{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161XU27","uniProtkbId":"A0A161XU27_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-07-06","entryVersion":30,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40473.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Coenzyme A biosynthesis bifunctional protein CoaBC"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"DNA/pantothenate metabolism flavoprotein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase/decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPCS-PPCDC"}]}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-DC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"4.1.1.36"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaC"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenate--cysteine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"6.3.2.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-S"}]}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40473.1"}],"value":"TY91_08170"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-4'-phosphopantothenate + L-cysteine + CTP = N-[(R)-4-phosphopantothenoyl]-L-cysteine + CMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19397"},{"database":"ChEBI","id":"CHEBI:10986"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:35235"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:60377"}],"ecNumber":"6.3.2.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-[(R)-4-phosphopantothenoyl]-L-cysteine + H(+) = (R)-4'-phosphopantetheine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16793"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:61723"}],"ecNumber":"4.1.1.36","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Binds 1 FMN per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the C-terminal section; belongs to the PPC synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40473.1"}],"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":3,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":397,"modifier":"EXACT"}},"description":"DNA/pantothenate metabolism flavoprotein C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04127"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":325,"modifier":"EXACT"},"end":{"value":325,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":339,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":343,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40473.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40473.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000039","properties":[{"key":"ProteinId","value":"KZL40473.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056996244.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000039.1"}]},{"database":"AlphaFoldDB","id":"A0A161XU27","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.2205","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9802554at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00241","properties":[{"key":"RectionId","value":"UER00353"}]},{"database":"Proteomes","id":"UP000076480","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0071513","properties":[{"key":"GoTerm","value":"C:phosphopantothenoylcysteine decarboxylase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004632","properties":[{"key":"GoTerm","value":"F:phosphopantothenate--cysteine ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004633","properties":[{"key":"GoTerm","value":"F:phosphopantothenoylcysteine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015937","properties":[{"key":"GoTerm","value":"P:coenzyme A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015941","properties":[{"key":"GoTerm","value":"P:pantothenate catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.10300","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1950","properties":[{"key":"EntryName","value":"Flavin prenyltransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02225","properties":[{"key":"EntryName","value":"CoaBC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR035929","properties":[{"key":"EntryName","value":"CoaB-like_sf"}]},{"database":"InterPro","id":"IPR005252","properties":[{"key":"EntryName","value":"CoaBC"}]},{"database":"InterPro","id":"IPR007085","properties":[{"key":"EntryName","value":"DNA/pantothenate-metab_flavo_C"}]},{"database":"InterPro","id":"IPR036551","properties":[{"key":"EntryName","value":"Flavin_trans-like"}]},{"database":"InterPro","id":"IPR003382","properties":[{"key":"EntryName","value":"Flavoprotein"}]},{"database":"NCBIfam","id":"TIGR00521","properties":[{"key":"EntryName","value":"coaBC_dfp"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359","properties":[{"key":"EntryName","value":"HOMO-OLIGOMERIC FLAVIN CONTAINING CYS DECARBOXYLASE FAMILY"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359:SF6","properties":[{"key":"EntryName","value":"PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04127","properties":[{"key":"EntryName","value":"DFP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02441","properties":[{"key":"EntryName","value":"Flavoprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102645","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52507","properties":[{"key":"EntryName","value":"Homo-oligomeric flavin-containing Cys decarboxylases, HFCD"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLNDKNVALYVTGSIAAYKSLYLTRLLVKAGARVRVVMTTAAQAFVTPMSFQVLSKNQVLTSAFDSKTPTAVDHIELADWTDYAIVAPASADIIGKLANGIADDMASLTLMATTAPILLAPAMNEHMLNQPAVQHNLNTLTTNGVHFVAPGTGFLAEGYEGKGRMAEPDTILAELQLLSRPKTVFSGKNVLVTAGGTRERIDPVRFITNDSSGKMGYAIAAELVNRGANVTLISAPTRLTVPNGTHLVPVTTTEDLADAVVHHFPKADILVMAAAVADFRPKTSVDQKIKKTADNDEMTLSLVKTTDILKTAASLKQPGQLTVGFAAETQNLITNATKKLTSKQLDLLVANDVSQPGVGFNGDTNQVTILSRDKTPVQTALVSKTAVAATVVDELARLVDTKEG","length":404,"molWeight":42847,"crc64":"9030F0539A160B6E","md5":"20FE68C0249674FC5BE091C8FFB0DB8F"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Binding site":5},"uniParcId":"UPI0006EECD88"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161XVA0","uniProtkbId":"A0A161XVA0_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-07-06","entryVersion":39,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41695.