIHLVRNINEIEAYLNRDTTRPMYGESMRDVWARREAWYRECCNYEFVVAGQQLKGIEAEDAKEWALVESNFERFLKVITRAGKGKYASRSQVVAKPTFFLSLTFPDISPALPHLSKLTLGSDVIELRVDLLKSSDASGISFRDHVAQQVSLLRRHSDLPILYTVRSVSQGGQWPDKDIDGMVSLLKDGLEWGVEYLDVEIGLPRSRIDEVLPKKGNTLIVASWHDCKGTVRWNSDTMEAQYKLAHSISPDVIKLIGTATSMKDNFDCSEFAARHTKANDLPLIAMNMGAQGQLSRVLNNYLTPVTHKLLPVKAAPGQLTARDILIARNAVGLLPAKQFYLFGTPIRQSLSPLMHNTSFQSLGLPYTYDLHETETVDESVVAKMRSKDFGGASVTIPHKIDVMSKLDEITEEAKAIGAVNTVVPVEQEGKPSILVGDNTDWLGIYYQIERNLSSTSVAQPQQMKGLVLGAGGTSRAALYALHRLGVEDISIFNRTMVKAQAVADSFKNLFDVKVLSSNDLLKGSSASGFDLVVSTVPGTIESASMFDDSVFGSAKKGVAVELAYTPRFTRFLKMAQQSGWATVEGGQVLVEQGGWQALKWVGRRWDLESVQQQMDLVQAGRE","length":1610,"molWeight":175192,"crc64":"0C82F6DA224CF172","md5":"93FC5E85D3156CF9AA320ACA44D74F26"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":5,"COFACTOR":1,"PATHWAY":5,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":9,"CAUTION":2},"countByFeatureType":{"Domain":5,"Region":3,"Active site":5,"Binding site":20},"uniParcId":"UPI001DC9E0C2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SR17","uniProtkbId":"A0A9P5SR17_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-09-13","entryVersion":13,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335681.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034536"}],"value":"Flavin-containing monooxygenase 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034528"}],"value":"1.14.13.148"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012850"}],"value":"1.14.13.8"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012698"}],"value":"1.6.3.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034561"}],"value":"Dimethylaniline monooxygenase [N-oxide-forming] 1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00033301"}],"value":"Dimethylaniline monooxygenase [N-oxide-forming] 5"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029725"}],"value":"Dimethylaniline oxidase 1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029728"}],"value":"Dimethylaniline oxidase 5"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00019213"}],"value":"Flavin-containing monooxygenase 5"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00033213"}],"value":"NADPH oxidase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034554"}],"value":"Trimethylamine monooxygenase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335681.1"}],"value":"BG006_010935"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045722"}],"value":"Acts as a Baeyer-Villiger monooxygenase on a broad range of substrates. Catalyzes the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Active on diverse carbonyl compounds, whereas soft nucleophiles are mostly non- or poorly reactive. In contrast with other forms of FMO it is non- or poorly active on 'classical' substrates such as drugs, pesticides, and dietary components containing soft nucleophilic heteroatoms. Able to oxidize drug molecules bearing a carbonyl group on an aliphatic chain, such as nabumetone and pentoxifylline. Also, in the absence of substrates, shows slow but yet significant NADPH oxidase activity. Acts as a positive modulator of cholesterol biosynthesis as well as glucose homeostasis, promoting metabolic aging via pleiotropic effects"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045957"}],"value":"Broad spectrum monooxygenase that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including xenobiotics. Catalyzes the S-oxygenation of hypotaurine to produce taurine, an organic osmolyte involved in cell volume regulation as well as a variety of cytoprotective and developmental processes. In vitro, catalyzes the N-oxygenation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO) and could therefore participate to the detoxification of this compound that is generated by the action of gut microbiota from dietary precursors such as choline, choline containing compounds, betaine or L-carnitine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-geranial + NADPH + O2 + H(+) = (1E)-2,6-dimethylhepta-1,5-dien-1-yl formate + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54860"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16980"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:138375"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048989"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54861"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048989"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N,N-dimethylaniline + NADPH + O2 + H(+) = N,N-dimethylaniline N-oxide + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24468"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16269"},{"database":"ChEBI","id":"CHEBI:17735"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.14.13.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049443"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:24469"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049443"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADPH + O2 + H(+) = H2O2 + NADP(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11260"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047864"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11261"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047864"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"heptan-2-one + NADPH + O2 + H(+) = pentyl acetate + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54836"},{"database":"ChEBI","id":"CHEBI:5672"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:87362"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047574"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54837"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047574"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"heptan-4-one + NADPH + O2 + H(+) = propyl butanoate + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54852"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:89484"},{"database":"ChEBI","id":"CHEBI:89719"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048990"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54853"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048990"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hexan-3-one + NADPH + O2 + H(+) = ethyl butanoate + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54844"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:88764"},{"database":"ChEBI","id":"CHEBI:89891"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047977"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54845"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047977"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hexan-3-one + NADPH + O2 + H(+) = propyl propanoate + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54848"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:89828"},{"database":"ChEBI","id":"CHEBI:89891"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047426"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54849"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047426"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hypotaurine + NADH + O2 + H(+) = taurine + NAD(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:74111"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57853"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:507393"}],"ecNumber":"1.14.13.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047338"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:74112"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047338"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hypotaurine + NADPH + O2 + H(+) = taurine + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:69819"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:57853"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:507393"}],"ecNumber":"1.14.13.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048041"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:69820"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048041"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"octan-3-one + NADPH + O2 + H(+) = ethyl hexanoate + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54856"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:80946"},{"database":"ChEBI","id":"CHEBI:86055"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048459"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54857"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048459"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"octan-3-one + NADPH + O2 + H(+) = pentyl propanoate + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54840"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:80946"},{"database":"ChEBI","id":"CHEBI:87373"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049475"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54841"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049475"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"sulcatone + NADPH + O2 + H(+) = 4-methylpent-3-en-1-yl acetate + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54864"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16310"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:138373"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047855"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54865"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047855"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"trimethylamine + NADPH + O2 = trimethylamine N-oxide + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31979"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:15724"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:58389"}],"ecNumber":"1.14.13.148","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048088"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:31980"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048088"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004389"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004389"}],"value":"Single-pass membrane protein","id":"SL-9904"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004524"}],"value":"Microsome membrane","id":"SL-0165"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009183"}],"value":"Belongs to the FMO family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335681.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022824"}],"id":"KW-0256","category":"Cellular component","name":"Endoplasmic reticulum"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022481"}],"id":"KW-0488","category":"PTM","name":"Methylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022848"}],"id":"KW-0492","category":"Cellular component","name":"Microsome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023033"}],"id":"KW-0503","category":"Molecular function","name":"Monooxygenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335681.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335681.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000090","properties":[{"key":"ProteinId","value":"KAF9335681.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SR17","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005789","properties":[{"key":"GoTerm","value":"C:endoplasmic reticulum membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004499","properties":[{"key":"GoTerm","value":"F:N,N-dimethylaniline monooxygenase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016174","properties":[{"key":"GoTerm","value":"F:NAD(P)H oxidase H2O2-forming activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0034899","properties":[{"key":"GoTerm","value":"F:trimethylamine monooxygenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"FunFam","id":"3.50.50.60:FF:000159","properties":[{"key":"EntryName","value":"Dimethylaniline monooxygenase [N-oxide-forming]"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.50.60","properties":[{"key":"EntryName","value":"FAD/NAD(P)-binding domain"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR036188","properties":[{"key":"EntryName","value":"FAD/NAD-bd_sf"}]},{"database":"InterPro","id":"IPR000960","properties":[{"key":"EntryName","value":"Flavin_mOase"}]},{"database":"InterPro","id":"IPR020946","properties":[{"key":"EntryName","value":"Flavin_mOase-like"}]},{"database":"InterPro","id":"IPR002257","properties":[{"key":"EntryName","value":"Flavin_mOase_5"}]},{"database":"InterPro","id":"IPR050346","properties":[{"key":"EntryName","value":"FMO-like"}]},{"database":"PANTHER","id":"PTHR23023","properties":[{"key":"EntryName","value":"DIMETHYLANILINE MONOOXYGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00743","properties":[{"key":"EntryName","value":"FMO-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000332","properties":[{"key":"EntryName","value":"FMO"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00370","properties":[{"key":"EntryName","value":"FMOXYGENASE"}]},{"database":"PRINTS","id":"PR01125","properties":[{"key":"EntryName","value":"FMOXYGENASE5"}]},{"database":"SUPFAM","id":"SSF51905","properties":[{"key":"EntryName","value":"FAD/NAD(P)-binding domain"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MATTGEHSKKRVAVIGAGASGLAAIKECLDEKDSIEVVGFEQENYLGGLWRYVEVSEENPNPHSSVYKSTIINTSKELMSYSDFAIPADWPTYLPNQKVAYYFDLYAQHFNLRPYIRFETKVVEVKELKDEKNRWLVRSHSVKATQPIEIKDEIFDYVMMCSGHHWKARYPSFPGMNEDDPEPYTGIQMHSHFYREVDSYKDKNVVVVGLGNSAVDLAVELSLNQSQVYLSCRRGAWVAPRWLFGRPLDHARTRFTHMVPFFLFQLIVASLFKIAVPPHHRNLKPERLPLSSHTTINTLLPERVSTGTVKPVKNIKKMGPGKRVEFEDGTVVEDVDVIFYCTGYHVSFPVLHPDIVTDGRDGSQNNRVWTWNYMVPPRHPNMAFVGLFQPLGAIMPISEMQCRFLVRTLVGKLDPLPSEQLMDKEIEARNKYIRKRYDDAARHTIQVDYASYCDSLAKRIGCMPTYGRLVKEFGLIEGTRLWKETIFGPPSPIQYRLVGPHAWEGAREAVWGYAGKQEYASSKYLQEPKAVDRKKDLSLFKAPREQ","length":546,"molWeight":62605,"crc64":"39C0C37A92A7B133","md5":"C192AF507C947179A0788E5A85627EEA"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":13,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"uniParcId":"UPI001E1734CA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SC57","uniProtkbId":"A0A9P5SC57_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-09-13","entryVersion":10,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9324725.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"value":"NADPH-dependent diflavin oxidoreductase 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"value":"1.18.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"value":"NADPH-dependent FMN and FAD-containing oxidoreductase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9324725.1"}],"value":"NDOR1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"value":"TAH18"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9324725.1"}],"value":"BG006_000282"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"value":"NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of DRE2, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. Positively controls H(2)O(2)-induced cell death"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 oxidized [2Fe-2S]-[protein] + NADPH = 2 reduced [2Fe-2S]-[protein] + NADP(+) + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67716"},{"database":"Rhea","id":"RHEA-COMP:17327"},{"database":"Rhea","id":"RHEA-COMP:17328"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001917"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00088"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"value":"Interacts with DRE2; as part of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"value":"Relocalizes to mitochondria after H(2)O(2) exposure"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"value":"Mitochondrion","id":"SL-0173"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"value":"Belongs to the NADPH-dependent diflavin oxidoreductase NDOR1 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"value":"In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"value":"In the N-terminal section; belongs to the flavodoxin family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00088"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9324725.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"Flavodoxin-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50902"}]},{"type":"Domain","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":503,"modifier":"EXACT"}},"description":"FAD-binding FR-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51384"}]},{"type":"Region","location":{"start":{"value":481,"modifier":"EXACT"},"end":{"value":502,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":488,"modifier":"EXACT"},"end":{"value":500,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00088"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00088"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":396,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":464,"modifier":"EXACT"},"end":{"value":467,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":567,"modifier":"EXACT"},"end":{"value":568,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":573,"modifier":"EXACT"},"end":{"value":577,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":610,"modifier":"EXACT"},"end":{"value":610,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":648,"modifier":"EXACT"},"end":{"value":648,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022643"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03178"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9324725.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9324725.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010001038","properties":[{"key":"ProteinId","value":"KAF9324725.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SC57","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005739","properties":[{"key":"GoTerm","value":"C:mitochondrion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0160246","properties":[{"key":"GoTerm","value":"F:NADPH-iron-sulfur [2Fe-2S] protein oxidoreductase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016651","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on NAD(P)H"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016226","properties":[{"key":"GoTerm","value":"P:iron-sulfur cluster assembly"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.40.50.360:FF:000034","properties":[{"key":"EntryName","value":"NADPH-dependent diflavin oxidoreductase 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.360","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.990.10","properties":[{"key":"EntryName","value":"NADPH-cytochrome p450 Reductase, Chain A, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.80","properties":[{"key":"EntryName","value":"Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.30.10","properties":[{"key":"EntryName","value":"Translation factors"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03178","properties":[{"key":"EntryName","value":"NDOR1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003097","properties":[{"key":"EntryName","value":"CysJ-like_FAD-binding"}]},{"database":"InterPro","id":"IPR017927","properties":[{"key":"EntryName","value":"FAD-bd_FR_type"}]},{"database":"InterPro","id":"IPR001094","properties":[{"key":"EntryName","value":"Flavdoxin-like"}]},{"database":"InterPro","id":"IPR008254","properties":[{"key":"EntryName","value":"Flavodoxin/NO_synth"}]},{"database":"InterPro","id":"IPR001709","properties":[{"key":"EntryName","value":"Flavoprot_Pyr_Nucl_cyt_Rdtase"}]},{"database":"InterPro","id":"IPR029039","properties":[{"key":"EntryName","value":"Flavoprotein-like_sf"}]},{"database":"InterPro","id":"IPR039261","properties":[{"key":"EntryName","value":"FNR_nucleotide-bd"}]},{"database":"InterPro","id":"IPR023173","properties":[{"key":"EntryName","value":"NADPH_Cyt_P450_Rdtase_alpha"}]},{"database":"InterPro","id":"IPR028879","properties":[{"key":"EntryName","value":"NDOR1"}]},{"database":"InterPro","id":"IPR017938","properties":[{"key":"EntryName","value":"Riboflavin_synthase-like_b-brl"}]},{"database":"PANTHER","id":"PTHR19384:SF10","properties":[{"key":"EntryName","value":"NADPH-DEPENDENT DIFLAVIN OXIDOREDUCTASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19384","properties":[{"key":"EntryName","value":"NITRIC OXIDE SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00667","properties":[{"key":"EntryName","value":"FAD_binding_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00258","properties":[{"key":"EntryName","value":"Flavodoxin_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00369","properties":[{"key":"EntryName","value":"FLAVODOXIN"}]},{"database":"PRINTS","id":"PR00371","properties":[{"key":"EntryName","value":"FPNCR"}]},{"database":"SUPFAM","id":"SSF52343","properties":[{"key":"EntryName","value":"Ferredoxin reductase-like, C-terminal NADP-linked domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52218","properties":[{"key":"EntryName","value":"Flavoproteins"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63380","properties":[{"key":"EntryName","value":"Riboflavin synthase domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51384","properties":[{"key":"EntryName","value":"FAD_FR"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50902","properties":[{"key":"EntryName","value":"FLAVODOXIN_LIKE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSTINNSTAAHSGQNTAADPAQLQFNSSSPHVDPHQLDHISIHSPRRILFLYGSQTGCAQDVAENAAREARRMHFSASVSAMDDYDRSLLIREHFVVFVASTTGQGEEPDNMKKFWRFLLRKSHPSDALDHMEYTVLGLGDSSYIKFNWPAKKLYKRLLQLGAIPFYEPAYADDQHYLGIIPENVIFQNSFSLSFDQKDTTTSISKPEPTPLSADIPEPGTFLATMIENRRITNPKHSQDVRHIELLINDPLFPGYHPGDVLSMRPRNLAKDVNEFLEYSGWTSIADDPLTVVENLADHQLPKHISHRQTLRSLFTNYLNVFTTPRTSFFQLLIHFTPNEDEKDKLREFVSPAGQDDLYSYSHRMRRTIFEVMQDFKDVRIPLNYILDVFPVIMPRSFSIASAPLVSVQEQHQSGRLNGCVSPAVATSNGQLDAGNIEGELQWKVDLCVAIVHYKTKLWKWRVGICTKWLKSLHAANDPGLPIEGGENTASETETPSGGPSQFMVRVQRGTLKLPKDPSTPLICIGPGANKNVLFFGCRKRAMDYHYQGEWEQLEREGSLRVFAACSRDQDDKVYVQHLIEAHGALVWKYLHEEKGIILLSGSSNRMPADVTRALQRVISTYGNMSIEQAHDYLTKVEKEGRFQQECWA","length":649,"molWeight":73505,"crc64":"E882F53BE3EDAE61","md5":"78EA71FCC381472DA17322D909048DE6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":3,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":1,"Compositional bias":1,"Binding site":12},"uniParcId":"UPI001D3E3F6B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SHH7","uniProtkbId":"A0A9P5SHH7_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-09-13","entryVersion":14,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9327797.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012429"}],"value":"protein kinase C"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012429"}],"value":"2.7.11.13"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9327797.1"}],"value":"PKC1_2"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9327797.1"}],"value":"BG006_008938"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00089"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005490"}],"value":"Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"value":"Belongs to the protein kinase superfamily. Ser/Thr protein kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9327797.