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTP synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"6.3.4.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Cytidine 5'-triphosphate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Cytidine triphosphate synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTP synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"UTP--ammonia ligase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"pyrG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41695.1"}],"value":"TY91_05620"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates"}],"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"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + L-glutamine + ATP + H2O = CTP + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26426"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047781"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + NH4(+) + ATP = CTP + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16597"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Belongs to the CTP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41695.1"}],"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":3,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":527,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":508,"modifier":"EXACT"},"end":{"value":508,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":510,"modifier":"EXACT"},"end":{"value":510,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":405,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":463,"modifier":"EXACT"},"end":{"value":463,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41695.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41695.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000034","properties":[{"key":"ProteinId","value":"KZL41695.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056997355.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000034.1"}]},{"database":"AlphaFoldDB","id":"A0A161XVA0","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.1669","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9801107at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00159","properties":[{"key":"RectionId","value":"UER00277"}]},{"database":"Proteomes","id":"UP000076480","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0097268","properties":[{"key":"GoTerm","value":"C:cytoophidium"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003883","properties":[{"key":"GoTerm","value":"F:CTP synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0044210","properties":[{"key":"GoTerm","value":"P:'de novo' CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019856","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03113","properties":[{"key":"EntryName","value":"CTPS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01746","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000009","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000002","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"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_01227","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR004468","properties":[{"key":"EntryName","value":"CTP_synthase"}]},{"database":"InterPro","id":"IPR017456","properties":[{"key":"EntryName","value":"CTP_synthase_N"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR033828","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF003792","properties":[{"key":"EntryName","value":"PRK05380.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00337","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550","properties":[{"key":"EntryName","value":"CTP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550:SF0","properties":[{"key":"EntryName","value":"CTP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06418","properties":[{"key":"EntryName","value":"CTP_synth_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"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":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTKYIFVTGGVVSSLGKGIVAASLGRLLKNRGLNVTIQKFDPYINVDPGTMSPYQHGEVFVTNDGTETDLDLGHYERFIDNDLNKYSNVTTGKIYSEVLEKERHGDYLGATVQVIPHITGMIKEKIMRAGKTLNADFVITEIGGTVGDIESQPFLEAIRQMKAEVGDENVVYIHTTLVPYLHAAGEMKTKPTQHSVRELRGLGIQPNILVVRTEAPITDAMRKKIALFCDVTPNAVIESRDVDTIYEIPLRLKAQGMDSLVLDHLHVTAPEADMTEWQQLVNKVNNLKKTINISLVGKYVSLQDAYISVAEALKHAGYPVDADINLSMIDSEKVNEDNVAEILKDADGILVPGGFGDRGIEGMITAIKYARENDVPFLGICLGMQMASVEFARDVLGYKDANSTEMNPNTKHNVIDLMADQADISDMGGTQRLGAYPCKLKTGTVTAEAYENQDVIQERHRHRYEFNNAYREEMEAKGLVFAGTSPDNHLVEVIEIPDKKFFVGAQYHPEFLSRPNRPEGLFKAFVAAANDVHDAK","length":536,"molWeight":59331,"crc64":"A4C0C7252C33C49E","md5":"689A1084DFF24AD5B8BE4E97B715E271"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":1,"Active site":4,"Binding site":17},"uniParcId":"UPI0006F1629D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A166FZA9","uniProtkbId":"A0A166FZA9_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-07-06","entryVersion":38,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL35986.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pyridoxal 5'-phosphate synthase subunit PdxT"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"4.3.3.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pdx2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pyridoxal 5'-phosphate synthase glutaminase subunit"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"3.5.1.2"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"pdxT"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL35986.1"}],"value":"TY91_14540"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054599"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS"}],"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"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + phosphate + 3 H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31507"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58273"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:59776"},{"database":"ChEBI","id":"CHEBI:597326"}],"ecNumber":"4.3.3.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047992"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00064749"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"In the presence of PdxS, forms a dodecamer of heterodimers. Only shows activity in the heterodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008345"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Belongs to the glutaminase PdxT/SNO family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00480"}],"value":"Belongs to the glutamine amidotransferase pdxT/SNO family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL35986.1"}],"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":"Active site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Active site","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Active site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Binding site","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00480"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL35986.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL35986.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL35986.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000099","properties":[{"key":"ProteinId","value":"KZL35986.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A166FZA9","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.3666","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9810320at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00245","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000076480","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:1903600","properties":[{"key":"GoTerm","value":"C:glutaminase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036381","properties":[{"key":"GoTerm","value":"F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016740","properties":[{"key":"GoTerm","value":"F:transferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006543","properties":[{"key":"GoTerm","value":"P:L-glutamine catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042823","properties":[{"key":"GoTerm","value":"P:pyridoxal 5'-phosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008614","properties":[{"key":"GoTerm","value":"P:pyridoxine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01749","properties":[{"key":"EntryName","value":"GATase1_PB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000010","properties":[{"key":"EntryName","value":"uncharacterized protein LOC100176842 isoform X2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01615","properties":[{"key":"EntryName","value":"PdxT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR002161","properties":[{"key":"EntryName","value":"PdxT/SNO"}]},{"database":"InterPro","id":"IPR021196","properties":[{"key":"EntryName","value":"PdxT/SNO_CS"}]},{"database":"NCBIfam","id":"TIGR03800","properties":[{"key":"EntryName","value":"PLP_synth_Pdx2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31559","properties":[{"key":"EntryName","value":"PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31559:SF0","properties":[{"key":"EntryName","value":"PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01174","properties":[{"key":"EntryName","value":"SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005639","properties":[{"key":"EntryName","value":"Glut_amidoT_SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01236","properties":[{"key":"EntryName","value":"PDXT_SNO_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51130","properties":[{"key":"EntryName","value":"PDXT_SNO_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLIGVLGLQGAVSEHERMLADCGAKTRRVKTPEDLNGLDGIVVPGGESTAIRKLLVRESMLEPLRDLVAQGLPTFGTCAGMVLLAQPESLAGIHADVERNGFGRQRESFESDLQVTGWETPFHGVFIRAPYLKSVSAPAEALITLDDGRIVAATEKNVLTTAFHPELTGDKRFHQYFIDEFVKATTKTA","length":189,"molWeight":20532,"crc64":"E0CD96BCBD87E958","md5":"3379E372093143CDDD4662EDAFC711BF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Active site":5,"Binding site":3},"uniParcId":"UPI0006D16A3F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A166H9U0","uniProtkbId":"A0A166H9U0_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-07-06","entryVersion":43,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41703.