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"C2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50004"}]},{"type":"Domain","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":395,"modifier":"EXACT"}},"description":"Fork-head","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50039"}]},{"type":"Domain","location":{"start":{"value":415,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"Phorbol-ester/DAG-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50081"}]},{"type":"Domain","location":{"start":{"value":481,"modifier":"EXACT"},"end":{"value":530,"modifier":"EXACT"}},"description":"Phorbol-ester/DAG-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50081"}]},{"type":"Domain","location":{"start":{"value":786,"modifier":"EXACT"},"end":{"value":1047,"modifier":"EXACT"}},"description":"Protein kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50011"}]},{"type":"Domain","location":{"start":{"value":1048,"modifier":"EXACT"},"end":{"value":1116,"modifier":"EXACT"}},"description":"AGC-kinase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51285"}]},{"type":"DNA binding","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":395,"modifier":"EXACT"}},"description":"Fork-head","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00089"}]},{"type":"Zinc finger","location":{"start":{"value":415,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"Phorbol-ester/DAG-type","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}]},{"type":"Zinc finger","location":{"start":{"value":481,"modifier":"EXACT"},"end":{"value":530,"modifier":"EXACT"}},"description":"Phorbol-ester/DAG-type","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}]},{"type":"Region","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":547,"modifier":"EXACT"},"end":{"value":575,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":612,"modifier":"EXACT"},"end":{"value":641,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":699,"modifier":"EXACT"},"end":{"value":755,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Compositional bias","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":612,"modifier":"EXACT"},"end":{"value":633,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":721,"modifier":"EXACT"},"end":{"value":743,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":913,"modifier":"EXACT"},"end":{"value":913,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]},{"type":"Binding site","location":{"start":{"value":825,"modifier":"EXACT"},"end":{"value":825,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Modified residue","location":{"start":{"value":1089,"modifier":"EXACT"},"end":{"value":1089,"modifier":"EXACT"}},"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}]},{"type":"Modified residue","location":{"start":{"value":1107,"modifier":"EXACT"},"end":{"value":1107,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}]},{"type":"Modified residue","location":{"start":{"value":1108,"modifier":"EXACT"},"end":{"value":1108,"modifier":"EXACT"}},"description":"Phosphotyrosine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00089"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00089"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022527"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"id":"KW-0723","category":"Molecular function","name":"Serine/threonine-protein kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022771"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9327797.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9327797.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000627","properties":[{"key":"ProteinId","value":"KAF9327797.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SHH7","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019992","properties":[{"key":"GoTerm","value":"F:diacylglycerol binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003700","properties":[{"key":"GoTerm","value":"F:DNA-binding transcription factor activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004674","properties":[{"key":"GoTerm","value":"F:protein serine/threonine kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043565","properties":[{"key":"GoTerm","value":"F:sequence-specific DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd20822","properties":[{"key":"EntryName","value":"C1_ScPKC1-like_rpt1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd20823","properties":[{"key":"EntryName","value":"C1_ScPKC1-like_rpt2"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd05570","properties":[{"key":"EntryName","value":"STKc_PKC"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.200.20:FF:000042","properties":[{"key":"EntryName","value":"Aurora kinase A"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.510.10:FF:000210","properties":[{"key":"EntryName","value":"Non-specific serine/threonine protein kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.60.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"2.60.40.150","properties":[{"key":"EntryName","value":"C2 domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.200.20","properties":[{"key":"EntryName","value":"Phosphorylase Kinase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.510.10","properties":[{"key":"EntryName","value":"Transferase(Phosphotransferase) domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000961","properties":[{"key":"EntryName","value":"AGC-kinase_C"}]},{"database":"InterPro","id":"IPR046349","properties":[{"key":"EntryName","value":"C1-like_sf"}]},{"database":"InterPro","id":"IPR000008","properties":[{"key":"EntryName","value":"C2_dom"}]},{"database":"InterPro","id":"IPR035892","properties":[{"key":"EntryName","value":"C2_domain_sf"}]},{"database":"InterPro","id":"IPR001766","properties":[{"key":"EntryName","value":"Fork_head_dom"}]},{"database":"InterPro","id":"IPR011009","properties":[{"key":"EntryName","value":"Kinase-like_dom_sf"}]},{"database":"InterPro","id":"IPR002219","properties":[{"key":"EntryName","value":"PKC_DAG/PE"}]},{"database":"InterPro","id":"IPR017892","properties":[{"key":"EntryName","value":"Pkinase_C"}]},{"database":"InterPro","id":"IPR000719","properties":[{"key":"EntryName","value":"Prot_kinase_dom"}]},{"database":"InterPro","id":"IPR017441","properties":[{"key":"EntryName","value":"Protein_kinase_ATP_BS"}]},{"database":"InterPro","id":"IPR008271","properties":[{"key":"EntryName","value":"Ser/Thr_kinase_AS"}]},{"database":"PANTHER","id":"PTHR24351","properties":[{"key":"EntryName","value":"RIBOSOMAL PROTEIN S6 KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00130","properties":[{"key":"EntryName","value":"C1_1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF00168","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00069","properties":[{"key":"EntryName","value":"Pkinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00433","properties":[{"key":"EntryName","value":"Pkinase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00109","properties":[{"key":"EntryName","value":"C1"},{"key":"MatchStatus","value":"2"}]},{"database":"SMART","id":"SM00133","properties":[{"key":"EntryName","value":"S_TK_X"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00220","properties":[{"key":"EntryName","value":"S_TKc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF49562","properties":[{"key":"EntryName","value":"C2 domain (Calcium/lipid-binding domain, CaLB)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF57889","properties":[{"key":"EntryName","value":"Cysteine-rich domain"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF56112","properties":[{"key":"EntryName","value":"Protein kinase-like (PK-like)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51285","properties":[{"key":"EntryName","value":"AGC_KINASE_CTER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50004","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50039","properties":[{"key":"EntryName","value":"FORK_HEAD_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00107","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_ATP"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50011","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_DOM"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00108","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_ST"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00479","properties":[{"key":"EntryName","value":"ZF_DAG_PE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50081","properties":[{"key":"EntryName","value":"ZF_DAG_PE_2"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MSDDQRLEDLRNRLQREKDIKNATLKLRGIQKSEHGIAACDFSLEESDQRISYFQNEVDKLQLKIYENSPKVARTHIPITLPSFSSGPPSVPGSSSTHTAYSPDSRTLTPGRKPSSSSSHYPDDFIFQRPLSTVDLLKAPTPITTKKVTYKLRELAYKLDIEKKVKAASERLELLGMSAKDGNAESSERVVLLKRALQKYQGLYIPGQEDDITTAPGAALRRPMTGVLHVRISGIKHQNHAPIRGSRPAESMAVIKIDGSPRAKTRMARTGPNGIRWNEEFEVPVTKASEIEIAVYDKPDHIAIPIGMFWLKISDLVEDLRRKKQVADNDAAWAAANVQDLTTRTPFIRPGTGPLGDNPINGVEGIESWWDLEPVGQISLKFNFVKDVAIRKRPSKLGRQGAVRKRKDEIREIQGHKFVSQKFFQIMCCALCAELFTGRGAQCEDCKFTCHQKCAEKVFIKCISSKGVEDPDEAKLNHRIPHRFETFTNLSPTWCSHCGHMLTFGRRHKKCTECPVVAHDGCSDLVPNHCGMPAETANKLMEEIRRRNQKTRFNQTPVRPTKSYESLPKVEPQRPTYQGIYSEQPRLPARPDSRPQQANLHGLDYNQRLQQQMEQMQIQQQMHGQYEYEQQQQHHQRKMEQQRLLEQQRLLEQQQQIQLQQQKQQLQQQIEQQQLRQQQLQLQLQQQQQQQHQQQQAQAQSQQYQQVGSERPQRPVPEIPLEDKFRNEQARLEQLRQEQEKKNRTPPVTPHMDQRPLVMPTAHMPTLKIVNKQTAKPMRKYGLTDFHFLAVLGKGNFGKVMLAEDKKKAGELFAIKVLKKESIVKQDEIESARSEKRIYQVANKERHPFLTTLHSCFQTDTRLYFVMEYVRGGDLMMHIQKDKRFGDHRAKFYGCQVLLALQYFHQNNIVYRDLKLDNILLTTDGHIKIADYGLCKENMPFGVTTRTICGTPEFMAPEILEEQPYDRAVDWWAFGVLMYEMLLGCAPFSGEEEDDIYDSILEDEPMYPQGFGRHEQALLQSLLVKVPSLRLGAGPSDAEEIMAHAYFRNVNFDDVYHKRIRPPFLPKISSDRDVSNFDSEFTSEAPGETPTDYRLDNVEQDMFKGFSYASPWALAS","length":1116,"molWeight":128250,"crc64":"6D5F4F4A78CFFB1E","md5":"FF6C4815396FAFC0069D372390B4D59A"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":6,"DNA binding":1,"Zinc finger":2,"Region":4,"Coiled coil":1,"Compositional bias":4,"Active site":1,"Binding site":1,"Modified residue":3},"uniParcId":"UPI001D4D6F50"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SHZ4","uniProtkbId":"A0A9P5SHZ4_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-09-13","entryVersion":10,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329800.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"ATP-dependent 6-phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"ATP-PFK"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Phosphofructokinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"2.7.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Phosphohexokinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329800.1"}],"value":"PFK1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329800.1"}],"value":"BG006_007171"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16109"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:32966"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048070"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000533"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000533"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000533"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade \"E\" sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329800.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":495,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Domain","location":{"start":{"value":575,"modifier":"EXACT"},"end":{"value":863,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":561,"modifier":"EXACT"}},"description":"N-terminal catalytic PFK domain 1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}]},{"type":"Region","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":575,"modifier":"EXACT"},"end":{"value":944,"modifier":"EXACT"}},"description":"C-terminal regulatory PFK domain 2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}]},{"type":"Active site","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}]},{"type":"Binding site","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":371,"modifier":"EXACT"},"end":{"value":371,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":435,"modifier":"EXACT"},"end":{"value":435,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":463,"modifier":"EXACT"},"end":{"value":463,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":469,"modifier":"EXACT"},"end":{"value":472,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":644,"modifier":"EXACT"},"end":{"value":644,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":701,"modifier":"EXACT"},"end":{"value":705,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":739,"modifier":"EXACT"},"end":{"value":739,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":806,"modifier":"EXACT"},"end":{"value":806,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":832,"modifier":"EXACT"},"end":{"value":832,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":838,"modifier":"EXACT"},"end":{"value":841,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":922,"modifier":"EXACT"},"end":{"value":922,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329800.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329800.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000446","properties":[{"key":"ProteinId","value":"KAF9329800.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SHZ4","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005945","properties":[{"key":"GoTerm","value":"C:6-phosphofructokinase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005739","properties":[{"key":"GoTerm","value":"C:mitochondrion"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003872","properties":[{"key":"GoTerm","value":"F:6-phosphofructokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016208","properties":[{"key":"GoTerm","value":"F:AMP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0070095","properties":[{"key":"GoTerm","value":"F:fructose-6-phosphate binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0048029","properties":[{"key":"GoTerm","value":"F:monosaccharide binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0061621","properties":[{"key":"GoTerm","value":"P:canonical glycolysis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030388","properties":[{"key":"GoTerm","value":"P:fructose 1,6-bisphosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006002","properties":[{"key":"GoTerm","value":"P:fructose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.40.50.460:FF:000007","properties":[{"key":"EntryName","value":"ATP-dependent 6-phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.460:FF:000008","properties":[{"key":"EntryName","value":"ATP-dependent 6-phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.450","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.10.180.10","properties":[{"key":"EntryName","value":"2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.460","properties":[{"key":"EntryName","value":"Phosphofructokinase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_03184","properties":[{"key":"EntryName","value":"Phosphofructokinase_I_E"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR009161","properties":[{"key":"EntryName","value":"6-Pfructokinase_euk"}]},{"database":"InterPro","id":"IPR022953","properties":[{"key":"EntryName","value":"ATP_PFK"}]},{"database":"InterPro","id":"IPR029068","properties":[{"key":"EntryName","value":"Glyas_Bleomycin-R_OHBP_Dase"}]},{"database":"InterPro","id":"IPR015912","properties":[{"key":"EntryName","value":"Phosphofructokinase_CS"}]},{"database":"InterPro","id":"IPR000023","properties":[{"key":"EntryName","value":"Phosphofructokinase_dom"}]},{"database":"InterPro","id":"IPR035966","properties":[{"key":"EntryName","value":"PKF_sf"}]},{"database":"NCBIfam","id":"TIGR02478","properties":[{"key":"EntryName","value":"6PF1K_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697:SF4","properties":[{"key":"EntryName","value":"ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00365","properties":[{"key":"EntryName","value":"PFK"},{"key":"MatchStatus","value":"2"}]},{"database":"PIRSF","id":"PIRSF000533","properties":[{"key":"EntryName","value":"ATP_PFK_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00476","properties":[{"key":"EntryName","value":"PHFRCTKINASE"}]},{"database":"SUPFAM","id":"SSF53784","properties":[{"key":"EntryName","value":"Phosphofructokinase"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00433","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MADQQHHTISLDHIANLILTAPTLETYHAAVSWFEELGFKAIMTETSVETTATWLQLFSNAATIHDVSLKIVHSPSGQLKLATSIKMDWRSVPALATITTNSLQDLEELFIASRWAYQRYAIPAKDASDFSEFAAIYTHDPMNNLLIFTNKPNPFETTIKRSKTIPSAQPDLDAEPASTDTTGRKRKIAILTSGGDAPGMNAAVRGVVRAAISRGCDAYAVHEGYQGLVDGGKMIKKMGWDDVQGYLSVGGTVIGTARCKAFRERPGRLLAAKNLVKEGIDALIVCGGDGSLTGADLFRSEWPSLLEELISTGDLTVEEAEPFTHLNIVGLVGSIDNDMSSTDITIGAVTCLHRICESIDSISSTASSHSRAFVVEVMGRHCGWLALMAGIATGADFIFIPERPPSGEDWEDEMCAEIKRHRDLGKRKTIVIVSEGAIDSNLKPITAKDMMDLLTDRLHLDTRMTILGHVQRGGSPSAFDRNLATMQGVEAVEAVLASTPDVPSAMIGMNENKISRTDLMKAVALTGEVAKAIQRKDFVGAMDLRDPAFNQQYEQFLATTLASNDEIKKNVQPLRIGIINVGAPAGGMNAAVRAAVRYARNRGHTPFAILNGFPGLIAGQVKEMQWMDVDGWMAHGGSELGTNRDQPSLDLGMVSYQLQKFNIQSLMLIGGFEAYTACLEMYNARNVYPAFCMPMVHIPATISNNVPGTEYSLGCDTSLNAIMTACDAIKQSATASRKRVFVVEVHGGKSGFLAVMSGLTVGATSVYIPEEGISLARLQKDVQHLCKRYSEDAEGKSQGRIIIRCEAASKTYTTDIVASIIKEEGHQQFDARTAILGHIQQGNSPSPLDRIRAMRLAVCSIDFLEEHTSDISSSSSTHSSASSGPAVYNKDPESIAVAGILGSNVSFTSVESLLKDTDMKNRKPKQSWWMDYRRTGILLARSKH","length":944,"molWeight":102443,"crc64":"E12A77BE71446079","md5":"FC8461DBA297515618873F854B1BAA30"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":3,"Active site":1,"Binding site":17},"uniParcId":"UPI001D6EC97E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SJ55","uniProtkbId":"A0A9P5SJ55_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-09-13","entryVersion":13,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9328734.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"4: Predicted","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044985"}],"value":"Lysosomal dipeptide transporter MFSD1"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045018"}],"value":"Major facilitator superfamily domain-containing protein 1"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9328734.1"}],"value":"BG006_008127"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045709"}],"value":"Lysosomal dipeptide uniporter that selectively exports lysine, arginine or histidine-containing dipeptides with a net positive charge from the lysosome lumen into the cytosol. Could play a role in a specific type of protein O-glycosylation indirectly regulating macrophages migration and tissue invasion. Also essential for liver homeostasis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alanyl-L-lysine(out) = L-alanyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79415"},{"database":"ChEBI","id":"CHEBI:192470"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044919"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-arginine(out) = L-alpha-aminoacyl-L-arginine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79367"},{"database":"ChEBI","id":"CHEBI:229968"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044881"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-histidine(out) = L-alpha-aminoacyl-L-histidine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79375"},{"database":"ChEBI","id":"CHEBI:229967"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044884"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-lysine(out) = L-alpha-aminoacyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79383"},{"database":"ChEBI","id":"CHEBI:229966"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044893"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-L-alpha-amino acid(out) = L-arginyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79371"},{"database":"ChEBI","id":"CHEBI:84315"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044899"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-glycine(out) = L-arginyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79391"},{"database":"ChEBI","id":"CHEBI:229955"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044903"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartyl-L-lysine(out) = L-aspartyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79411"},{"database":"ChEBI","id":"CHEBI:229953"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044898"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-L-alpha-amino acid(out) = L-histidyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79379"},{"database":"ChEBI","id":"CHEBI:229964"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044912"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-glycine(out) = L-histidyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79395"},{"database":"ChEBI","id":"CHEBI:229957"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044878"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alanine(out) = L-lysyl-L-alanine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79399"},{"database":"ChEBI","id":"CHEBI:229954"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044876"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alpha-amino acid(out) = L-lysyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79387"},{"database":"ChEBI","id":"CHEBI:229965"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044891"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-lysine(out) = L-lysyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79403"},{"database":"ChEBI","id":"CHEBI:229956"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044900"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-glycine(out) = L-lysyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79407"},{"database":"ChEBI","id":"CHEBI:191202"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044924"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00046376"}],"value":"Homodimer. Interacts with lysosomal protein GLMP (via lumenal domain); the interaction starts while both proteins are still in the endoplasmic reticulum and is required for stabilization of MFSD1 in lysosomes but has no direct effect on its targeting to lysosomes or transporter activity"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004127"}],"value":"Endomembrane system","id":"SL-0147"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004127"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9328734.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":383,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":412,"modifier":"EXACT"},"end":{"value":431,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":437,"modifier":"EXACT"},"end":{"value":458,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":470,"modifier":"EXACT"},"end":{"value":493,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":505,"modifier":"EXACT"},"end":{"value":524,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":529,"modifier":"EXACT"}},"description":"Major facilitator superfamily (MFS) profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50850"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":553,"modifier":"EXACT"},"end":{"value":589,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":630,"modifier":"EXACT"},"end":{"value":653,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"Pro residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":553,"modifier":"EXACT"},"end":{"value":580,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023228"}],"id":"KW-0458","category":"Cellular component","name":"Lysosome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9328734.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9328734.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000537","properties":[{"key":"ProteinId","value":"KAF9328734.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SJ55","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0012505","properties":[{"key":"GoTerm","value":"C:endomembrane system"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0022857","properties":[{"key":"GoTerm","value":"F:transmembrane transporter activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.20.1250.20","properties":[{"key":"EntryName","value":"MFS general substrate transporter like domains"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR011701","properties":[{"key":"EntryName","value":"MFS"}]},{"database":"InterPro","id":"IPR020846","properties":[{"key":"EntryName","value":"MFS_dom"}]},{"database":"InterPro","id":"IPR036259","properties":[{"key":"EntryName","value":"MFS_trans_sf"}]},{"database":"InterPro","id":"IPR052187","properties":[{"key":"EntryName","value":"MFSD1"}]},{"database":"PANTHER","id":"PTHR23512","properties":[{"key":"EntryName","value":"MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23512:SF3","properties":[{"key":"EntryName","value":"MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07690","properties":[{"key":"EntryName","value":"MFS_1"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF103473","properties":[{"key":"EntryName","value":"MFS general substrate transporter"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50850","properties":[{"key":"EntryName","value":"MFS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNYSANEQTSLVGPKASDTRRGYYGNQLRRPPSPTSSRDPAFVRPSSPRPFNPPQPLQQQLDRAQQRHDQAHAITSRHWVVLALACLLLFGNYYCYDIPAALNVQLEEWMGTSYEVHQYQLNLLYSAYSLPNIILPLAGGYLIDRLSASRMLILFSLCICLGQGVFAVGLSFKSITVMVLGRFIFGIGGECLEVAQAKITTDWFKSRWLGLALGLNLSSARIGTALNDNLSPAIATTTGGVLAASWTGFGVCVLSLGCGIALAHLDGPASRKQSGVRVDAKDRKQEAISSPKDNIIGRQSLNVSSDSTMTLSSEAMEEQEEIEKENEMAEDDQMLYSEIFTLQTNFWILCLCCILLYGAAVPFNHISSDFLQKKWYTNNPTRAGTVMSIPDLVSSVGSPLCGYLIDRFGHRARYIPLSALLLIWAHTQLGFTQINPVLAMLVLGLAYSLFASALWPCIPFLVEDHQLGTAYGLVTIALNLSLTVFPMAVAAILHLTDGSYQWVEGLFIALAGMGFVLSIVLNILDRRQGGHLQMAEGVHAPLLDDISGYDHDPRRFSGDSRRFSQESRRYSREGYMSDRDMGEEDGMVTTKPVGEGIITIIPHRRRHSMAGFAGHLERARLNNYAQHVQTSPELNGIPGSFPNQPTYLSERHQ","length":653,"molWeight":72087,"crc64":"FFA95D481AC69EEB","md5":"9511EE900DA807E335AB045F54B9E3DE"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":13,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":10,"Domain":1,"Region":3,"Compositional bias":3},"uniParcId":"UPI001DEAAFA4"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SJR7","uniProtkbId":"A0A9P5SJR7_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-09-13","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9331538.