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bifunctional protein GlmU"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"UDP-N-acetylglucosamine pyrophosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.7.7.23"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"N-acetylglucosamine-1-phosphate uridyltransferase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Glucosamine-1-phosphate N-acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.3.1.157"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41703.1"}],"value":"TY91_05660"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H(+) = UDP-N-acetyl-alpha-D-glucosamine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13509"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:57705"},{"database":"ChEBI","id":"CHEBI:57776"}],"ecNumber":"2.7.7.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048493"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13725"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57776"},{"database":"ChEBI","id":"CHEBI:58516"}],"ecNumber":"2.3.1.157","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048247"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bacterial outer membrane biogenesis; LPS lipid A biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005166"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005208"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007707"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the C-terminal section; belongs to the transferase hexapeptide repeat family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007947"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41703.1"}],"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":220,"modifier":"EXACT"}},"description":"Nucleotidyl transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00483"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Active site","location":{"start":{"value":363,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":351,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":377,"modifier":"EXACT"},"end":{"value":377,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":386,"modifier":"EXACT"},"end":{"value":387,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":405,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":423,"modifier":"EXACT"},"end":{"value":423,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":440,"modifier":"EXACT"},"end":{"value":440,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41703.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41703.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000034","properties":[{"key":"ProteinId","value":"KZL41703.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056997359.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000034.1"}]},{"database":"AlphaFoldDB","id":"A0A166H9U0","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.1677","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9775031at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00113","properties":[{"key":"RectionId","value":"UER00532"}]},{"database":"UniPathway","id":"UPA00973","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000076480","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:0019134","properties":[{"key":"GoTerm","value":"F:glucosamine-1-phosphate N-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003977","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylglucosamine diphosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000902","properties":[{"key":"GoTerm","value":"P:cell morphogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009245","properties":[{"key":"GoTerm","value":"P:lipid A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006048","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylglucosamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd02540","properties":[{"key":"EntryName","value":"GT2_GlmU_N_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03353","properties":[{"key":"EntryName","value":"LbH_GlmU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.10.10","properties":[{"key":"EntryName","value":"Hexapeptide repeat proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01631","properties":[{"key":"EntryName","value":"GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005882","properties":[{"key":"EntryName","value":"Bifunctional_GlmU"}]},{"database":"InterPro","id":"IPR050065","properties":[{"key":"EntryName","value":"GlmU-like"}]},{"database":"InterPro","id":"IPR038009","properties":[{"key":"EntryName","value":"GlmU_C_LbH"}]},{"database":"InterPro","id":"IPR001451","properties":[{"key":"EntryName","value":"Hexapep"}]},{"database":"InterPro","id":"IPR018357","properties":[{"key":"EntryName","value":"Hexapep_transf_CS"}]},{"database":"InterPro","id":"IPR005835","properties":[{"key":"EntryName","value":"NTP_transferase_dom"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"NCBIfam","id":"NF010934","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01173","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584:SF3","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN GLMU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584","properties":[{"key":"EntryName","value":"NUCLEOTIDYL TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00132","properties":[{"key":"EntryName","value":"Hexapep"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14602","properties":[{"key":"EntryName","value":"Hexapep_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00483","properties":[{"key":"EntryName","value":"NTP_transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00101","properties":[{"key":"EntryName","value":"HEXAPEP_TRANSFERASES"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSTRNTIILAAGKGTRMKSKLYKVLHKVCGRSMVDHVLTQVEKTNMDRIVTVVGYGAEKVEDTLHDRTEYVLQKEQLGTGHAVLQTEPLLKNQDGTTLVVSGDTPLFQAQTFENLFKYHEAKKAMATVLTSKAPDPTGYGRIVRNEVGIVEKIVEQKDASEKEQEIDEINTGVYVFDNKALFAALHEIKNDNAQGEYYLTDVIEILKNRGDIVAAYRMNDFEESMGVNDRVALSKATKVMQRRINEAHMRNGVTLINPEDTYIDVDVKIGADTIIEPGVLLKGKTVIGDDCFIGAHSEIHDSTIHNNVTVTSSYIEDSEMDEGSNIGPMSHLRPESKIGPKVHLGNFVEVKKATIDEGTKVGHLTYVGNAHLGKRINVGCGVVFVNYDGAHKHDTTVGDDAFIGSNSNLVAPLTVADHSFIAAGSTITDEVEQYDMAIARARQTNKPGYFKKLPYDPENE","length":460,"molWeight":50723,"crc64":"47ABBE41FBBFEC73","md5":"95488B646DDDB1173BA09BEC6A8106FA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":3,"Active site":1,"Binding site":19},"uniParcId":"UPI0006EFBF0F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161V5X7","uniProtkbId":"A0A161V5X7_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-07-06","entryVersion":29,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41137.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Carbamoyl phosphate synthase small chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"6.3.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Carbamoyl phosphate synthetase glutamine chain"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"carA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41137.1"}],"value":"TY91_07850"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Small subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The small subunit (glutamine amidotransferase) binds and cleaves glutamine to supply the large subunit with the substrate ammonia"}],"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"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}]}},{"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"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005077"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007800"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Belongs to the CarA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41137.1"}],"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":2,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"Carbamoyl-phosphate synthase small subunit N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM01097"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"CPSase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}]},{"type":"Active site","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}]},{"type":"Binding site","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41137.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41137.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000038","properties":[{"key":"ProteinId","value":"KZL41137.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_063285412.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000038.1"}]},{"database":"AlphaFoldDB","id":"A0A161V5X7","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.2137","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9804328at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00068","properties":[{"key":"RectionId","value":"UER00171"}]},{"database":"UniPathway","id":"UPA00070","properties":[{"key":"RectionId","value":"UER00115"}]},{"database":"Proteomes","id":"UP000076480","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"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:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd01744","properties":[{"key":"EntryName","value":"GATase1_CPSase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.30.20","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase small subunit, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01209","properties":[{"key":"EntryName","value":"CPSase_S_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050472","properties":[{"key":"EntryName","value":"Anth_synth/Amidotransfase"}]},{"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":"IPR035686","properties":[{"key":"EntryName","value":"CPSase_GATase1"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"NCBIfam","id":"TIGR01368","properties":[{"key":"EntryName","value":"CPSaseIIsmall"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009475","properties":[{"key":"EntryName","value":"PRK12838.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43418:SF7","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE SMALL CHAIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43418","properties":[{"key":"EntryName","value":"MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED"},{"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":"PRINTS","id":"PR00099","properties":[{"key":"EntryName","value":"CPSGATASE"}]},{"database":"PRINTS","id":"PR00096","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"SMART","id":"SM01097","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"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":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTQRFLILEDGSSYPGEGFGAGATTTGELVFNTSMLGYQEIVTNQIYHNQIIVFSQPTIGSIGITHDSYESILPTAKGMVVRDVSDISKNRQRSLSLDQFLKQHNIPGISGIDTRHLIRQIQKNGTMKGSIVDVDDDHAFDQLHATVLTNQQVAQVATPVPYPNPNSGYNVVVVDFGLKHGILRQLSRRKCNVTVLPWNTDAQSIISLDPDGVILSTGPGSPLDLPESVLEMIRTIQERIPLFAIGLGHELFALANGAEVTALPVAHHGASHPIRKIITNEIIYALEGQEFVVDGESVDRDRLITTYRDLIDSSIQGLRHRDYPAFSVQFFPDGAPGPNDSVDLFDEFIEIMGTREGLHG","length":360,"molWeight":39521,"crc64":"ABF7EA52948CA06A","md5":"6470DFB96B7CB47590D51DED3ECC02A9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":1,"Active site":1,"Binding site":4},"uniParcId":"UPI0007AE5003"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161V611","uniProtkbId":"A0A161V611_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-07-06","entryVersion":34,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41177.