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Phosphatidyl-N-methylethanolamine N-methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"2.1.1.71"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Phospholipid methyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"PLMT"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9331538.1"}],"value":"OPI3"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9331538.1"}],"value":"BG006_005589"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00931"}],"value":"Catalyzes three sequential methylation reactions of phosphatidylethanolamine (PE) by AdoMet, thereby producing phosphatidylcholine (PC)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phosphocholine + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32739"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57643"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:64572"}],"ecNumber":"2.1.1.71","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051252"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32735"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:64572"},{"database":"ChEBI","id":"CHEBI:64573"}],"ecNumber":"2.1.1.71","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052459"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00931"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11164"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:64573"},{"database":"ChEBI","id":"CHEBI:64612"}],"ecNumber":"2.1.1.17","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00931"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005189"}],"value":"Lipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004969"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00931"}],"value":"Phospholipid metabolism; phosphatidylcholine biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Mitochondrion membrane","id":"SL-0171"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00931"}],"value":"Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9331538.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Topological domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Transmembrane","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Intramembrane","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Topological domain","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Transmembrane","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Topological domain","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Transmembrane","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Topological domain","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Transmembrane","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Topological domain","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Domain","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"Phospholipid methyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04191"}]},{"type":"Region","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022824"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0256","category":"Cellular component","name":"Endoplasmic reticulum"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0594","category":"Biological process","name":"Phospholipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023264"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-1208","category":"Biological process","name":"Phospholipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9331538.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9331538.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000316","properties":[{"key":"ProteinId","value":"KAF9331538.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SJR7","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005789","properties":[{"key":"GoTerm","value":"C:endoplasmic reticulum membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0031966","properties":[{"key":"GoTerm","value":"C:mitochondrial membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000773","properties":[{"key":"GoTerm","value":"F:phosphatidyl-N-methylethanolamine N-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004608","properties":[{"key":"GoTerm","value":"F:phosphatidylethanolamine N-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006656","properties":[{"key":"GoTerm","value":"P:phosphatidylcholine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.20.120.1630:FF:000005","properties":[{"key":"EntryName","value":"Phosphatidylethanolamine N-methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.120.1630","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03216","properties":[{"key":"EntryName","value":"PLMT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR024960","properties":[{"key":"EntryName","value":"PEMT/MFAP"}]},{"database":"InterPro","id":"IPR007318","properties":[{"key":"EntryName","value":"Phopholipid_MeTrfase"}]},{"database":"PANTHER","id":"PTHR15458","properties":[{"key":"EntryName","value":"PHOSPHATIDYLETHANOLAMINE N-METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR15458:SF5","properties":[{"key":"EntryName","value":"PHOSPHATIDYLETHANOLAMINE N-METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04191","properties":[{"key":"EntryName","value":"PEMT"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005444","properties":[{"key":"EntryName","value":"PEMT"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51599","properties":[{"key":"EntryName","value":"SAM_PEMT_PEM2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGIMSIRQCYNDERLSVDWSDYRIIICVACIIFNPTFWNIVARKEYRSKFITRMFNGNGLYGCYALAATIFILGLVRDAVFKWAIDGQPKAQCMEEPLIQAMAYILFGVGNILVLSSMYVLGVTGTYLGDYFGILMEERVTSFPFSVNENPMYNGTVLIFLGTAMWSLSPAGIYLSLIVHFVYRIALKFEGPFTTQIYIKRDSDRAAASKTSVPTRAAKKSGRNTKKDL","length":229,"molWeight":25842,"crc64":"9A503C756679C8E6","md5":"5C8D773AC252919ECC183D1ABA7059B5"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":3,"PATHWAY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Topological domain":5,"Transmembrane":4,"Intramembrane":1,"Domain":1,"Region":1,"Compositional bias":1,"Binding site":2},"uniParcId":"UPI001D723C7F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SK55","uniProtkbId":"A0A9P5SK55_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-09-13","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9331156.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00067568"}],"value":"Folic acid synthesis protein FOL1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012458"}],"value":"2.5.1.15"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013253"}],"value":"2.7.6.3"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013043"}],"value":"4.1.2.25"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00068111"}],"value":"Folic acid synthesis protein fol1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9331156.1"}],"value":"FOL1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9331156.1"}],"value":"BG006_005971"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00058009"}],"value":"Catalyzes three sequential steps of tetrahydrofolate biosynthesis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate = 7,8-dihydropteroate + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19949"},{"database":"ChEBI","id":"CHEBI:17836"},{"database":"ChEBI","id":"CHEBI:17839"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:72950"}],"ecNumber":"2.5.1.15","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000012"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11412"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:44841"},{"database":"ChEBI","id":"CHEBI:72950"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"2.7.6.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000198"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10540"},{"database":"ChEBI","id":"CHEBI:17001"},{"database":"ChEBI","id":"CHEBI:17071"},{"database":"ChEBI","id":"CHEBI:44841"}],"ecNumber":"4.1.2.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001353"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005013"}],"value":"Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005051"}],"value":"Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004763"}],"value":"Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009951"}],"value":"In the C-terminal section; belongs to the DHPS family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009640"}],"value":"In the N-terminal section; belongs to the DHNA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061548"}],"value":"In the central section; belongs to the HPPK family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9331156.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":499,"modifier":"EXACT"},"end":{"value":763,"modifier":"EXACT"}},"description":"Pterin-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50972"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022909"}],"id":"KW-0289","category":"Biological process","name":"Folate biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9331156.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9331156.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000344","properties":[{"key":"ProteinId","value":"KAF9331156.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SK55","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005740","properties":[{"key":"GoTerm","value":"C:mitochondrial envelope"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003848","properties":[{"key":"GoTerm","value":"F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004150","properties":[{"key":"GoTerm","value":"F:dihydroneopterin aldolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004156","properties":[{"key":"GoTerm","value":"F:dihydropteroate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046654","properties":[{"key":"GoTerm","value":"P:tetrahydrofolate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00534","properties":[{"key":"EntryName","value":"DHNA_DHNTPE"},{"key":"MatchStatus","value":"2"}]},{"database":"CDD","id":"cd00739","properties":[{"key":"EntryName","value":"DHPS"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00483","properties":[{"key":"EntryName","value":"HPPK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.20:FF:000006","properties":[{"key":"EntryName","value":"Dihydropteroate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1130.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.70.560","properties":[{"key":"EntryName","value":"7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.20","properties":[{"key":"EntryName","value":"Dihydropteroate synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR045031","properties":[{"key":"EntryName","value":"DHP_synth-like"}]},{"database":"InterPro","id":"IPR006390","properties":[{"key":"EntryName","value":"DHP_synth_dom"}]},{"database":"InterPro","id":"IPR011005","properties":[{"key":"EntryName","value":"Dihydropteroate_synth-like_sf"}]},{"database":"InterPro","id":"IPR006157","properties":[{"key":"EntryName","value":"FolB_dom"}]},{"database":"InterPro","id":"IPR043133","properties":[{"key":"EntryName","value":"GTP-CH-I_C/QueF"}]},{"database":"InterPro","id":"IPR000550","properties":[{"key":"EntryName","value":"Hppk"}]},{"database":"InterPro","id":"IPR035907","properties":[{"key":"EntryName","value":"Hppk_sf"}]},{"database":"InterPro","id":"IPR000489","properties":[{"key":"EntryName","value":"Pterin-binding_dom"}]},{"database":"NCBIfam","id":"TIGR01496","properties":[{"key":"EntryName","value":"DHPS"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00526","properties":[{"key":"EntryName","value":"folB_dom"},{"key":"MatchStatus","value":"2"}]},{"database":"NCBIfam","id":"TIGR01498","properties":[{"key":"EntryName","value":"folK"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20941","properties":[{"key":"EntryName","value":"FOLATE SYNTHESIS PROTEINS"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20941:SF1","properties":[{"key":"EntryName","value":"FOLIC ACID SYNTHESIS PROTEIN FOL1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02152","properties":[{"key":"EntryName","value":"FolB"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF01288","properties":[{"key":"EntryName","value":"HPPK"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00809","properties":[{"key":"EntryName","value":"Pterin_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00905","properties":[{"key":"EntryName","value":"FolB"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF55083","properties":[{"key":"EntryName","value":"6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51717","properties":[{"key":"EntryName","value":"Dihydropteroate synthetase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55620","properties":[{"key":"EntryName","value":"Tetrahydrobiopterin biosynthesis enzymes-like"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00792","properties":[{"key":"EntryName","value":"DHPS_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00793","properties":[{"key":"EntryName","value":"DHPS_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00794","properties":[{"key":"EntryName","value":"HPPK"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50972","properties":[{"key":"EntryName","value":"PTERIN_BINDING"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDHQQQHPKGAASDAVELPMHDKICIRDLTVRNIIGVDAWERSKRQPIIINLVVYTSVSQAGDTDHLPYSIHYGILCKTVEAHSEKTEFRSVEALADSIARVVITKCHAPKITVRIDKPRALLHAASAGVEITRQKSDYTAEQLAGTVPCPLKFNHQDVIFVKDLRLSCIIGVNPWEREEEQVVVLNLQIYPGYDDSNDRKADYVSSTHNYRTIVRTITKYIEASSYKTVEAFVTSVARIAIEKCHVSKITVKMEKPSAIVFAGSAGVEITRDRAFFANAAANKTHTRGVSSVSSIALNPHHLRDIPRRGPVPAHLTHESFLALGSNLGDSAANLSNALKMLEQDGHVRVVDTSFMYETPPMYVTDQPPFLNAACKIKTDLAPLDLLKKLKEIEAEMGRDFNTIRNGPRPIDLDILLYDSIEYKDDTLTIPHIAMQDREFVLRPLCDIAKDVEHPKLYRHISQLLSQLLLKQEENKIDDGAIHKSVPLRGKIYHWDAKTLIMGILNTTPDSFSDGGNYSTTESAALRAQQLVEDGADIIDIGGMSTRPNSEEISEEEELNRVVPVIKLLRSRGFEAPISVDTFRASVADKAIEAGADLINDVSAGRRDPAMYGVMAKWNVPVCLMHMRGDSKTMMSQTDYGAKNDVVGAIARDLHKSVQRAIAAGVHRWNIIVDPGVGFAKDSEQSLQVLRRLPELIHSESSQLIGYPCLVGPSRKAFIGQLTQQADATKRTWGTAAACTASVAGGASIVRVHDVKEIRDVIKVSDAIWRVKA","length":773,"molWeight":85496,"crc64":"53D668408D4F5633","md5":"088DE910C3D8CD81D87FA827346257EB"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":3,"SIMILARITY":3,"CAUTION":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI001DD31FE7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SKK6","uniProtkbId":"A0A9P5SKK6_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-09-13","entryVersion":14,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329756.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012429"}],"value":"protein kinase C"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012429"}],"value":"2.7.11.13"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329756.1"}],"value":"PKC1_1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329756.1"}],"value":"BG006_007198"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047470"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047272"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00089"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005490"}],"value":"Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"value":"Belongs to the protein kinase superfamily. Ser/Thr protein kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329756.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"C2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50004"}]},{"type":"Domain","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":394,"modifier":"EXACT"}},"description":"Fork-head","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50039"}]},{"type":"Domain","location":{"start":{"value":414,"modifier":"EXACT"},"end":{"value":461,"modifier":"EXACT"}},"description":"Phorbol-ester/DAG-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50081"}]},{"type":"Domain","location":{"start":{"value":480,"modifier":"EXACT"},"end":{"value":529,"modifier":"EXACT"}},"description":"Phorbol-ester/DAG-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50081"}]},{"type":"Domain","location":{"start":{"value":748,"modifier":"EXACT"},"end":{"value":1008,"modifier":"EXACT"}},"description":"Protein kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50011"}]},{"type":"Domain","location":{"start":{"value":1009,"modifier":"EXACT"},"end":{"value":1076,"modifier":"EXACT"}},"description":"AGC-kinase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51285"}]},{"type":"DNA binding","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":394,"modifier":"EXACT"}},"description":"Fork-head","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00089"}]},{"type":"Zinc finger","location":{"start":{"value":414,"modifier":"EXACT"},"end":{"value":461,"modifier":"EXACT"}},"description":"Phorbol-ester/DAG-type","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}]},{"type":"Zinc finger","location":{"start":{"value":480,"modifier":"EXACT"},"end":{"value":529,"modifier":"EXACT"}},"description":"Phorbol-ester/DAG-type","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}]},{"type":"Region","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":589,"modifier":"EXACT"},"end":{"value":709,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Active site","location":{"start":{"value":874,"modifier":"EXACT"},"end":{"value":874,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]},{"type":"Binding site","location":{"start":{"value":786,"modifier":"EXACT"},"end":{"value":786,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Modified residue","location":{"start":{"value":1050,"modifier":"EXACT"},"end":{"value":1050,"modifier":"EXACT"}},"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}]},{"type":"Modified residue","location":{"start":{"value":1068,"modifier":"EXACT"},"end":{"value":1068,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}]},{"type":"Modified residue","location":{"start":{"value":1069,"modifier":"EXACT"},"end":{"value":1069,"modifier":"EXACT"}},"description":"Phosphotyrosine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00089"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00089"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022527"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"id":"KW-0723","category":"Molecular function","name":"Serine/threonine-protein kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022771"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329756.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329756.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000449","properties":[{"key":"ProteinId","value":"KAF9329756.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SKK6","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019992","properties":[{"key":"GoTerm","value":"F:diacylglycerol binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004697","properties":[{"key":"GoTerm","value":"F:diacylglycerol-dependent serine/threonine kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0003700","properties":[{"key":"GoTerm","value":"F:DNA-binding transcription factor activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0043565","properties":[{"key":"GoTerm","value":"F:sequence-specific DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0007165","properties":[{"key":"GoTerm","value":"P:signal transduction"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd20822","properties":[{"key":"EntryName","value":"C1_ScPKC1-like_rpt1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd20823","properties":[{"key":"EntryName","value":"C1_ScPKC1-like_rpt2"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd05570","properties":[{"key":"EntryName","value":"STKc_PKC"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.200.20:FF:000042","properties":[{"key":"EntryName","value":"Aurora kinase A"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.510.10:FF:000210","properties":[{"key":"EntryName","value":"Non-specific serine/threonine protein kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.60.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"2.60.40.150","properties":[{"key":"EntryName","value":"C2 domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.200.20","properties":[{"key":"EntryName","value":"Phosphorylase Kinase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.510.10","properties":[{"key":"EntryName","value":"Transferase(Phosphotransferase) domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000961","properties":[{"key":"EntryName","value":"AGC-kinase_C"}]},{"database":"InterPro","id":"IPR046349","properties":[{"key":"EntryName","value":"C1-like_sf"}]},{"database":"InterPro","id":"IPR000008","properties":[{"key":"EntryName","value":"C2_dom"}]},{"database":"InterPro","id":"IPR035892","properties":[{"key":"EntryName","value":"C2_domain_sf"}]},{"database":"InterPro","id":"IPR001766","properties":[{"key":"EntryName","value":"Fork_head_dom"}]},{"database":"InterPro","id":"IPR011072","properties":[{"key":"EntryName","value":"HR1_rho-bd"}]},{"database":"InterPro","id":"IPR036274","properties":[{"key":"EntryName","value":"HR1_rpt_sf"}]},{"database":"InterPro","id":"IPR011009","properties":[{"key":"EntryName","value":"Kinase-like_dom_sf"}]},{"database":"InterPro","id":"IPR002219","properties":[{"key":"EntryName","value":"PKC_DAG/PE"}]},{"database":"InterPro","id":"IPR017892","properties":[{"key":"EntryName","value":"Pkinase_C"}]},{"database":"InterPro","id":"IPR000719","properties":[{"key":"EntryName","value":"Prot_kinase_dom"}]},{"database":"InterPro","id":"IPR017441","properties":[{"key":"EntryName","value":"Protein_kinase_ATP_BS"}]},{"database":"InterPro","id":"IPR008271","properties":[{"key":"EntryName","value":"Ser/Thr_kinase_AS"}]},{"database":"PANTHER","id":"PTHR24351","properties":[{"key":"EntryName","value":"RIBOSOMAL PROTEIN S6 KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00130","properties":[{"key":"EntryName","value":"C1_1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF00168","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00069","properties":[{"key":"EntryName","value":"Pkinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00433","properties":[{"key":"EntryName","value":"Pkinase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00109","properties":[{"key":"EntryName","value":"C1"},{"key":"MatchStatus","value":"2"}]},{"database":"SMART","id":"SM00742","properties":[{"key":"EntryName","value":"Hr1"},{"key":"MatchStatus","value":"2"}]},{"database":"SMART","id":"SM00133","properties":[{"key":"EntryName","value":"S_TK_X"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00220","properties":[{"key":"EntryName","value":"S_TKc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF49562","properties":[{"key":"EntryName","value":"C2 domain (Calcium/lipid-binding domain, CaLB)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF57889","properties":[{"key":"EntryName","value":"Cysteine-rich domain"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF46585","properties":[{"key":"EntryName","value":"HR1 repeat"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56112","properties":[{"key":"EntryName","value":"Protein kinase-like (PK-like)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51285","properties":[{"key":"EntryName","value":"AGC_KINASE_CTER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50004","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50039","properties":[{"key":"EntryName","value":"FORK_HEAD_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00107","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_ATP"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50011","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_DOM"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00108","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_ST"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00479","properties":[{"key":"EntryName","value":"ZF_DAG_PE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50081","properties":[{"key":"EntryName","value":"ZF_DAG_PE_2"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MSDAQKLEDLQKRLQKEKSIKDATLKLREVQESDSGKAVCDATLADVAQRIFYFQNEIDKLILKQQMNTSGPVRTQIPITLPNPEGAPESVRAARAPRSPHTQPQTTVDEDGTVMEFHGDFLSNRPLSTVDLLKSETAITTKKVEYKLRELAYKLDVEKKVKVASEKLEQLGMTAKDDNAESAEKVALLKRALQKYQGLYIPGQEDEVPIVSGSGTALRRPMTGVLHVRLSGIKHQNNVPTRNSKPAESMAIIKIDGVVKGKTRMARNGPQGIRWNEEFEIPVTKASEIEITICDKPDYVPVTIGMFWLKISDLVEELRRKKVEADNDAAWAAANVHELAVKNHLARPSTGSMAEVAINSTVDGVESWWDLEPIGQISMKFNFVKDVAIRKRPSRLGRQGAVRKRKDEIREIQGHKFVSQKFYEIMCCALCAELFTGKGSQCEDCNFSCHQRCAEKVFIKCISSNSAEDPDEAKLNHRIPHRFETFTNLSPTWCSHCGHMLTFGRRHKKCSECPVMAHDGCSDLVPNHCGMPAETANKLMEEIRRRNQSGRFYAAGANKHAKKPSETKFDTIKLPHQSAFSEKDPAMIIAEEQEALKQQQLRLQMEQLKLQQERESREKEIMLQKQKEHQMQLQQQQEQLQQQQLQQQQKQQQLEQQRVQLQQQQVYQQQMQQQRQDSERAHELDKFRREQARLEQLRLEQERAQQKIQGSPMTTPQMEQKPLVMPKVHTPTLKIVNKQGRKFAMNDFHFLAVLGRGNFGKVMLAEDKKGGELFAIKALKKESIVKHDEVESARSEKRIFQVANKDRHPFLTTLHSCFQTDTRIYFVMEYVRGGDLMMHIQMDKRFGERRAKFYGCEVLLALQYFHENNIVYRDLKLDNIMLALDGHIKIGDYGLCKENMPYGVTTRTICGTPEFMAPEIIEEQPYDRSVDWWTFGVLMYEMLLGRAPFSGEEEDDIYDSIMDDEPFYPAGFGRHEQALLQSLLVKVPALRLGAGPTDAEEIKAHAYFRNVNFDDVFHKRIPPPFLPKISSAKDVSNFDSEFTSESTGETPTDYRLNNVEQDLFKGFSYVSPWIPA","length":1076,"molWeight":123180,"crc64":"FE05098FFBE18133","md5":"D1F948A84A0FA2FA66B3A7CD3694C9A7"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":4,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":6,"DNA binding":1,"Zinc finger":2,"Region":1,"Coiled coil":1,"Active site":1,"Binding site":1,"Modified residue":3},"uniParcId":"UPI001E0477CF"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SLA5","uniProtkbId":"A0A9P5SLA5_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-09-13","entryVersion":14,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329634.