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Signal recognition particle receptor FtsY"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"SRP receptor"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"3.6.5.4"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"ftsY"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41177.1"}],"value":"TY91_08075"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + H2O = GDP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19669"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58189"}],"ecNumber":"3.6.5.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Belongs to the GTP-binding SRP family. FtsY subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41177.1"}],"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":474,"modifier":"EXACT"},"end":{"value":487,"modifier":"EXACT"}},"description":"SRP54-type proteins GTP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS00300"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":307,"modifier":"EXACT"},"end":{"value":314,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":389,"modifier":"EXACT"},"end":{"value":393,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":453,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41177.1"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41177.1"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023170"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0675","category":"Molecular function","name":"Receptor"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41177.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41177.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000038","properties":[{"key":"ProteinId","value":"KZL41177.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056996235.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000038.1"}]},{"database":"AlphaFoldDB","id":"A0A161V611","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.2185","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9804720at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000076480","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:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003924","properties":[{"key":"GoTerm","value":"F:GTPase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005047","properties":[{"key":"GoTerm","value":"F:signal recognition particle binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006614","properties":[{"key":"GoTerm","value":"P:SRP-dependent cotranslational protein targeting to membrane"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd17874","properties":[{"key":"EntryName","value":"FtsY"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.120.140:FF:000002","properties":[{"key":"EntryName","value":"Signal recognition particle receptor FtsY"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000053","properties":[{"key":"EntryName","value":"Signal recognition particle receptor FtsY"},{"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":"1.20.120.140","properties":[{"key":"EntryName","value":"Signal recognition particle SRP54, nucleotide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00920","properties":[{"key":"EntryName","value":"FtsY"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR013822","properties":[{"key":"EntryName","value":"Signal_recog_particl_SRP54_hlx"}]},{"database":"InterPro","id":"IPR004390","properties":[{"key":"EntryName","value":"SR_rcpt_FtsY"}]},{"database":"InterPro","id":"IPR036225","properties":[{"key":"EntryName","value":"SRP/SRP_N"}]},{"database":"InterPro","id":"IPR000897","properties":[{"key":"EntryName","value":"SRP54_GTPase_dom"}]},{"database":"InterPro","id":"IPR042101","properties":[{"key":"EntryName","value":"SRP54_N_sf"}]},{"database":"NCBIfam","id":"TIGR00064","properties":[{"key":"EntryName","value":"ftsY"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43134","properties":[{"key":"EntryName","value":"SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43134:SF1","properties":[{"key":"EntryName","value":"SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00448","properties":[{"key":"EntryName","value":"SRP54"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02881","properties":[{"key":"EntryName","value":"SRP54_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00962","properties":[{"key":"EntryName","value":"SRP54"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00963","properties":[{"key":"EntryName","value":"SRP54_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47364","properties":[{"key":"EntryName","value":"Domain of the SRP/SRP receptor G-proteins"},{"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":"PS00300","properties":[{"key":"EntryName","value":"SRP54"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGLFDFFKRRSKADEEKKTEQLVNTEASAAAEPKPDTAPAAEPESESGDRTVKAPSEAETRVPDETDTADQDAPATPVTTPLTSTEDAPEPASVKDEPASSGTSAAPVQTSETVHDTPATDAFKTPADQQAEETAQAPEPVAEPAQAAPTEKTETTAGIETPAVTPTKGDAPVTPSTDVTSQSADEAVSTPEQTPSDAERYDKGLEKSRETFGDRLNHLLANFRHVDESFFDDLEETLIGADVGYEAAMQISDQLRDEVKLQNAKKPKDVQNVVVEKLIDLYDAAGTEENNDLNFADKGPTVILFVGVNGVGKTTTIGKMANLFKQQGKKVLLAAADTFRAGAIEQLNVWAKRDGVDIVMKPEKSDPSAVVFDAVKKAKAEDYDILFVDTAGRLQNKANLMNELAKMKRVISREIPDAPHEVLLVLDSTTGQNALNQAKLFKETTDVTGIVLTKLDGTARGGIVLAIRNELHLPVKYVGLGEQVDDLRPFEPTEFVYGLFKGLIDVK","length":507,"molWeight":54591,"crc64":"3A8747F9E2D2D78F","md5":"A61E9897C634E74EB29BF27C90703C4A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":6,"Binding site":3},"uniParcId":"UPI0006EFF961"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161V6B1","uniProtkbId":"A0A161V6B1_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-07-06","entryVersion":41,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41481.