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00067298"}],"value":"Protein phosphatase PP2A regulatory subunit B"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034808"}],"value":"5.6.2.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00042301"}],"value":"Minichromosome maintenance 9"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329634.1"}],"value":"CDC55_2"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329634.1"}],"value":"BG006_007298"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00055525"}],"value":"Phosphatase 2A affects a variety of biological processes in the cell such as transcription, cell cycle progression and cellular morphogenesis, and provides an initial identification of critical substrates for this phosphatase. The regulatory subunit may direct the catalytic subunit to distinct, albeit overlapping, subsets of substrates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048988"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.","ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034617"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001947"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}],"value":"Belongs to the MCM family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008259"}],"value":"Belongs to the phosphatase 2A regulatory subunit B family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329634.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":676,"modifier":"EXACT"},"end":{"value":1068,"modifier":"EXACT"}},"description":"MCM C-terminal AAA(+) ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50051"}]},{"type":"Region","location":{"start":{"value":905,"modifier":"EXACT"},"end":{"value":975,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1134,"modifier":"EXACT"},"end":{"value":1176,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1208,"modifier":"EXACT"},"end":{"value":1273,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Motif","location":{"start":{"value":743,"modifier":"EXACT"},"end":{"value":750,"modifier":"EXACT"}},"description":"Walker A","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}]},{"type":"Motif","location":{"start":{"value":805,"modifier":"EXACT"},"end":{"value":808,"modifier":"EXACT"}},"description":"Walker B","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}]},{"type":"Compositional bias","location":{"start":{"value":916,"modifier":"EXACT"},"end":{"value":925,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":953,"modifier":"EXACT"},"end":{"value":970,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1160,"modifier":"EXACT"},"end":{"value":1169,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1213,"modifier":"EXACT"},"end":{"value":1222,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1229,"modifier":"EXACT"},"end":{"value":1238,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Site","location":{"start":{"value":873,"modifier":"EXACT"},"end":{"value":873,"modifier":"EXACT"}},"description":"Arginine finger","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}],"id":"KW-0235","category":"Biological process","name":"DNA replication"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022574"}],"id":"KW-0853","category":"Domain","name":"WD repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329634.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329634.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000458","properties":[{"key":"ProteinId","value":"KAF9329634.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SLA5","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0031261","properties":[{"key":"GoTerm","value":"C:DNA replication preinitiation complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0042555","properties":[{"key":"GoTerm","value":"C:MCM complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005656","properties":[{"key":"GoTerm","value":"C:nuclear pre-replicative complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0043596","properties":[{"key":"GoTerm","value":"C:nuclear replication fork"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0000159","properties":[{"key":"GoTerm","value":"C:protein phosphatase type 2A complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0043138","properties":[{"key":"GoTerm","value":"F:3'-5' DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019888","properties":[{"key":"GoTerm","value":"F:protein phosphatase regulator activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0010972","properties":[{"key":"GoTerm","value":"P:negative regulation of G2/M transition of mitotic cell cycle"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006279","properties":[{"key":"GoTerm","value":"P:premeiotic DNA replication"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:1902531","properties":[{"key":"GoTerm","value":"P:regulation of intracellular signal transduction"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"FunFam","id":"3.40.50.300:FF:001141","properties":[{"key":"EntryName","value":"DNA helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.130.10.10:FF:000174","properties":[{"key":"EntryName","value":"Protein phosphatase PP2A regulatory subunit B"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.130.10.10:FF:000189","properties":[{"key":"EntryName","value":"Protein phosphatase PP2A regulatory subunit B"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.140","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.130.10.10","properties":[{"key":"EntryName","value":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR031327","properties":[{"key":"EntryName","value":"MCM"}]},{"database":"InterPro","id":"IPR058768","properties":[{"key":"EntryName","value":"MCM9_N"}]},{"database":"InterPro","id":"IPR001208","properties":[{"key":"EntryName","value":"MCM_dom"}]},{"database":"InterPro","id":"IPR041562","properties":[{"key":"EntryName","value":"MCM_lid"}]},{"database":"InterPro","id":"IPR033762","properties":[{"key":"EntryName","value":"MCM_OB"}]},{"database":"InterPro","id":"IPR012340","properties":[{"key":"EntryName","value":"NA-bd_OB-fold"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR000009","properties":[{"key":"EntryName","value":"PP2A_PR55"}]},{"database":"InterPro","id":"IPR018067","properties":[{"key":"EntryName","value":"PP2A_PR55_CS"}]},{"database":"InterPro","id":"IPR015943","properties":[{"key":"EntryName","value":"WD40/YVTN_repeat-like_dom_sf"}]},{"database":"InterPro","id":"IPR036322","properties":[{"key":"EntryName","value":"WD40_repeat_dom_sf"}]},{"database":"InterPro","id":"IPR001680","properties":[{"key":"EntryName","value":"WD40_rpt"}]},{"database":"PANTHER","id":"PTHR11871","properties":[{"key":"EntryName","value":"PROTEIN PHOSPHATASE PP2A REGULATORY SUBUNIT B"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00493","properties":[{"key":"EntryName","value":"MCM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF26066","properties":[{"key":"EntryName","value":"MCM9_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17855","properties":[{"key":"EntryName","value":"MCM_lid"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17207","properties":[{"key":"EntryName","value":"MCM_OB"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00600","properties":[{"key":"EntryName","value":"PP2APR55"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00350","properties":[{"key":"EntryName","value":"MCM"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00320","properties":[{"key":"EntryName","value":"WD40"},{"key":"MatchStatus","value":"7"}]},{"database":"SUPFAM","id":"SSF50249","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50978","properties":[{"key":"EntryName","value":"WD40 repeat-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50051","properties":[{"key":"EntryName","value":"MCM_CTD"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01024","properties":[{"key":"EntryName","value":"PR55_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01025","properties":[{"key":"EntryName","value":"PR55_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTSEGENSWKFAQCFGDKGEVEDITEADIISTVEFDHTGDYLATGDKGGRVVLFERNEGKKGCEYKFHTEFQSHEPEFDYLKSLEIEEKINKIKWCKRQNSAHFLLSTNDKTVKLWKVFEKSIKVVAENNHSSGQRVPNGSLQLPKLAHHDSIVAAVPRKVYANAHAYHINSISINSDAETYISADDLRINLWNLDISDQSFNIVDIKPVNMEELTEVITAAEFHPMHCNLFMYSSSKGTIKLSDMRESALCDQHSKLFEEEEDPSNKSFFSEIISSISDVKFSKDGRYILSRDYLTLKVWDINMESRPVQTINIHDHLRNKLCDLYENDCIFDKFECTFSGDGKNVLTGSYNNNFHIFDRNGTNDVTLQADKSAFKAKRVGSAKNKMAARPGFKNGKKDDINVESIDFSKKILHASWHPNENSIAVAATNNLFIFTSSAIESTALMVAKFSELTPDKVTRLKDVLKQGMLNRQENEILEILYGTDTTRHYSLSVHLMDLVDTSSDTELGSGVWWPLLSKSPHKVLPLMDAALQEAQKELLKRSDVATNNERWRGEKQDMFFKPKCSVRVNGQLPKGCRDYQEIKIQEQTTKLAMGTIPRSMFVILHDDLVDYAKSGDDVTITGTVIRRWKPPMPGDRCDIELAILANHVFIYNEQRVGVGVTEEQRLMFEQFWLKYRPPISHDNEPAKPFTARNIILSQVCPQVYGLYIVKLAVMLVLTGGVQKVDKSGLKVRGEPHLLLVGDPGTGKSQFLKFATQLNPRSILTTGIGTSSAGLTVTAVKDGNEWLLEAGALVLADRGLCCIDEFGGMREHDKTAIHEAMEQQSISIAKAGIVCKLNTRCSVIAATNPKGKYDPEQSVSINIALASPLLSRFDLVLVLMDTGNLNWDRKISSFILNSKMMADQDDPHRAMSRSQRSRRKRRMLNRIQTFTEREGNGEASTGGRRRVMGDDGSPELTDESNSDEDDVGQDPEGPWSIGKLKAYLIWVRATFEPRLTPPAEEVLTKYYQLQRKADVRNAARTTIRLLESLIRLSQAHARLMAKDLVTVEDAVAIVSLMEATVQGGVAVLGGVNPLHASFPKSAEDEYQMQETVLLRRLDLEHLASTPRAQRSQERRNEANDEWIHDVKEEVLSPVGPNSGRLVDVDQFRMPGSKRRRSPQPGTSSTNNGYGIKPGTRNAFLDDDDEEEMLQQFRQDDMLPGCIEEEDTYEEPLFDRRADRRNAPPPGWKGKEVDRGPGRVEQPTTCTSHRIEDDDDDDDLYGFRPPGSGSVEI","length":1273,"molWeight":143291,"crc64":"E3755072EDCFCC14","md5":"A6FD02E41C85C544BB0D6E1BDA9D4F9F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":3,"Motif":2,"Compositional bias":5,"Site":1},"uniParcId":"UPI001DCE2BBC"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SNC2","uniProtkbId":"A0A9P5SNC2_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-09-13","entryVersion":13,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9332285.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"4: Predicted","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044985"}],"value":"Lysosomal dipeptide transporter MFSD1"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045018"}],"value":"Major facilitator superfamily domain-containing protein 1"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9332285.1"}],"value":"BG006_004826"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045709"}],"value":"Lysosomal dipeptide uniporter that selectively exports lysine, arginine or histidine-containing dipeptides with a net positive charge from the lysosome lumen into the cytosol. Could play a role in a specific type of protein O-glycosylation indirectly regulating macrophages migration and tissue invasion. Also essential for liver homeostasis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alanyl-L-lysine(out) = L-alanyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79415"},{"database":"ChEBI","id":"CHEBI:192470"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044919"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-arginine(out) = L-alpha-aminoacyl-L-arginine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79367"},{"database":"ChEBI","id":"CHEBI:229968"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044881"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-histidine(out) = L-alpha-aminoacyl-L-histidine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79375"},{"database":"ChEBI","id":"CHEBI:229967"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044884"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-lysine(out) = L-alpha-aminoacyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79383"},{"database":"ChEBI","id":"CHEBI:229966"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044893"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-L-alpha-amino acid(out) = L-arginyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79371"},{"database":"ChEBI","id":"CHEBI:84315"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044899"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-glycine(out) = L-arginyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79391"},{"database":"ChEBI","id":"CHEBI:229955"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044903"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartyl-L-lysine(out) = L-aspartyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79411"},{"database":"ChEBI","id":"CHEBI:229953"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044898"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-L-alpha-amino acid(out) = L-histidyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79379"},{"database":"ChEBI","id":"CHEBI:229964"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044912"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-glycine(out) = L-histidyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79395"},{"database":"ChEBI","id":"CHEBI:229957"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044878"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alanine(out) = L-lysyl-L-alanine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79399"},{"database":"ChEBI","id":"CHEBI:229954"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044876"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alpha-amino acid(out) = L-lysyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79387"},{"database":"ChEBI","id":"CHEBI:229965"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044891"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-lysine(out) = L-lysyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79403"},{"database":"ChEBI","id":"CHEBI:229956"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044900"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-glycine(out) = L-lysyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79407"},{"database":"ChEBI","id":"CHEBI:191202"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044924"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00046376"}],"value":"Homodimer. Interacts with lysosomal protein GLMP (via lumenal domain); the interaction starts while both proteins are still in the endoplasmic reticulum and is required for stabilization of MFSD1 in lysosomes but has no direct effect on its targeting to lysosomes or transporter activity"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004127"}],"value":"Endomembrane system","id":"SL-0147"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004127"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9332285.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":340,"modifier":"EXACT"},"end":{"value":357,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":377,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":428,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":434,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":463,"modifier":"EXACT"},"end":{"value":487,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":493,"modifier":"EXACT"},"end":{"value":513,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Region","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":300,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023228"}],"id":"KW-0458","category":"Cellular component","name":"Lysosome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9332285.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9332285.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000269","properties":[{"key":"ProteinId","value":"KAF9332285.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SNC2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0012505","properties":[{"key":"GoTerm","value":"C:endomembrane system"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0022857","properties":[{"key":"GoTerm","value":"F:transmembrane transporter activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.20.1250.20","properties":[{"key":"EntryName","value":"MFS general substrate transporter like domains"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR011701","properties":[{"key":"EntryName","value":"MFS"}]},{"database":"InterPro","id":"IPR036259","properties":[{"key":"EntryName","value":"MFS_trans_sf"}]},{"database":"InterPro","id":"IPR052187","properties":[{"key":"EntryName","value":"MFSD1"}]},{"database":"PANTHER","id":"PTHR23512","properties":[{"key":"EntryName","value":"MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23512:SF3","properties":[{"key":"EntryName","value":"MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07690","properties":[{"key":"EntryName","value":"MFS_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF103473","properties":[{"key":"EntryName","value":"MFS general substrate transporter"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLATACFVMFGNYYAFDNPASLNQPLQEYMGMSDDRYAYFLNILYTSYSLPNIVLPWLGGYASDRFGHRKLLLSLSATVAFGHMVVCLGVQYKYVPAMILGRVLFGAGESLAVAQSAITVKYFRGKELAMALGINLCVARLGSVLNDILTPYIWTLSNVPVAFWGGFVSCILSFITACLLVWLDSNYGSLVAPAESGFSRLRTHHSDTRFSLDALDSTMRDELHQQYDPATPFGKARDSVGEEISLNILVKKPKCGPSTQRASMGVITEYRSSIGGQYRRNTRHSTESRSGESDEDEDDFDLDESLGTIPLAFSTQARQLSSARQCLQELSGLLDYSQSFWVLFLITFLLVGVQVPFNSIHAGFLQMRWYHNDPQKAAQIMTVPDLLSAILVLPVGYFVDHYGQKSWLFMLCGLIIGFAHSILGLVSIATPVPALMALGISSAIGALFTSAIPVLVKSHQIATAYGISSSAMNMAFTLFPLIVAKLMTVDPSVYTYVEVFFASCGFGGFLLAVRLKCLDRYGDLDRREMDNVNGGLVHH","length":539,"molWeight":59335,"crc64":"85961E1245FE28A7","md5":"14CEF041D5255167689516762B011384"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":13,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":11,"Region":1},"uniParcId":"UPI001D7BE4BD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SPG0","uniProtkbId":"A0A9P5SPG0_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-09-13","entryVersion":14,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9332804.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"value":"alpha-1,2-Mannosidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"value":"3.2.1.-"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9332804.1"}],"value":"BG006_004302"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribose 5-phosphate + ATP = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15609"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58017"},{"database":"ChEBI","id":"CHEBI:78346"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"2.7.6.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049535"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) + 4 H2O = N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2) + 4 beta-D-mannose","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:56008"},{"database":"Rhea","id":"RHEA-COMP:14356"},{"database":"Rhea","id":"RHEA-COMP:14367"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28563"},{"database":"ChEBI","id":"CHEBI:59087"},{"database":"ChEBI","id":"CHEBI:139493"}],"ecNumber":"3.2.1.113","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048605"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) + 3 H2O = N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2) + 3 beta-D-mannose","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:56028"},{"database":"Rhea","id":"RHEA-COMP:14358"},{"database":"Rhea","id":"RHEA-COMP:14367"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28563"},{"database":"ChEBI","id":"CHEBI:59087"},{"database":"ChEBI","id":"CHEBI:60628"}],"ecNumber":"3.2.1.113","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047669"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001913"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-2"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004996"}],"value":"Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004922"}],"value":"Protein modification; protein glycosylation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007658"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"value":"Belongs to the glycosyl hydrolase 47 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006478"}],"value":"Belongs to the ribose-phosphate pyrophosphokinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9332804.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"Ribose-phosphate pyrophosphokinase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF13793"}]},{"type":"Region","location":{"start":{"value":349,"modifier":"EXACT"},"end":{"value":454,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":519,"modifier":"EXACT"},"end":{"value":538,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1088,"modifier":"EXACT"},"end":{"value":1127,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":418,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":436,"modifier":"EXACT"},"end":{"value":446,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":519,"modifier":"EXACT"},"end":{"value":538,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1088,"modifier":"EXACT"},"end":{"value":1108,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1116,"modifier":"EXACT"},"end":{"value":1127,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":634,"modifier":"EXACT"},"end":{"value":634,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-1"}]},{"type":"Active site","location":{"start":{"value":766,"modifier":"EXACT"},"end":{"value":766,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-1"}]},{"type":"Active site","location":{"start":{"value":891,"modifier":"EXACT"},"end":{"value":891,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-1"}]},{"type":"Active site","location":{"start":{"value":930,"modifier":"EXACT"},"end":{"value":930,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-1"}]},{"type":"Binding site","location":{"start":{"value":1018,"modifier":"EXACT"},"end":{"value":1018,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-2"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108"}},{"type":"Disulfide bond","location":{"start":{"value":833,"modifier":"EXACT"},"end":{"value":877,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-3"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-2"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-3"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-2"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022727"}],"id":"KW-0545","category":"Biological process","name":"Nucleotide biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9332804.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9332804.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000238","properties":[{"key":"ProteinId","value":"KAF9332804.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SPG0","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005783","properties":[{"key":"GoTerm","value":"C:endoplasmic reticulum"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0002189","properties":[{"key":"GoTerm","value":"C:ribose phosphate diphosphokinase complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005509","properties":[{"key":"GoTerm","value":"F:calcium ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004571","properties":[{"key":"GoTerm","value":"F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004749","properties":[{"key":"GoTerm","value":"F:ribose phosphate diphosphokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006015","properties":[{"key":"GoTerm","value":"P:5-phosphoribose 1-diphosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0036503","properties":[{"key":"GoTerm","value":"P:ERAD pathway"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0009165","properties":[{"key":"GoTerm","value":"P:nucleotide biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009156","properties":[{"key":"GoTerm","value":"P:ribonucleoside monophosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06223","properties":[{"key":"EntryName","value":"PRTases_typeI"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2020:FF:000031","properties":[{"key":"EntryName","value":"Probable PRS4-ribose-phosphate pyrophosphokinase 3"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2020:FF:000005","properties":[{"key":"EntryName","value":"Ribose-phosphate pyrophosphokinase 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.50.10.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR012341","properties":[{"key":"EntryName","value":"6hp_glycosidase-like_sf"}]},{"database":"InterPro","id":"IPR001382","properties":[{"key":"EntryName","value":"Glyco_hydro_47"}]},{"database":"InterPro","id":"IPR050749","properties":[{"key":"EntryName","value":"Glycosyl_Hydrolase_47"}]},{"database":"InterPro","id":"IPR000842","properties":[{"key":"EntryName","value":"PRib_PP_synth_CS"}]},{"database":"InterPro","id":"IPR029099","properties":[{"key":"EntryName","value":"Pribosyltran_N"}]},{"database":"InterPro","id":"IPR029057","properties":[{"key":"EntryName","value":"PRTase-like"}]},{"database":"InterPro","id":"IPR000836","properties":[{"key":"EntryName","value":"PRTase_dom"}]},{"database":"InterPro","id":"IPR005946","properties":[{"key":"EntryName","value":"Rib-P_diPkinase"}]},{"database":"InterPro","id":"IPR036026","properties":[{"key":"EntryName","value":"Seven-hairpin_glycosidases"}]},{"database":"NCBIfam","id":"NF002320","properties":[{"key":"EntryName","value":"PRK01259.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01251","properties":[{"key":"EntryName","value":"ribP_PPkin"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11742:SF55","properties":[{"key":"EntryName","value":"ENDOPLASMIC RETICULUM MANNOSYL-OLIGOSACCHARIDE 1,2-ALPHA-MANNOSIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11742","properties":[{"key":"EntryName","value":"MANNOSYL-OLIGOSACCHARIDE ALPHA-1,2-MANNOSIDASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01532","properties":[{"key":"EntryName","value":"Glyco_hydro_47"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14572","properties":[{"key":"EntryName","value":"Pribosyl_synth"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF13793","properties":[{"key":"EntryName","value":"Pribosyltran_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00747","properties":[{"key":"EntryName","value":"GLYHDRLASE47"}]},{"database":"SMART","id":"SM01400","properties":[{"key":"EntryName","value":"Pribosyltran_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53271","properties":[{"key":"EntryName","value":"PRTase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48225","properties":[{"key":"EntryName","value":"Seven-hairpin glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00114","properties":[{"key":"EntryName","value":"PRPP_SYNTHASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MASNSIKIFAGNSHVELAKLVARRLGTELSKVVVLKYSNQETSVTIGESVRDEDVFIIQSGCGEINDNLMELLIMINACKTASARRITAIIPCFPYARQDKKDKSRAPITAKLIANMLTVAGANHVITMDLHASQIQGFFNVPVDNLYAEPSTLKYIAEQIPDYKNGVIVSPDAGGAKRATSIADRLDLDFALIHKERKKANEVSRMVLVGDVKGKIAILVDDMADTCGTLGLAAKTLAENGALKVYAIVTHGILCGKAVQVINDSVLTKVVVTNTVPHDDKKKICPKLDTIDISGTLAEAIRRTHNGESVSFLFSHAVRQDQESLIAISNRRQDIPSSTQYQLEFEYQDDISSESSYTASDNELGEQEEPVFATPDSAGLDAAPAPAPAEEEAVEDSSSKDDVSGISQVPEPSSLSSHLRLRKPVYTSDDEEDKEREGDHHRELSHLSQTSLHGEEDMFKCQDRGPVIPLHVDGDDKYGKVPLSGRTQGRRWFRVRYAAIALGLITLGYLTLSSSNKDQRSWSLNGTSSGKRKQWSGNITNPEIWEERKEKVKEAFQHSWAAYKRDAWGKDEYHPISQKGSNMLQNGEGFGFTIVDSLDTMLLMGLEDEFQEARVWIRDHLSFNQDAEVNLFETTIRVLGGLLAAYDQSGQDKVFLKKAVDLADRLMGAFDTKSGIPYASVHLGKSHGVPGHVGGLSSTSEVSTLQLEFKYLSFLTGDDKYWKVVEKVMFKMREMEDLDGLVPIYISPTLGEYHGPEIRLGSRGDSYYEYLIKQYLQTGKKEPVYKEMYDRTIVGVKKHLLGRTVPQNLLFVGEISTHNPQFLSPKMDHLVCFLGGTMALASTEGRALDPATFPRSNFSKLQEEDFKMGEELTESCYEMYRQTETGLAAEIVYWVEKLEQVEHKQEPEYFAGSDFIINNRDGHNWLRPETVESLFYLWRLTKNEMYREWGWKIFEAIEKHSRVSTGGYSSIHDIRRKDHIEYSDKMETFFLAETLKYLYLLFGPEEVLPLDQYVFNTEAHPLPVFTPPERLLVGSQHLDDVKKPEREAEALPSENRHTVADSLPIPFEELKEADDIDQALEDIVVDEAGEEEASEVEVEYEESDAEAVGEGPEVDSTQQENVEPFL","length":1127,"molWeight":126313,"crc64":"89FE05EC0FCDCD2F","md5":"6ED38B960D398A01F5C9E1AE43F9C57F"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":2,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":3,"Compositional bias":6,"Active site":4,"Binding site":1,"Disulfide bond":1},"uniParcId":"UPI001DB8C243"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SPV8","uniProtkbId":"A0A9P5SPV8_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-09-13","entryVersion":13,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335028.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Ubiquinone biosynthesis O-methyltransferase, mitochondrial"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"3-demethylubiquinol 3-O-methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"2.1.1.64"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"3-demethylubiquinone 3-O-methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"2.1.1.-"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Polyprenyldihydroxybenzoate methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"2.1.1.114"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335028.1"}],"value":"COQ3"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335028.1"}],"value":"BG006_001017"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"O-methyltransferase required for two non-consecutive steps during ubiquinone biosynthesis. Catalyzes the 2 O-methylation of 3,4-dihydroxy-5-(all-trans-polyprenyl)benzoic acid into 4-hydroxy-3-methoxy-5-(all-trans-polyprenyl)benzoic acid. Also catalyzes the last step of ubiquinone biosynthesis by mediating methylation of 3-demethylubiquinone into ubiquinone. Also able to mediate the methylation of 3-demethylubiquinol into ubiquinol"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 3,4-dihydroxy-5-(all-trans-polyprenyl)benzoate + S-adenosyl-L-methionine = a 4-hydroxy-3-methoxy-5-(all-trans-polyprenyl)benzoate + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:44452"},{"database":"Rhea","id":"RHEA-COMP:10930"},{"database":"Rhea","id":"RHEA-COMP:10931"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:64694"},{"database":"ChEBI","id":"CHEBI:84443"}],"ecNumber":"2.1.1.114","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:44380"},{"database":"Rhea","id":"RHEA-COMP:9566"},{"database":"Rhea","id":"RHEA-COMP:10914"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17976"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:84422"}],"ecNumber":"2.1.1.64","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 3-demethylubiquinone + S-adenosyl-L-methionine = a ubiquinone + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:81215"},{"database":"Rhea","id":"RHEA-COMP:9565"},{"database":"Rhea","id":"RHEA-COMP:19654"},{"database":"ChEBI","id":"CHEBI:16389"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:231825"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Cofactor biosynthesis; ubiquinone biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Matrix side","id":"SL-9913"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Belongs to the class I-like SAM-binding methyltransferase superfamily. UbiG/COQ3 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335028.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Region","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0999","category":"Cellular component","name":"Mitochondrion inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022688"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0831","category":"Biological process","name":"Ubiquinone biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335028.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335028.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000119","properties":[{"key":"ProteinId","value":"KAF9335028.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SPV8","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0031314","properties":[{"key":"GoTerm","value":"C:extrinsic component of mitochondrial inner membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0061542","properties":[{"key":"GoTerm","value":"F:3-demethylubiquinol 3-O-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0010420","properties":[{"key":"GoTerm","value":"F:polyprenyldihydroxybenzoate methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02440","properties":[{"key":"EntryName","value":"AdoMet_MTases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.150","properties":[{"key":"EntryName","value":"Vaccinia Virus protein VP39"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00472","properties":[{"key":"EntryName","value":"UbiG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029063","properties":[{"key":"EntryName","value":"SAM-dependent_MTases_sf"}]},{"database":"InterPro","id":"IPR010233","properties":[{"key":"EntryName","value":"UbiG_MeTrfase"}]},{"database":"NCBIfam","id":"TIGR01983","properties":[{"key":"EntryName","value":"UbiG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43464","properties":[{"key":"EntryName","value":"METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43464:SF19","properties":[{"key":"EntryName","value":"UBIQUINONE BIOSYNTHESIS O-METHYLTRANSFERASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13489","properties":[{"key":"EntryName","value":"Methyltransf_23"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53335","properties":[{"key":"EntryName","value":"S-adenosyl-L-methionine-dependent methyltransferases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSASTIRATARLARTKVTEACSQGWRHGALGPLTPMTSVASQHRTLSTSSSTKHSHHDQSKQSTEAGLDSIYTVNKDEIAKFAAMSDEWWAPQGPFKMLHLMNPPRIRYIRNRLEASRAISASSSSTDTHSRARFPLQGLRILDVGCGGGLLAEALARLGAQVTGLDASNENIQMAKIHSKKDPLLNGGSPGSLEYRHQTAEQLLEQGLQFDVVCSMEVIEHVENPAGFLKVLGQLVKPNGDLILSTMSRTPLAYFLTVFSAEHVLRMVPVGTHHWSKYITPKELEAGVRDLAGCEVLNVQGIGFNPLSGQWELNRNRTEQSMGILANIGASFAESVNYFLAAKKTSPSASASSPPS","length":357,"molWeight":38701,"crc64":"311BC110A4B0A209","md5":"D47D0565E94E8439F9B9FA7CD9A9ED35"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Region":1,"Compositional bias":1,"Binding site":7},"uniParcId":"UPI001D6FBC06"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SQ48","uniProtkbId":"A0A9P5SQ48_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-09-13","entryVersion":14,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335651.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Sulfate adenylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"2.7.7.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"ATP-sulfurylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Sulfate adenylate transferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"SAT"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335651.1"}],"value":"MET3"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335651.1"}],"value":"BG006_010997"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24152"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58243"},{"database":"ChEBI","id":"CHEBI:58339"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001823"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"sulfate + ATP + H(+) = adenosine 5'-phosphosulfate + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18133"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16189"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58243"}],"ecNumber":"2.7.7.4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00062002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Homohexamer. Dimer of trimers"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"The adenylyl-sulfate kinase (APS kinase) is non-functional. It is involved in allosteric regulation by PAPS. PAPS binding induces a large rotational rearrangement of domains lowering the substrate affinity of the enzyme"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"In the C-terminal section; belongs to the APS kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"In the N-terminal section; belongs to the sulfate adenylyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335651.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"ATP-sulfurylase PUA-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF14306"}]},{"type":"Domain","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"Sulphate adenylyltransferase catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01747"}]},{"type":"Domain","location":{"start":{"value":396,"modifier":"EXACT"},"end":{"value":548,"modifier":"EXACT"}},"description":"APS kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01583"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"N-terminal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Region","location":{"start":{"value":396,"modifier":"EXACT"},"end":{"value":574,"modifier":"EXACT"}},"description":"Allosteric regulation domain; adenylyl-sulfate kinase-like","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Active site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Active site","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Active site","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"sulfate","id":"ChEBI:CHEBI:16189"}},{"type":"Binding site","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"sulfate","id":"ChEBI:CHEBI:16189"}},{"type":"Binding site","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"sulfate","id":"ChEBI:CHEBI:16189"}},{"type":"Binding site","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":435,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58339"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"3'-phosphoadenylyl sulfate","id":"ChEBI:CHEBI:58339","note":"allosteric inhibitor"}},{"type":"Site","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Site","location":{"start":{"value":207,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Site","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"Induces change in substrate recognition on ATP binding","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0198","category":"Biological process","name":"Cysteine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335651.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335651.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000091","properties":[{"key":"ProteinId","value":"KAF9335651.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SQ48","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004020","properties":[{"key":"GoTerm","value":"F:adenylylsulfate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004781","properties":[{"key":"GoTerm","value":"F:sulfate adenylyltransferase (ATP) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070814","properties":[{"key":"GoTerm","value":"P:hydrogen sulfide biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000103","properties":[{"key":"GoTerm","value":"P:sulfate assimilation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02027","properties":[{"key":"EntryName","value":"APSK"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00517","properties":[{"key":"EntryName","value":"ATPS"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.400.10:FF:000003","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000802","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000052","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.400.10","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03106","properties":[{"key":"EntryName","value":"Sulf_adenylyltr_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002891","properties":[{"key":"EntryName","value":"APS"}]},{"database":"InterPro","id":"IPR059117","properties":[{"key":"EntryName","value":"APS_kinase_dom"}]},{"database":"InterPro","id":"IPR025980","properties":[{"key":"EntryName","value":"ATP-Sase_PUA-like_dom"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR015947","properties":[{"key":"EntryName","value":"PUA-like_sf"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"InterPro","id":"IPR027535","properties":[{"key":"EntryName","value":"Sulf_adenylyltr_euk"}]},{"database":"InterPro","id":"IPR050512","properties":[{"key":"EntryName","value":"Sulf_AdTrans/APS_kinase"}]},{"database":"InterPro","id":"IPR024951","properties":[{"key":"EntryName","value":"Sulfurylase_cat_dom"}]},{"database":"InterPro","id":"IPR002650","properties":[{"key":"EntryName","value":"Sulphate_adenylyltransferase"}]},{"database":"NCBIfam","id":"TIGR00455","properties":[{"key":"EntryName","value":"apsK"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004040","properties":[{"key":"EntryName","value":"PRK05537.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00339","properties":[{"key":"EntryName","value":"sopT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42700","properties":[{"key":"EntryName","value":"SULFATE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42700:SF1","properties":[{"key":"EntryName","value":"SULFATE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01583","properties":[{"key":"EntryName","value":"APS_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01747","properties":[{"key":"EntryName","value":"ATP-sulfurylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14306","properties":[{"key":"EntryName","value":"PUA_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52374","properties":[{"key":"EntryName","value":"Nucleotidylyl transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF88697","properties":[{"key":"EntryName","value":"PUA domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MANTPHGGILKDLVARDLPIRSQLLEESATLASIVLTERQLCDLELIISGGFSPLEGFLNEKDYKSVVDDLRLANGALFSIPINLDVSQEDIDALSLQPNKRVTLRDPRNDEPIAILTIQDIYTPDKVKEAVQVFGDDDLAHPAVKYLHQNVKEFYVGGNVQAVQPPVHYDYVAYRNTPAELRAYFQKLNWTRVVAFQTRNPMHRAHRELTVRAARSRQANVLINPVVGLTKPGDIDHFTRVRVYEAIIRRYPTGMAALSLLPLAMRMAGPREALWHAIIRKNHGSTHFIIGRDHAGPGKNSAGKDFYGPYDAQYLVEKYKDEIDIEVVPFQQVTYLPDSDEYVPSNEVPAGAKTLDISGTELRRRLRTGAHIPEWFSYPEVVALLRESHPPRSKQGFTVFLTGYHASKKESIARALQVALNQQGGRSISLLLGETIRGKLSSELGFSKRERDININRLGFVSAELTRAGAGVIVAPIAPYEEARQQARQEVEKSGGFFLVHVATPLEQAIAWDRDGVYERAKKGEIKGFTGIDDPYEVPKHAELTVNPAVESVAQIVRRIVLLLDQQGYFGDV","length":574,"molWeight":64120,"crc64":"88D8EED9C434150B","md5":"E5EE78B289565326D6F26395D53CF3CC"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":3,"Region":2,"Active site":3,"Binding site":7,"Site":3},"uniParcId":"UPI001D8C6F74"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SR30","uniProtkbId":"A0A9P5SR30_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-09-13","entryVersion":8,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335905.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Phosphatidylserine decarboxylase proenzyme 1, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"4.1.1.65"}]},"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Phosphatidylserine decarboxylase 1 beta chain"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Phosphatidylserine decarboxylase 1 alpha chain"}}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335905.1"}],"value":"PSD1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335905.1"}],"value":"BG006_010330"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20828"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57262"},{"database":"ChEBI","id":"CHEBI:64612"}],"ecNumber":"4.1.1.65","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyruvate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:15361"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Binds 1 pyruvoyl group covalently per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005189"}],"value":"Lipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","molecule":"Phosphatidylserine decarboxylase 1 alpha chain","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Intermembrane side","id":"SL-9912"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Phosphatidylserine decarboxylase 1 beta chain","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Single-pass membrane protein","id":"SL-9904"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Intermembrane side","id":"SL-9912"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type I sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335905.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":433,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase 1 beta chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"featureId":"PRO_5040554444"},{"type":"Chain","location":{"start":{"value":434,"modifier":"EXACT"},"end":{"value":467,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase 1 alpha chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"featureId":"PRO_5040554443"},{"type":"Topological domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"Mitochondrial matrix","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Topological domain","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":467,"modifier":"EXACT"}},"description":"Mitochondrial intermembrane","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Region","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Active site","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Active site","location":{"start":{"value":434,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Active site","location":{"start":{"value":434,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Site","location":{"start":{"value":433,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"Cleavage (non-hydrolytic); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Modified residue","location":{"start":{"value":434,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"Pyruvic acid (Ser); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0999","category":"Cellular component","name":"Mitochondrion inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0594","category":"Biological process","name":"Phospholipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023264"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-1208","category":"Biological process","name":"Phospholipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023317"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0865","category":"PTM","name":"Zymogen"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335905.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9335905.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000081","properties":[{"key":"ProteinId","value":"KAF9335905.