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"value":"Alanine--tRNA ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"value":"6.1.1.7"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"value":"Alanyl-tRNA synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"value":"AlaRS"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41481.1"}],"value":"alaS"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41481.1"}],"value":"TY91_06940"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024779"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"value":"Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"tRNA(Ala) + L-alanine + ATP = L-alanyl-tRNA(Ala) + AMP + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12540"},{"database":"Rhea","id":"RHEA-COMP:9657"},{"database":"Rhea","id":"RHEA-COMP:9923"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57972"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78497"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.1.1.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048300"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"value":"Binds 1 zinc ion per subunit."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"value":"Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008226"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"value":"Belongs to the class-II aminoacyl-tRNA synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41481.1"}],"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":713,"modifier":"EXACT"}},"description":"Alanyl-transfer RNA synthetases family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50860"}]},{"type":"Coiled coil","location":{"start":{"value":730,"modifier":"EXACT"},"end":{"value":764,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Binding site","location":{"start":{"value":568,"modifier":"EXACT"},"end":{"value":568,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":572,"modifier":"EXACT"},"end":{"value":572,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":670,"modifier":"EXACT"},"end":{"value":670,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":674,"modifier":"EXACT"},"end":{"value":674,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023146"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"id":"KW-0030","category":"Molecular function","name":"Aminoacyl-tRNA synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"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":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022917"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022555"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"id":"KW-0820","category":"Molecular function","name":"tRNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00036"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41481.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41481.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000036","properties":[{"key":"ProteinId","value":"KZL41481.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_063285376.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000036.1"}]},{"database":"AlphaFoldDB","id":"A0A161V6B1","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.1943","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9803884at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000076480","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:0004813","properties":[{"key":"GoTerm","value":"F:alanine-tRNA ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002161","properties":[{"key":"GoTerm","value":"F:aminoacyl-tRNA deacylase activity"},{"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:0140096","properties":[{"key":"GoTerm","value":"F:catalytic activity, acting on a protein"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0003676","properties":[{"key":"GoTerm","value":"F:nucleic acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006419","properties":[{"key":"GoTerm","value":"P:alanyl-tRNA aminoacylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00673","properties":[{"key":"EntryName","value":"AlaRS_core"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.310.40:FF:000001","properties":[{"key":"EntryName","value":"Alanine--tRNA ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.930.10:FF:000046","properties":[{"key":"EntryName","value":"Alanine--tRNA ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.980.10:FF:000004","properties":[{"key":"EntryName","value":"Alanine--tRNA ligase, cytoplasmic"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.30.130","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.310.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.54.