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SR30","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005743","properties":[{"key":"GoTerm","value":"C:mitochondrial inner membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004609","properties":[{"key":"GoTerm","value":"F:phosphatidylserine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006646","properties":[{"key":"GoTerm","value":"P:phosphatidylethanolamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016540","properties":[{"key":"GoTerm","value":"P:protein autoprocessing"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"HAMAP","id":"MF_03208","properties":[{"key":"EntryName","value":"PS_decarb_PSD_B_type1_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003817","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"}]},{"database":"InterPro","id":"IPR033177","properties":[{"key":"EntryName","value":"PSD-B"}]},{"database":"InterPro","id":"IPR033661","properties":[{"key":"EntryName","value":"PSD_type1_euk"}]},{"database":"NCBIfam","id":"TIGR00163","properties":[{"key":"EntryName","value":"PS_decarb"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10067","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10067:SF6","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02666","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MQAHALPLTRVAFRRTPVCAARATLLRPSTTQCAPSPLVHRNFHASRRTFNQESNTNQKPYGERVKSAWRDTPIKWRPIPIGLGLAFIAFLQYQKILRREAEKDNDKSTQALIVGPWHVHVISELPLKTISRLWGAFNSITLPMWFRVPGFKLYSWIFGCNLDEMKDPDLTHYKNLSEFFYRELKDGARPVDYDAALISPSDGRVFHFGLVDGSRVEHVKGMSYSLDQFLGAHRASETAEIVKASHSANIVNEEEFAEVNGINYSLDSLLGNDQQPTMEHKRQDSEGNVVHDDEADKKSMTQVPKHLKLRPGNALFFCVIYLAPGDYHRFHSPTNWVAETRRHFSGELYSVSPWMVKQLQNLFVLNERVVLLGKWRHGFFSMVPVGATNELRTNHHEDHYKRGYGEVVYSGVSRLLNGQPLHVGEEMGGFKLGSTVVLVFEAPENFKFLIEPGQVVRMGQPLGQIEE","length":467,"molWeight":53179,"crc64":"E7664D4E89319B8E","md5":"BF0D7620FC21D79C693727F278CB1314"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":2,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Chain":2,"Topological domain":2,"Region":1,"Compositional bias":1,"Active site":4,"Site":1,"Modified residue":1},"uniParcId":"UPI001D92D613"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SRA2","uniProtkbId":"A0A9P5SRA2_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-09-13","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9334624.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00026218"}],"value":"Oxidized purine nucleoside triphosphate hydrolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00026103"}],"value":"3.6.1.56"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031927"}],"value":"2-hydroxy-dATP diphosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030682"}],"value":"7,8-dihydro-8-oxoguanine triphosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030634"}],"value":"8-oxo-dGTPase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032071"}],"value":"Methylated purine nucleoside triphosphate hydrolase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029673"}],"value":"Nucleoside diphosphate-linked moiety X motif 1"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9334624.1"}],"value":"BG006_001807"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00053094"}],"value":"Oxidized purine nucleoside triphosphate hydrolase which is a prominent sanitizer of the oxidized nucleotide pool. Catalyzes the hydrolysis of 2-oxo-dATP (2-hydroxy-dATP) into 2-oxo-dAMP. Also has a significant hydrolase activity toward 2-oxo-ATP, 8-oxo-dGTP and 8-oxo-dATP. Through the hydrolysis of oxidized purine nucleoside triphosphates, prevents their incorporation into DNA and the subsequent transversions A:T to C:G and G:C to T:A. Also catalyzes the hydrolysis of methylated purine nucleoside triphosphate preventing their integration into DNA. Through this antimutagenic activity protects cells from oxidative stress"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-oxo-ATP + H2O = 2-oxo-AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67392"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:71395"},{"database":"ChEBI","id":"CHEBI:172878"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024596"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:67393"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024596"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-oxo-dATP + H2O = 2-oxo-dAMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31583"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:63212"},{"database":"ChEBI","id":"CHEBI:77897"}],"ecNumber":"3.6.1.56","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024459"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:31584"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024459"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"8-oxo-dATP + H2O = 8-oxo-dAMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65396"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:71361"},{"database":"ChEBI","id":"CHEBI:172871"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024448"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65397"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024448"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31575"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:63224"},{"database":"ChEBI","id":"CHEBI:77896"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024486"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:31576"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024486"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-methyl-ATP + H2O = N(6)-methyl-AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67608"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:144842"},{"database":"ChEBI","id":"CHEBI:172873"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048002"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:67609"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048002"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-methyl-dATP + H2O = N(6)-methyl-dAMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67604"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:169976"},{"database":"ChEBI","id":"CHEBI:172872"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049032"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:67605"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049032"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"O(6)-methyl-dGTP + H2O = O(6)-methyl-dGMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67600"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:169974"},{"database":"ChEBI","id":"CHEBI:169975"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048894"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:67601"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048894"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005582"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003476"}],"value":"Belongs to the Nudix hydrolase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9334624.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"Nudix hydrolase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51462"}]},{"type":"Motif","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"Nudix box","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00794"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00794"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00794"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9334624.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9334624.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000138","properties":[{"key":"ProteinId","value":"KAF9334624.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SRA2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0008413","properties":[{"key":"GoTerm","value":"F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008828","properties":[{"key":"GoTerm","value":"F:dATP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042262","properties":[{"key":"GoTerm","value":"P:DNA protection"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd03427","properties":[{"key":"EntryName","value":"NUDIX_MTH1_Nudt1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.79.10","properties":[{"key":"EntryName","value":"Nucleoside Triphosphate Pyrophosphohydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003563","properties":[{"key":"EntryName","value":"8ODP"}]},{"database":"InterPro","id":"IPR020476","properties":[{"key":"EntryName","value":"Nudix_hydrolase"}]},{"database":"InterPro","id":"IPR015797","properties":[{"key":"EntryName","value":"NUDIX_hydrolase-like_dom_sf"}]},{"database":"InterPro","id":"IPR020084","properties":[{"key":"EntryName","value":"NUDIX_hydrolase_CS"}]},{"database":"InterPro","id":"IPR000086","properties":[{"key":"EntryName","value":"NUDIX_hydrolase_dom"}]},{"database":"PANTHER","id":"PTHR43758","properties":[{"key":"EntryName","value":"7,8-DIHYDRO-8-OXOGUANINE TRIPHOSPHATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43758:SF2","properties":[{"key":"EntryName","value":"OXIDIZED PURINE NUCLEOSIDE TRIPHOSPHATE HYDROLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00293","properties":[{"key":"EntryName","value":"NUDIX"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01403","properties":[{"key":"EntryName","value":"8OXTPHPHTASE"}]},{"database":"PRINTS","id":"PR00502","properties":[{"key":"EntryName","value":"NUDIXFAMILY"}]},{"database":"SUPFAM","id":"SSF55811","properties":[{"key":"EntryName","value":"Nudix"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51462","properties":[{"key":"EntryName","value":"NUDIX"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00893","properties":[{"key":"EntryName","value":"NUDIX_BOX"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDPFHITSKKVLTLVMVIDKDNQKILLGYKKRGFGAHLWNGFGGKVEPGETVRQGALRELQEEAGITVDDHKIQKAGLLLFLFENDPMGLECHVYKAYEYHGEIRECEEMRPQWFDIKDIPYEQMWEDDKIWLPELLKGQDPFYGRIYLKRKPLEVEGEEEGKVTVAAAAPSSTSNVSLTMVTVPFTTAQPKSGPFALFDHRLDLNLSKIPKEIAFDGTIASYED","length":225,"molWeight":25622,"crc64":"EC53A6AAE6A066C1","md5":"79E6C5D9DC9DF12300F92F24B348CA4B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":7,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Motif":1},"uniParcId":"UPI001D2FB276"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SRL2","uniProtkbId":"A0A9P5SRL2_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-09-13","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9334403.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00068518"}],"value":"Glutamate synthase [NADH]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024383"}],"value":"1.4.1.14"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9334403.1"}],"value":"GLT1_2"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9334403.1"}],"value":"BG006_002241"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057049"}],"value":"Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 L-glutamate + NAD(+) = L-glutamine + 2-oxoglutarate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13753"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:58359"}],"ecNumber":"1.4.1.14","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048867"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001917"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"[3Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000187-2"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:21137"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000187-2"}],"value":"Binds 1 [3Fe-4S] cluster."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004944"}],"value":"Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NAD(+) route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004802"}],"value":"Energy metabolism; nitrogen metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004909"}],"value":"Nitrogen metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011233"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009716"}],"value":"Belongs to the glutamate synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9334403.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"Glutamine amidotransferase type-2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51278"}]},{"type":"Region","location":{"start":{"value":931,"modifier":"EXACT"},"end":{"value":955,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":942,"modifier":"EXACT"},"end":{"value":953,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"For GATase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000187-1"}]},{"type":"Active site","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00609"}]},{"type":"Binding site","location":{"start":{"value":1136,"modifier":"EXACT"},"end":{"value":1136,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:21137"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000187-2"}],"ligand":{"name":"[3Fe-4S] cluster","id":"ChEBI:CHEBI:21137"}},{"type":"Binding site","location":{"start":{"value":1142,"modifier":"EXACT"},"end":{"value":1142,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:21137"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000187-2"}],"ligand":{"name":"[3Fe-4S] cluster","id":"ChEBI:CHEBI:21137"}},{"type":"Binding site","location":{"start":{"value":1147,"modifier":"EXACT"},"end":{"value":1147,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:21137"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000187-2"}],"ligand":{"name":"[3Fe-4S] cluster","id":"ChEBI:CHEBI:21137"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023291"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000187-2"}],"id":"KW-0003","category":"Ligand","name":"3Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022643"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023164"}],"id":"KW-0314","category":"Biological process","name":"Glutamate biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00609"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000187-2"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9334403.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9334403.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000150","properties":[{"key":"ProteinId","value":"KAF9334403.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016040","properties":[{"key":"GoTerm","value":"F:glutamate synthase (NADH) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0051536","properties":[{"key":"GoTerm","value":"F:iron-sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019676","properties":[{"key":"GoTerm","value":"P:ammonia assimilation cycle"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0097054","properties":[{"key":"GoTerm","value":"P:L-glutamate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00982","properties":[{"key":"EntryName","value":"gltB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00713","properties":[{"key":"EntryName","value":"GltS"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd02808","properties":[{"key":"EntryName","value":"GltS_FMN"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000031","properties":[{"key":"EntryName","value":"Glutamate synthase 1 [NADH]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000017","properties":[{"key":"EntryName","value":"Glutamate synthase [NADH], amyloplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.50.50.60:FF:000022","properties":[{"key":"EntryName","value":"Glutamate synthase [NADH], amyloplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.160.20.60:FF:000001","properties":[{"key":"EntryName","value":"Glutamate synthase, large subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.60.20.10:FF:000001","properties":[{"key":"EntryName","value":"Glutamate synthase, large subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1060.10","properties":[{"key":"EntryName","value":"Alpha-helical ferredoxin"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.50.60","properties":[{"key":"EntryName","value":"FAD/NAD(P)-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.20.60","properties":[{"key":"EntryName","value":"Glutamate synthase, alpha subunit, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.20.10","properties":[{"key":"EntryName","value":"Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR028261","properties":[{"key":"EntryName","value":"DPD_II"}]},{"database":"InterPro","id":"IPR036188","properties":[{"key":"EntryName","value":"FAD/NAD-bd_sf"}]},{"database":"InterPro","id":"IPR023753","properties":[{"key":"EntryName","value":"FAD/NAD-binding_dom"}]},{"database":"InterPro","id":"IPR017932","properties":[{"key":"EntryName","value":"GATase_2_dom"}]},{"database":"InterPro","id":"IPR002489","properties":[{"key":"EntryName","value":"Glu_synth_asu_C"}]},{"database":"InterPro","id":"IPR036485","properties":[{"key":"EntryName","value":"Glu_synth_asu_C_sf"}]},{"database":"InterPro","id":"IPR006982","properties":[{"key":"EntryName","value":"Glu_synth_centr_N"}]},{"database":"InterPro","id":"IPR012220","properties":[{"key":"EntryName","value":"Glu_synth_euk"}]},{"database":"InterPro","id":"IPR002932","properties":[{"key":"EntryName","value":"Glu_synthdom"}]},{"database":"InterPro","id":"IPR051394","properties":[{"key":"EntryName","value":"Glutamate_Synthase"}]},{"database":"InterPro","id":"IPR009051","properties":[{"key":"EntryName","value":"Helical_ferredxn"}]},{"database":"InterPro","id":"IPR029055","properties":[{"key":"EntryName","value":"Ntn_hydrolases_N"}]},{"database":"NCBIfam","id":"NF008730","properties":[{"key":"EntryName","value":"gltB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43100","properties":[{"key":"EntryName","value":"GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43100:SF1","properties":[{"key":"EntryName","value":"GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14691","properties":[{"key":"EntryName","value":"Fer4_20"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00310","properties":[{"key":"EntryName","value":"GATase_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04898","properties":[{"key":"EntryName","value":"Glu_syn_central"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01645","properties":[{"key":"EntryName","value":"Glu_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01493","properties":[{"key":"EntryName","value":"GXGXG"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07992","properties":[{"key":"EntryName","value":"Pyr_redox_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000187","properties":[{"key":"EntryName","value":"GOGAT"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF69336","properties":[{"key":"EntryName","value":"Alpha subunit of glutamate synthase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46548","properties":[{"key":"EntryName","value":"alpha-helical ferredoxin"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51395","properties":[{"key":"EntryName","value":"FMN-linked oxidoreductases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56235","properties":[{"key":"EntryName","value":"N-terminal nucleophile aminohydrolases (Ntn hydrolases)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51971","properties":[{"key":"EntryName","value":"Nucleotide-binding domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51278","properties":[{"key":"EntryName","value":"GATASE_TYPE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MESFMRSNNIESNSSWAGALPVAQGLYNPENEKDSCGVGFIASIKGEHSHHILKDASNILCNMTHRGATSADPRDGDGAGVMSGIPHTFMVEEAARLKVTLPAQGEYAVGNVFLRPDEPHLREQKATFESIAQKNGLKVLGWRKVPVDNSILGPSALSKEPSIQQPFVVLDPAVHATFDDKLFNRQLYVLRKEATHAITLKNWFYICSLSNQNIVYKGQLSPSQVYKFFYDLQNHEYTTHFALVHSRFSTNTFPSWDRAQPMRWAAHNGEINTLRGNKNWMRAREGVMSSDYFGDDLQKLFPIIEEGGSDSSAFDNVLELLVINGVLSLPEAIMMMLPEAWQSNGNIEPEKKAWYEWAACLMEPYDGPALMTFSDGRFCGASLDRNGLRPCRFYKTTDGLMICASEVGTMNIAPERILEKGRLQPGKMLLVDTLEGRVVDDRELKLSIASRQNFRKWVDEQMLSMDEVVAKAPKFDIMSTIDDLSLTQDPRLSAFKLTIEQLNLLLLPMTTDGKEALGSMGNDAPLACLSTEPQLIFDYFRQLFAQVTNPPIDPIREEIVMSLECYVGPEGNILEMDQSQCHKLRLPTPVVSLTEMEAIKNLESTRPDWKTRIIDITFSKSEGPSGYLMCLERVCSEVSDAIHDGVKIVILSDRETNAERVAISSLIATGGVHHYLVRMKQRSRVAIAVETAEAREVHHACVLLGYGADMICPYLAQEAILKLHRENAIKSEAGPEKLIKNYIKATNNGILKVMSKMGISTLQSYKGAQIFEALGLDESVIARSFAGTASRIKGVGFELLSLDALALHERAWPSRDTVAIEGIPESGDYHWRNGAIPHINDPDGIANLQDAVRRKNDNAYEAYSRNAFEQIKSCTLRGLLEFDFSKSTPISVDEVEPWTEICKRFCTGAMSYGSISMEAHSTLSVAMNRIGGKSNSGEGGEDPARSIPKDNGDSLRSSIKQIASGRFGVTSYYLSDAEEIQIKMAQGAKPGEGGELPGHKVSDEIGKTRHSTPGVGLISPPPHHDIYSIEDLKQLIYDAKAANPRARISVKLVSEVGVGVIASGVAKAKADHILISGHDGGTGASRWTGIKYAGLPWELGLAESHQTLVLNDLRGRVVVQTDEWGFATTPLIAMGCTMMRKCHLNTCPVGIATQDPLLREKFAGSPEHVINFFYYVAEELRTIMAKLGFRTINEMVGRTDVLVVDEARRNPKTANIDLSPILTPAHTLRPGAATFNVRKQEHMHHTRLDNKFISEAQEALNTGRRVELEGRVVNTDRALGTTVSYHVSSKYGENGLPDDTIHINLKGSAGQSLGAWLAPGVTIELEGDSNDYVGKGLSGGRLIVYPPKVSTFKSEENVIIGNTCLYGATSGKAFFGGIAAERFAVRNSGATAIVEGTGDHGCEYMTGGRVVVLGSTGRNFAAGMSGGIAYVLDLAGDFKSKVNMEMVQFETINEDEEVAWFRDTLEDHRHYTGSAVADRILKNLGEYLPKIVKVMPTDYRKVLDAQRAAKFAAAAQKAVEVIAPVLTAAPLAAKPKPDEPALVDLEDSMVDAETYKKRSEMVDKVRGFMKYKRRGDAYRNPKKRTKDYKEISARMTDGELQVQAARCMDCGVPFCQSNTTGCPIGNIIPKWNDLVFKNQWEEALNRLLMTNNFPEFTGRVCPAPCEGSCLDKGIVQRRIDLMAAEGIRFVPNTHVGVTTDVNSIRDENDALILATGATWPRDLPIVNRNLDGIHFAMEFLQLNTQSLLDSELNDGKYISAKGKHVVVIGGGDTGCDCIATSLRHGATSIVNFELLPQPPAVRAKDNPWPQFPRVFKQDYGHSEVQSHFGKDPREYSIVTKEFVSDGNGKVKGLNTIRVEWTQDATGRWSMKEMAGTEQYFQADLVLLSMGFMGPEAELLKSVGVKLDGRSNVETPKGSYQTSVGNVFAAGDARRGQSLIVWGINEGRQCAREVDEFLVGNTLLPVTGGMQRRSMKALAFETQHGASSLVSMA","length":1992,"molWeight":219176,"crc64":"A6BF1AA820FB140C","md5":"50F7C9F5CB5A35C74CA93BC4B2A992FD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":3,"PATHWAY":3,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Active site":2,"Binding site":3},"uniParcId":"UPI001DB62A7F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SSB3","uniProtkbId":"A0A9P5SSB3_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-09-13","entryVersion":16,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9337257.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013184"}],"value":"histone acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013184"}],"value":"2.3.1.48"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9337257.1"}],"value":"ESA1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9337257.1"}],"value":"BG006_005657"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045805"}],"value":"Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac. The NuA4 complex is involved in the DNA damage response and is required for chromosome segregation. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) through homologous recombination. Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins. In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-butenoyl-CoA + L-lysyl-[protein] = N(6)-(2E)-butenoyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53908"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:13707"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:137954"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047752"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:53909"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047752"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24180"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:15921"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:131780"},{"database":"ChEBI","id":"CHEBI:144968"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047557"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:24181"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047557"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21992"},{"database":"Rhea","id":"RHEA-COMP:9845"},{"database":"Rhea","id":"RHEA-COMP:11338"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048940"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:21993"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048940"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45948"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45948"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047787"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:45949"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047787"}]}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010107"}],"value":"Belongs to the MYST (SAS/MOZ) family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9337257.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":503,"modifier":"EXACT"}},"description":"MYST-type HAT","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51726"}]},{"type":"Region","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":405,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602717-51"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]},{"type":"Binding site","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":409,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":488,"modifier":"EXACT"},"end":{"value":488,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Modified residue","location":{"start":{"value":329,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"N6-acetyllysine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022990"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0007","category":"PTM","name":"Acetylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023159"}],"id":"KW-0010","category":"Molecular function","name":"Activator"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022853"}],"id":"KW-0156","category":"Molecular function","name":"Chromatin regulator"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023015"}],"id":"KW-0805","category":"Biological process","name":"Transcription regulation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9337257.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9337257.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000032","properties":[{"key":"ProteinId","value":"KAF9337257.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SSB3","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0000785","properties":[{"key":"GoTerm","value":"C:chromatin"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003682","properties":[{"key":"GoTerm","value":"F:chromatin binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004402","properties":[{"key":"GoTerm","value":"F:histone acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003712","properties":[{"key":"GoTerm","value":"F:transcription coregulator activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006357","properties":[{"key":"GoTerm","value":"P:regulation of transcription by RNA polymerase II"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"1.10.10.10:FF:000022","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.60.60:FF:000001","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.630.30:FF:000002","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.30.140","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.630.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.60.60","properties":[{"key":"EntryName","value":"N-acetyl transferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.10","properties":[{"key":"EntryName","value":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016181","properties":[{"key":"EntryName","value":"Acyl_CoA_acyltransferase"}]},{"database":"InterPro","id":"IPR016197","properties":[{"key":"EntryName","value":"Chromo-like_dom_sf"}]},{"database":"InterPro","id":"IPR000953","properties":[{"key":"EntryName","value":"Chromo/chromo_shadow_dom"}]},{"database":"InterPro","id":"IPR002717","properties":[{"key":"EntryName","value":"HAT_MYST-type"}]},{"database":"InterPro","id":"IPR050603","properties":[{"key":"EntryName","value":"MYST_HAT"}]},{"database":"InterPro","id":"IPR025995","properties":[{"key":"EntryName","value":"Tudor-knot"}]},{"database":"InterPro","id":"IPR036388","properties":[{"key":"EntryName","value":"WH-like_DNA-bd_sf"}]},{"database":"InterPro","id":"IPR040706","properties":[{"key":"EntryName","value":"Zf-MYST"}]},{"database":"PANTHER","id":"PTHR10615","properties":[{"key":"EntryName","value":"HISTONE ACETYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10615:SF218","properties":[{"key":"EntryName","value":"HISTONE ACETYLTRANSFERASE ESA1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01853","properties":[{"key":"EntryName","value":"MOZ_SAS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF11717","properties":[{"key":"EntryName","value":"Tudor-knot"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17772","properties":[{"key":"EntryName","value":"zf-MYST"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00298","properties":[{"key":"EntryName","value":"CHROMO"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55729","properties":[{"key":"EntryName","value":"Acyl-CoA N-acyltransferases (Nat)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54160","properties":[{"key":"EntryName","value":"Chromo domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51726","properties":[{"key":"EntryName","value":"MYST_HAT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSAVSSPFPSTVVGGDIGSIIVGCKLQVLHGTPSEYRKAEVLSIRPTPVPDDQNRHEYYVHYSDYNKRLDEWVTPERLNLLGEIEYPKAKKPKSALSGLEKESTGKASEPGTPGASSRGTKNNRKSQLSKAATASKSGGDAGSPAPGTPGTPGANKRKASAMDESGEKVPSIQVNGNEEDDDDASSVANGDTPVGAGGNMDENGVFSKEQEIEKLRTSGSMTQNPHEVARVKNLNLIQIGKHEVETWYFSPYPIEYAYLPILYICEFCLSYFPGVKQLSRHRVKCTLQHPPGNEIYRKDDISFFEIDGRKQKVYCRNLCLLSKLFLDHKTLYYDVDPFLFYVMTMRDEDGAHFIGYFSKEKESSEQYNVACILTMPQYQRMGFGRLLIAFSYELSKVEKRLGSPEKPLSDLGLLSYRAFWAETIVSLLVDQQKTGIELSIDDIANRTAFQPTDVLHTLQNLNALKYYHGQYVIVLSDTVIKNNERAMKKKKREVDPKALNWKPIHFTATQLRFL","length":514,"molWeight":57594,"crc64":"519BE3D3D56A3C97","md5":"FC0404D0D8790B89535493632AF4C91D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":5,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":2,"Active site":1,"Binding site":2,"Modified residue":1},"uniParcId":"UPI001DA1C56F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5SVB3","uniProtkbId":"A0A9P5SVB3_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-09-13","entryVersion":10,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9336415.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"4: Predicted","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044985"}],"value":"Lysosomal dipeptide transporter MFSD1"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045018"}],"value":"Major facilitator superfamily domain-containing protein 1"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9336415.1"}],"value":"BG006_008822"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045709"}],"value":"Lysosomal dipeptide uniporter that selectively exports lysine, arginine or histidine-containing dipeptides with a net positive charge from the lysosome lumen into the cytosol. Could play a role in a specific type of protein O-glycosylation indirectly regulating macrophages migration and tissue invasion. Also essential for liver homeostasis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alanyl-L-lysine(out) = L-alanyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79415"},{"database":"ChEBI","id":"CHEBI:192470"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044919"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-arginine(out) = L-alpha-aminoacyl-L-arginine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79367"},{"database":"ChEBI","id":"CHEBI:229968"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044881"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-histidine(out) = L-alpha-aminoacyl-L-histidine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79375"},{"database":"ChEBI","id":"CHEBI:229967"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044884"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-lysine(out) = L-alpha-aminoacyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79383"},{"database":"ChEBI","id":"CHEBI:229966"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044893"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-L-alpha-amino acid(out) = L-arginyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79371"},{"database":"ChEBI","id":"CHEBI:84315"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044899"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-glycine(out) = L-arginyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79391"},{"database":"ChEBI","id":"CHEBI:229955"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044903"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartyl-L-lysine(out) = L-aspartyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79411"},{"database":"ChEBI","id":"CHEBI:229953"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044898"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-L-alpha-amino acid(out) = L-histidyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79379"},{"database":"ChEBI","id":"CHEBI:229964"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044912"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-glycine(out) = L-histidyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79395"},{"database":"ChEBI","id":"CHEBI:229957"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044878"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alanine(out) = L-lysyl-L-alanine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79399"},{"database":"ChEBI","id":"CHEBI:229954"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044876"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alpha-amino acid(out) = L-lysyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79387"},{"database":"ChEBI","id":"CHEBI:229965"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044891"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-lysine(out) = L-lysyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79403"},{"database":"ChEBI","id":"CHEBI:229956"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044900"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-glycine(out) = L-lysyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79407"},{"database":"ChEBI","id":"CHEBI:191202"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044924"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00046376"}],"value":"Homodimer. Interacts with lysosomal protein GLMP (via lumenal domain); the interaction starts while both proteins are still in the endoplasmic reticulum and is required for stabilization of MFSD1 in lysosomes but has no direct effect on its targeting to lysosomes or transporter activity"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9336415.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":410,"modifier":"EXACT"},"end":{"value":433,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":504,"modifier":"EXACT"},"end":{"value":524,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":636,"modifier":"EXACT"},"end":{"value":658,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":559,"modifier":"EXACT"},"end":{"value":578,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":590,"modifier":"EXACT"},"end":{"value":624,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":559,"modifier":"EXACT"},"end":{"value":575,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":597,"modifier":"EXACT"},"end":{"value":613,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":614,"modifier":"EXACT"},"end":{"value":624,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9336415.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9336415.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000061","properties":[{"key":"ProteinId","value":"KAF9336415.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5SVB3","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0022857","properties":[{"key":"GoTerm","value":"F:transmembrane transporter activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.20.1250.20","properties":[{"key":"EntryName","value":"MFS general substrate transporter like domains"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR011701","properties":[{"key":"EntryName","value":"MFS"}]},{"database":"InterPro","id":"IPR036259","properties":[{"key":"EntryName","value":"MFS_trans_sf"}]},{"database":"InterPro","id":"IPR052187","properties":[{"key":"EntryName","value":"MFSD1"}]},{"database":"PANTHER","id":"PTHR23512","properties":[{"key":"EntryName","value":"MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23512:SF12","properties":[{"key":"EntryName","value":"TRANSPORTER, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G00260)-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07690","properties":[{"key":"EntryName","value":"MFS_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF103473","properties":[{"key":"EntryName","value":"MFS general substrate transporter"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSDSRLDYQPLQPIATTRHSQDNVNNSHSHNHNHNRTDSDDSVDRHDEEQHISEVQALVSPTQEQESFTFSQTYHGSESNQNKDSVKAAEWAIRMQAFFCAAMLGVSTHFTMHITGPLKDVLKENMGISNTQFSLLQSSLTLFPTLVPLIGGLLVERYGTGPSSIVFTTIVILGQVIVILGCWTHSIKIMVIGYCLFGIGAAPITIIQETIWVRYFRKNGLALVLALGLTSGKLAGFAALAGAYPLSTLNPFGFVTPFLVSLIISVIAWVMNIVFLILLKKPKEGADTMTKITILLKAKRTSLGWREVYGFSSMFWCILTISFLVGASWNPFMHQASNIVKHRYELNDEQAAWQASIILAIPLVIYPFLGTFIDHAGKRAWLLLVTAGLLICTHVLLLIPYSAVPIPPTIPMLLFALSLSLGTLSIVTSMPVLTKHVPTGLGLHRSIDNIGATLFGTVSGMMQDFSRVDADGESETESFFDRLYYKFFPVKVDLALQEREDVQLLGMFLLVALLLFIACAVFVWGDYYWTDGEGGKTGLLDEQDAEEVSMAEIGSSTLGFHSSNQTINRTEATSEQTERLLDAGAYGRDRHGRRAEEDEDSDSEDEDSQDESGEERFGVRIESGDDEIPRNKKLQAHFWIMFWTALLLCSWAVFGIGISR","length":660,"molWeight":73238,"crc64":"E747FEAED511AD26","md5":"295E3B428D2A68C66D08AB3EE816F523"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":13,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":12,"Region":3,"Compositional bias":4},"uniParcId":"UPI001D75BA56"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5VJ64","uniProtkbId":"A0A9P5VJ64_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-09-13","entryVersion":10,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326834.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}],"value":"Histidine biosynthesis trifunctional protein"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}],"value":"Phosphoribosyl-AMP cyclohydrolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}],"value":"3.5.4.19"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}],"value":"Phosphoribosyl-ATP pyrophosphohydrolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}],"value":"3.6.1.31"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}],"value":"Histidinol dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}],"value":"HDH"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}],"value":"1.1.1.23"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326834.1"}],"value":"HIS4"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326834.1"}],"value":"BG006_009789"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20049"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:58435"},{"database":"ChEBI","id":"CHEBI:59457"}],"ecNumber":"3.5.4.19","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000024"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22828"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:59457"},{"database":"ChEBI","id":"CHEBI:73183"}],"ecNumber":"3.6.1.31","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001460"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidinol + 2 NAD(+) + H2O = L-histidine + 2 NADH + 3 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20641"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57595"},{"database":"ChEBI","id":"CHEBI:57699"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.1.1.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049489"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001947"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005204"}],"value":"Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005169"}],"value":"Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004940"}],"value":"Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008260"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}],"value":"In the C-terminal section; belongs to the histidinol dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326834.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":233,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"Phosphoribosyl-AMP cyclohydrolase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01502"}]},{"type":"Region","location":{"start":{"value":393,"modifier":"EXACT"},"end":{"value":422,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":394,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023102"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}],"id":"KW-0368","category":"Biological process","name":"Histidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001257"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326834.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9326834.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000731","properties":[{"key":"ProteinId","value":"KAF9326834.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5VJ64","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004399","properties":[{"key":"GoTerm","value":"F:histidinol dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004635","properties":[{"key":"GoTerm","value":"F:phosphoribosyl-AMP cyclohydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004636","properties":[{"key":"GoTerm","value":"F:phosphoribosyl-ATP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000105","properties":[{"key":"GoTerm","value":"P:L-histidine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06572","properties":[{"key":"EntryName","value":"Histidinol_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd11546","properties":[{"key":"EntryName","value":"NTP-PPase_His4"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.287.1080:FF:000002","properties":[{"key":"EntryName","value":"Histidine biosynthesis bifunctional protein HisIE"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.20.810:FF:000002","properties":[{"key":"EntryName","value":"Histidine biosynthesis trifunctional protein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1980:FF:000050","properties":[{"key":"EntryName","value":"Histidine biosynthesis trifunctional protein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1980:FF:000001","properties":[{"key":"EntryName","value":"Histidinol dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.5.1300:FF:000002","properties":[{"key":"EntryName","value":"Histidinol dehydrogenase, chloroplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.5.1300","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.287.1080","properties":[{"key":"EntryName","value":"MazG-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1980","properties":[{"key":"EntryName","value":"Nitrogenase molybdenum iron protein domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.10.20.810","properties":[{"key":"EntryName","value":"Phosphoribosyl-AMP cyclohydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01024","properties":[{"key":"EntryName","value":"HisD"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016161","properties":[{"key":"EntryName","value":"Ald_DH/histidinol_DH"}]},{"database":"InterPro","id":"IPR008179","properties":[{"key":"EntryName","value":"HisE"}]},{"database":"InterPro","id":"IPR016298","properties":[{"key":"EntryName","value":"Histidine_synth_trifunct"}]},{"database":"InterPro","id":"IPR001692","properties":[{"key":"EntryName","value":"Histidinol_DH_CS"}]},{"database":"InterPro","id":"IPR012131","properties":[{"key":"EntryName","value":"Hstdl_DH"}]},{"database":"InterPro","id":"IPR021130","properties":[{"key":"EntryName","value":"PRib-ATP_PPHydrolase-like"}]},{"database":"InterPro","id":"IPR002496","properties":[{"key":"EntryName","value":"PRib_AMP_CycHydrolase_dom"}]},{"database":"InterPro","id":"IPR038019","properties":[{"key":"EntryName","value":"PRib_AMP_CycHydrolase_sf"}]},{"database":"NCBIfam","id":"TIGR00069","properties":[{"key":"EntryName","value":"hisD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR03188","properties":[{"key":"EntryName","value":"histidine_hisI"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21256:SF2","properties":[{"key":"EntryName","value":"HISTIDINE BIOSYNTHESIS TRIFUNCTIONAL PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21256","properties":[{"key":"EntryName","value":"HISTIDINOL DEHYDROGENASE HDH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00815","properties":[{"key":"EntryName","value":"Histidinol_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01502","properties":[{"key":"EntryName","value":"PRA-CH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01503","properties":[{"key":"EntryName","value":"PRA-PH"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001257","properties":[{"key":"EntryName","value":"His_trifunctional"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00083","properties":[{"key":"EntryName","value":"HOLDHDRGNASE"}]},{"database":"SUPFAM","id":"SSF53720","properties":[{"key":"EntryName","value":"ALDH-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF101386","properties":[{"key":"EntryName","value":"all-alpha NTP pyrophosphatases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF141734","properties":[{"key":"EntryName","value":"HisI-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00611","properties":[{"key":"EntryName","value":"HISOL_DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MILPLIDLTSENYQDQLKAFSLLPNQVLAVPTPDDARLQSVLKSQNKDAYWVQPATFDAQDPLAQIHALLDAGSDKVVLPFAAFASGGIDSFSHIPQERLAVSVYPADFDKVDQLVATVSAFILNVDTSAESLETIKSVTKVVQSGLLPRGGIKRVIAAFSSNGPASTPGLLAISELGRFGVDTQLSSSVLSADHQEGKLNLGEAFMATIVSDRPDGLFPTIVVDEQGISLGLVYSSLESVVESFRTRKGVYFSRSRGLWYKGASSGSTQDLIKVHVDCDSDALQFTVHQHGTGFCHNNIRGCFGPSSGLAHLDQTLQSRKISAPAGSYTHRLFKDSNLVQSKIMEEAEELCQATTAEDIAWETADLIYFALVKCVANGVTLRDVEQQLENRSRKITRRPGHAKPKWDVSAKTGQASDGATPVAPVTATASVVAPKTGRIAMKSYKMKALSADEQSKLLLRPIIQSNDIMARVKPIVEGVRERGDAALLELTAKFDGVQLESTVISAPFSPESMILDEQTKKAIDQAYDNIQKFHAAQLQDKALVVETMPGVVCTRFARPIERVGLYVPGGTAVLPSTALMLGIPAAVAGCSEIVIATPPRKDGSIVPEVMYVAHKVGASKVLMAGGAQAVAAMAYGTETCPKVDKICGPGNQYVTAAKMLTQIDSSSLVSIDMPAGPSELLVIADMTSVPAYVASDLLSQAEHGTDSQVVLIAVGLTAEHLTAIEDQVHEQASRLPRVDIVRESIPKSYIIEVDTMEEAMRFSNEYAPEHLILHLEQAERHVESVNNAGSVFVGHWSPESCGDYASGTNHTLPTYGYARMYSGVNTDTFLKHITSQQLTREGLDAIGDTVMRLAEIEGLEAHRNAVAVRINDIRGRA","length":878,"molWeight":94463,"crc64":"ABB2FD5383001448","md5":"2265C7316FD061C128551B0AE669472F"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":3,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1},"uniParcId":"UPI001D9008B6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5VL53","uniProtkbId":"A0A9P5VL53_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-09-13","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329896.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00039850"}],"value":"Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012046"}],"value":"1.3.8.1"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00039036"}],"value":"1.3.8.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00042821"}],"value":"2-methyl branched chain acyl-CoA dehydrogenase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00041537"}],"value":"2-methylbutyryl-coenzyme A dehydrogenase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329896.1"}],"value":"BG006_007108"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00094237"}],"value":"Short and branched chain specific acyl-CoA dehydrogenase that catalyzes the proR-proR stereospecific alpha,beta-dehydrogenation of fatty acyl-CoA thioesters using the electron transfer flavoprotein (ETF) as their physiologic electron acceptor, resulting in the formation of trans-2-enoyl-CoA ((2E)-enoyl-CoA). Among the different mitochondrial acyl-CoA dehydrogenases, acts specifically on short and branched chain acyl-CoA derivatives such as (S)-2-methylbutyryl-CoA as well as short straight chain acyl-CoAs such as butyryl-CoA (butanoyl-CoA). Plays an important role in the metabolism of L-isoleucine by catalyzing the dehydrogenation of 2-methylbutyryl-CoA, one of the steps of the L-isoleucine catabolic pathway. Can also act on valproyl-CoA, a metabolite of valproic acid, an antiepileptic drug"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R)-2-methylbutanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = ethylacryloyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65296"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:156439"},{"database":"ChEBI","id":"CHEBI:156440"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048592"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65297"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048592"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2S)-2-methylbutanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:48256"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57337"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:88166"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049552"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:48257"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049552"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-methylbutanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43780"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57336"},{"database":"ChEBI","id":"CHEBI:57337"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"ecNumber":"1.3.8.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048235"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:43781"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048235"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-methylpropanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = 2-methylpropenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:44180"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57338"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:62500"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051903"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:44181"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051903"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a short-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a short-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47196"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:87487"},{"database":"ChEBI","id":"CHEBI:87488"}],"ecNumber":"1.3.8.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051002"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:47197"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051002"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"butanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24004"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:57371"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049096"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:24005"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049096"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hexanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43464"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:62077"},{"database":"ChEBI","id":"CHEBI:62620"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049192"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:43465"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049192"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"valproyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-2-propylpent-2-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65344"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:156457"},{"database":"ChEBI","id":"CHEBI:156458"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048307"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65345"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048307"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00037895"}],"value":"Amino-acid degradation; L-isoleucine degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005198"}],"value":"Lipid metabolism; mitochondrial fatty acid beta-oxidation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011881"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004305"}],"value":"Mitochondrion matrix","id":"SL-0170"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"value":"Belongs to the acyl-CoA dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329896.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02771"}]},{"type":"Domain","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase middle","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02770"}]},{"type":"Domain","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00441"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022990"}],"id":"KW-0007","category":"PTM","name":"Acetylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022946"}],"id":"KW-0809","category":"Domain","name":"Transit peptide"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329896.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9329896.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000440","properties":[{"key":"ProteinId","value":"KAF9329896.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5VL53","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005759","properties":[{"key":"GoTerm","value":"C:mitochondrial matrix"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003853","properties":[{"key":"GoTerm","value":"F:short-chain 2-methyl fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046395","properties":[{"key":"GoTerm","value":"P:carboxylic acid catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006631","properties":[{"key":"GoTerm","value":"P:fatty acid metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd01158","properties":[{"key":"EntryName","value":"SCAD_SBCAD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.540.10:FF:000012","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase short/branched chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.140.10:FF:000002","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase short/branched chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.110.10:FF:000001","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.540.10","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase/oxidase, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.110.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.140.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006089","properties":[{"key":"EntryName","value":"Acyl-CoA_DH_CS"}]},{"database":"InterPro","id":"IPR046373","properties":[{"key":"EntryName","value":"Acyl-CoA_Oxase/DH_mid-dom_sf"}]},{"database":"InterPro","id":"IPR036250","properties":[{"key":"EntryName","value":"AcylCo_DH-like_C"}]},{"database":"InterPro","id":"IPR009075","properties":[{"key":"EntryName","value":"AcylCo_DH/oxidase_C"}]},{"database":"InterPro","id":"IPR006091","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_M"}]},{"database":"InterPro","id":"IPR013786","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_N"}]},{"database":"InterPro","id":"IPR037069","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_N_sf"}]},{"database":"InterPro","id":"IPR009100","properties":[{"key":"EntryName","value":"AcylCoA_DH/oxidase_NM_dom_sf"}]},{"database":"PANTHER","id":"PTHR43884","properties":[{"key":"EntryName","value":"ACYL-COA DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43884:SF1","properties":[{"key":"EntryName","value":"SHORT_BRANCHED CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00441","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02770","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02771","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF016578","properties":[{"key":"EntryName","value":"HsaA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47203","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56645","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase NM domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00072","properties":[{"key":"EntryName","value":"ACYL_COA_DH_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00073","properties":[{"key":"EntryName","value":"ACYL_COA_DH_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFSAIRPRLALAVAKPVLNAVRPRFFSQAAVARSNIASLHTLTEDEQLLKESVARFAQEQVLPKVAQMDETEQLDKDVLKGLFEQGLMGIETDSKYDGSESSFMSAILTIEELAKVDPSISVICDVQNTLVNTLFRKYASEDIKSRYLPRLATDTVGCFCLSEAGSGSDAFALQTRAVKDGDNYILNGSKMWITNSGEAEIFLVFANVDPSKGYKGITCFVVDKNMGVKINKKESKLGIRASSTCTLNFDDLVVPASNILGEVGKGYKYAIEILNEGRIGIAAQMLGLAQGVFDVTMPYLFQRKQFGSFIGNFQGMQQQYAQIAVDIEAARLLTYNAARLKEQGKPFVKEAAMAKLYASQVAERTASRCIEWAGGVGFTRDFPIEKFYRDCKIGAIYEGTSNIQLQTIAKILEKQYSS","length":418,"molWeight":46046,"crc64":"C3060BE2B7AC0E8E","md5":"C4BCC6137EEB2F3BB8F520F3A68BD4A2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":8,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI001E048965"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5VL55","uniProtkbId":"A0A9P5VL55_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-09-13","entryVersion":13,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9330222.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Inosine triphosphate pyrophosphatase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"ITPase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Inosine triphosphatase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"3.6.1.66"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Non-canonical purine NTP pyrophosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Non-standard purine NTP pyrophosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Nucleoside-triphosphate diphosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Nucleoside-triphosphate pyrophosphatase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"NTPase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"XTP/dITP diphosphatase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9330222.1"}],"value":"BG006_006812"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054940"}],"value":"Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ITP + H2O = IMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:29399"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58053"},{"database":"ChEBI","id":"CHEBI:61402"}],"ecNumber":"3.6.1.66","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093218"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:29400"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093218"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-hydroxy-dATP + H2O = N(6)-hydroxy-dAMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:83971"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:233529"},{"database":"ChEBI","id":"CHEBI:233530"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093271"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:83972"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093271"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"XTP + H2O = XMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28610"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57464"},{"database":"ChEBI","id":"CHEBI:61314"}],"ecNumber":"3.6.1.66","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dITP + H2O = dIMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28342"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61194"},{"database":"ChEBI","id":"CHEBI:61382"}],"ecNumber":"3.6.1.66","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093255"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:28343"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093255"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008023"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003781"}],"value":"Belongs to the HAM1 NTPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9330222.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Binding site","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61402"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"ITP","id":"ChEBI:CHEBI:61402"}},{"type":"Binding site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61402"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"ITP","id":"ChEBI:CHEBI:61402"}},{"type":"Binding site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61402"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"ITP","id":"ChEBI:CHEBI:61402"}},{"type":"Binding site","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61402"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"ITP","id":"ChEBI:CHEBI:61402"}},{"type":"Binding site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61402"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"ITP","id":"ChEBI:CHEBI:61402"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023080"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0546","category":"Biological process","name":"Nucleotide metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9330222.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9330222.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000413","properties":[{"key":"ProteinId","value":"KAF9330222.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5VL55","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0035870","properties":[{"key":"GoTerm","value":"F:dITP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036220","properties":[{"key":"GoTerm","value":"F:ITP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036222","properties":[{"key":"GoTerm","value":"F:XTP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009204","properties":[{"key":"GoTerm","value":"P:deoxyribonucleoside triphosphate catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009143","properties":[{"key":"GoTerm","value":"P:nucleoside triphosphate catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00515","properties":[{"key":"EntryName","value":"HAM1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.950.10:FF:000003","properties":[{"key":"EntryName","value":"Inosine triphosphate pyrophosphatase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.950.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03148","properties":[{"key":"EntryName","value":"HAM1_NTPase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR027502","properties":[{"key":"EntryName","value":"ITPase"}]},{"database":"InterPro","id":"IPR029001","properties":[{"key":"EntryName","value":"ITPase-like_fam"}]},{"database":"InterPro","id":"IPR002637","properties":[{"key":"EntryName","value":"RdgB/HAM1"}]},{"database":"NCBIfam","id":"TIGR00042","properties":[{"key":"EntryName","value":"RdgB/HAM1 family non-canonical purine NTP pyrophosphatase"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11067:SF9","properties":[{"key":"EntryName","value":"INOSINE TRIPHOSPHATE PYROPHOSPHATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11067","properties":[{"key":"EntryName","value":"INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01725","properties":[{"key":"EntryName","value":"Ham1p_like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52972","properties":[{"key":"EntryName","value":"ITPase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MALKKLGNKNKLVEVQQILGPHFDLQSVKIDLPELQGTTQDVSKEKCRQAAEIVKGPVITEDTSLGFNALNGLPGPYIKWFLEGVGHTGLNKMLDGFEDRSAFALCTFALSKGPGTEPILFEGRTDGSIVQARGPTHFGWDPVFLPDGFDTTYAEMDKDIKNTISHRGRALAKLREYLEKEENN","length":184,"molWeight":20348,"crc64":"38C4ECF1699D7C41","md5":"3922FC538F8155D0881353877BF00C51"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Binding site":7},"uniParcId":"UPI001D708FE0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9P5VM93","uniProtkbId":"A0A9P5VM93_9FUNG","entryAudit":{"firstPublicDate":"2023-09-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-09-13","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Podila minutissima","taxonId":64525,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9332008.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Mortierellomycota","Mortierellomycotina","Mortierellomycetes","Mortierellales","Mortierellaceae","Podila"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"Lon protease homolog, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"3.4.21.53"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9332008.1"}],"value":"PIM1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9332008.1"}],"value":"BG006_005128"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of proteins in presence of ATP.","ecNumber":"3.4.21.53","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10087"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"Homohexamer or homoheptamer. Organized in a ring with a central cavity"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004305"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"Mitochondrion matrix","id":"SL-0170"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01122"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000591"}],"value":"Belongs to the peptidase S16 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9332008.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":209,"modifier":"EXACT"},"end":{"value":513,"modifier":"EXACT"}},"description":"Lon N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51787"}]},{"type":"Domain","location":{"start":{"value":956,"modifier":"EXACT"},"end":{"value":1142,"modifier":"EXACT"}},"description":"Lon proteolytic","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51786"}]},{"type":"Region","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":349,"modifier":"EXACT"},"end":{"value":372,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1150,"modifier":"EXACT"},"end":{"value":1208,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"Gly residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":356,"modifier":"EXACT"},"end":{"value":371,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1159,"modifier":"EXACT"},"end":{"value":1168,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1169,"modifier":"EXACT"},"end":{"value":1188,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":1048,"modifier":"EXACT"},"end":{"value":1048,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10087"}]},{"type":"Active site","location":{"start":{"value":1091,"modifier":"EXACT"},"end":{"value":1091,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01122"}]},{"type":"Binding site","location":{"start":{"value":666,"modifier":"EXACT"},"end":{"value":673,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000696485"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022825"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0720","category":"Molecular function","name":"Serine protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022946"}],"id":"KW-0809","category":"Domain","name":"Transit peptide"}],"references":[{"referenceNumber":1,"citation":{"id":"33364917","citationType":"journal article","authors":["Vandepol N.","Liber J.","Desiro A.","Na H.","Kennedy M.","Barry K.","Grigoriev I.V.","Miller A.N.","O'Donnell K.","Stajich J.E.","Bonito G."],"citationCrossReferences":[{"database":"PubMed","id":"33364917"}],"title":"Resolving the Mortierellaceae phylogeny through synthesis of multi-gene phylogenetics and phylogenomics.","publicationDate":"2020","journal":"Fungal Divers.","firstPage":"267","lastPage":"289","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9332008.1"}],"value":"NVP1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAF9332008.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAAAUY010000288","properties":[{"key":"ProteinId","value":"KAF9332008.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9P5VM93","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000696485","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005759","properties":[{"key":"GoTerm","value":"C:mitochondrial matrix"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043565","properties":[{"key":"GoTerm","value":"F:sequence-specific DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003697","properties":[{"key":"GoTerm","value":"F:single-stranded DNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0034599","properties":[{"key":"GoTerm","value":"P:cellular response to oxidative stress"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051131","properties":[{"key":"GoTerm","value":"P:chaperone-mediated protein complex assembly"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0007005","properties":[{"key":"GoTerm","value":"P:mitochondrion organization"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0070407","properties":[{"key":"GoTerm","value":"P:oxidation-dependent protein catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006515","properties":[{"key":"GoTerm","value":"P:protein quality control for misfolded or incompletely synthesized proteins"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd19500","properties":[{"key":"EntryName","value":"RecA-like_Lon"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000021","properties":[{"key":"EntryName","value":"Lon protease homolog"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.5.5270:FF:000001","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.58.1480:FF:000003","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.30.130.40:FF:000010","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.230.10:FF:000015","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.5.5270","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.1480","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.230.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.130.40","properties":[{"key":"EntryName","value":"LON domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03120","properties":[{"key":"EntryName","value":"lonm_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR003959","properties":[{"key":"EntryName","value":"ATPase_AAA_core"}]},{"database":"InterPro","id":"IPR004815","properties":[{"key":"EntryName","value":"Lon_bac/euk-typ"}]},{"database":"InterPro","id":"IPR054594","properties":[{"key":"EntryName","value":"Lon_lid"}]},{"database":"InterPro","id":"IPR008269","properties":[{"key":"EntryName","value":"Lon_proteolytic"}]},{"database":"InterPro","id":"IPR027065","properties":[{"key":"EntryName","value":"Lon_Prtase"}]},{"database":"InterPro","id":"IPR003111","properties":[{"key":"EntryName","value":"Lon_prtase_N"}]},{"database":"InterPro","id":"IPR046336","properties":[{"key":"EntryName","value":"Lon_prtase_N_sf"}]},{"database":"InterPro","id":"IPR027503","properties":[{"key":"EntryName","value":"Lonm_euk"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR008268","properties":[{"key":"EntryName","value":"Peptidase_S16_AS"}]},{"database":"InterPro","id":"IPR015947","properties":[{"key":"EntryName","value":"PUA-like_sf"}]},{"database":"InterPro","id":"IPR020568","properties":[{"key":"EntryName","value":"Ribosomal_Su5_D2-typ_SF"}]},{"database":"InterPro","id":"IPR014721","properties":[{"key":"EntryName","value":"Ribsml_uS5_D2-typ_fold_subgr"}]},{"database":"NCBIfam","id":"TIGR00763","properties":[{"key":"EntryName","value":"lon"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43718","properties":[{"key":"EntryName","value":"LON PROTEASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43718:SF2","properties":[{"key":"EntryName","value":"LON PROTEASE HOMOLOG, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00004","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05362","properties":[{"key":"EntryName","value":"Lon_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22667","properties":[{"key":"EntryName","value":"Lon_lid"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02190","properties":[{"key":"EntryName","value":"LON_substr_bdg"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00830","properties":[{"key":"EntryName","value":"ENDOLAPTASE"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00464","properties":[{"key":"EntryName","value":"LON"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF88697","properties":[{"key":"EntryName","value":"PUA domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54211","properties":[{"key":"EntryName","value":"Ribosomal protein S5 domain 2-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51787","properties":[{"key":"EntryName","value":"LON_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51786","properties":[{"key":"EntryName","value":"LON_PROTEOLYTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01046","properties":[{"key":"EntryName","value":"LON_SER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSARNAVLVITRQISPSAQSLKVALARTTINPTLTHQTARTPRAWSAFDGQLRPFSCSSAQSNQFRRQRSLLPSNTTASQLVNGHQFTTVFGSRRALSSTARNLKEKNDNGNDNKGNKKGDNKGDNKSENPDGKDSGSGSGSGSSGSSGSSSSEGGSGASSGSNGSSSSGGKGDRKITKFTFDVGGGSSTNILESSLAKPAIPEVYPQVLTLPIGRRPLFPGFYKAVVIKNPAVANAIKELMKRGQPYVGAFLLKDEDLDVDTVTSMDQIHKVGVFAQITTIFPASAGSDEGSITAVLYPHRRIKIKELLPPMILPDGTEAPREGVLVKESGEASTSSTTEKTQAMIKGTEEGAPKETTTTTAVTKTSSGAESTVIDGTTVAGEEGASSSDPKDAAPHLPTAFLAKEYAVTLSNVENMVDEPYNRKNQVIRAITSEIVAVFKDIASLNPLFRDQIANFSMSQSAGNVFEEPAKLADFATAVSQGDPEELQSVLESLTIEDRMQKALLVLKKELMNAQLQSKISKDVENKIAKRQREYYLMEQLKGIKKELGIESDGKDKLIEKFREKGVKLAMPEQAKKVFDEEISKLEHLEPAASEFNVTRNYLDWLTNVPWGVRSPENYDIRHAVRVLDEDHYGLKDVKDRILEFIAVGRLRGTVEGKIICLVGPPGVGKTSIGKSIARALDREFYRFSVGGLTDVAEIKGHRRTYVGAMPGKVVQALKRVQTENPLILIDEVDKVGRGHQGDPASALLELLDPEQNGSFLDHYMDVPIDLSKVLFVCTANVLDTIPGPLLDRMEVIQLSGYISDEKVAIASRYLAPTAKQAAGLEGANVTLHDDAIEALIKNYCRESGVRNLKKQIDKVFRKAALKIVQDLPEVDRVEPKAKDSEKLAGIVKDTPDEILLDDTEALKTHDIKAEEVNKPKATVPSSVKVDITADNLKDYVGPAVFQADRLYDATPAGVVMGLAWTSMGGSALYIESCLDGGLSEKSRPNFLRTGQMGDVMKESTSIAYTFAKNLVGRRFPENRFFNKAAIHLHVPEGATPKDGPSAGITMTTSLLSLALNRPLDPTIAMTGELTLTGKVLKIGGLKEKTIAAKRSGVKTLIFPQANLSDWEELPANVKEGVNGVPAAWYEDVYKVVFGDSISEEEGNHVWQKELPGGEDAEDEIDNREPRKNEINAKRKSDKDNGNESTTCRSRMSESLDWQKYY","length":1208,"molWeight":131190,"crc64":"CCA5E5E21F3141CB","md5":"F615F53BC85836DE0E722D3ED4066FD1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":3,"Compositional bias":6,"Active site":2,"Binding site":1},"uniParcId":"UPI001DF1F9F2"}}]}