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.250.550","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.930.10","properties":[{"key":"EntryName","value":"Bira Bifunctional Protein, Domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.980.10","properties":[{"key":"EntryName","value":"Threonyl-trna Synthetase, Chain A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00036_B","properties":[{"key":"EntryName","value":"Ala_tRNA_synth_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR045864","properties":[{"key":"EntryName","value":"aa-tRNA-synth_II/BPL/LPL"}]},{"database":"InterPro","id":"IPR002318","properties":[{"key":"EntryName","value":"Ala-tRNA-lgiase_IIc"}]},{"database":"InterPro","id":"IPR018162","properties":[{"key":"EntryName","value":"Ala-tRNA-ligase_IIc_anticod-bd"}]},{"database":"InterPro","id":"IPR018165","properties":[{"key":"EntryName","value":"Ala-tRNA-synth_IIc_core"}]},{"database":"InterPro","id":"IPR018164","properties":[{"key":"EntryName","value":"Ala-tRNA-synth_IIc_N"}]},{"database":"InterPro","id":"IPR023033","properties":[{"key":"EntryName","value":"Ala_tRNA_ligase_euk/bac"}]},{"database":"InterPro","id":"IPR003156","properties":[{"key":"EntryName","value":"DHHA1_dom"}]},{"database":"InterPro","id":"IPR018163","properties":[{"key":"EntryName","value":"Thr/Ala-tRNA-synth_IIc_edit"}]},{"database":"InterPro","id":"IPR009000","properties":[{"key":"EntryName","value":"Transl_B-barrel_sf"}]},{"database":"InterPro","id":"IPR012947","properties":[{"key":"EntryName","value":"tRNA_SAD"}]},{"database":"NCBIfam","id":"TIGR00344","properties":[{"key":"EntryName","value":"alaS"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11777:SF9","properties":[{"key":"EntryName","value":"ALANINE--TRNA LIGASE, CYTOPLASMIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11777","properties":[{"key":"EntryName","value":"ALANYL-TRNA SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02272","properties":[{"key":"EntryName","value":"DHHA1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01411","properties":[{"key":"EntryName","value":"tRNA-synt_2c"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07973","properties":[{"key":"EntryName","value":"tRNA_SAD"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00980","properties":[{"key":"EntryName","value":"TRNASYNTHALA"}]},{"database":"SMART","id":"SM00863","properties":[{"key":"EntryName","value":"tRNA_SAD"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55681","properties":[{"key":"EntryName","value":"Class II aaRS and biotin synthetases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF101353","properties":[{"key":"EntryName","value":"Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55186","properties":[{"key":"EntryName","value":"ThrRS/AlaRS common domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50447","properties":[{"key":"EntryName","value":"Translation proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50860","properties":[{"key":"EntryName","value":"AA_TRNA_LIGASE_II_ALA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKQLSSSQIRQMYLDFFKSKGHTIEPSASLVPVDDPTLLWINSGVATMKKYFNGSVVPKNPRLTSSQKSIRTNDIENVGRTARHHTLFEMLGNFSVGDYFKKEAITWAWELLTSDDWFGWDPELLYMTVYPQDDDAKQFWQEAGVQPDHIIEAEDNFWDIGEGPSGPDSEIFYDRGKSFNNLADDDPENYPGGENERYLEVWNIVFSQFNHEPDGSYKPLPRKNIDTGMGLERVVSVFQNAKTNFETDLFLPMINATEDFSDGKKYNADPKLDISFKVIADHSRAITFAIGDGALPSNDGRGYVIRRLIRRAVVNGRKLGINGAFLYKLVPVVGEVMKSYYPEVLEQADYIAKVVKSEEDRFNETLTDGLALLNDLVAKTKKSGAKEIDGADAFKLYDTYGFPVELTREYTLDEGITVDEDGFKAEMKKQQDRARNARSKNESMGVQSDLLINVKSASEYVGYTQLDVKAAKVTDIVADGALVDGAETGTVQVVFDKTPFYAEMGGQIADQGDVLAADGSVAATVADVQHAPNGQNLHTLKLQQPMHVGDTFELKVDAAFHSKVEKNHTATHLLDQALRNVFGGHTQQAGSLVEPNYLRFDFTHFGQVTEDDLAKVEAIVNEKIFEEIPVTTVETDQATGKKMGAIALFSDKYGDKVRVVSIGDFSIEFCGGTHVKNTNELGLFKIVSETGIGAGTRRIEAVTAGDAYKYLKGHDDLLTTTATVLKTPQVEEVPAKVAQLQEQIKALTNEKAAVEAKLAGQQADKIFDNVQEINGKQLITGVVQVSSMDQLRQLADTWRQKKLSDVLVLGAQVGEKANLIVAASDDAMKAGIKAGDLIKAISPKINGGGGGRPNLAQAGGKKPAGLNDAMSEAAKWLSNLA","length":881,"molWeight":96733,"crc64":"D11DBE131DB0CB21","md5":"8A7FCF07C0B28729CB4BFB0260DFA515"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Coiled coil":1,"Binding site":4},"uniParcId":"UPI0007AECC1C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161V6K2","uniProtkbId":"A0A161V6K2_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-07-06","entryVersion":41,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41608.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00070926"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"value":"NH(3)-dependent NAD(+) synthetase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00066987"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"value":"6.3.1.5"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"value":"nadE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41608.1"}],"value":"TY91_06310"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00055966"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"value":"Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"deamido-NAD(+) + NH4(+) + ATP = AMP + diphosphate + NAD(+) + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21188"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:58437"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.3.1.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051206"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003812"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"value":"Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005859"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003811"}],"value":"Belongs to the NAD synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41608.1"}],"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":24,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"NAD/GMP synthase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02540"}]},{"type":"Binding site","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58437"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"ligand":{"name":"deamido-NAD(+)","id":"ChEBI:CHEBI:58437","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58437"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"ligand":{"name":"deamido-NAD(+)","id":"ChEBI:CHEBI:58437","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58437"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"ligand":{"name":"deamido-NAD(+)","id":"ChEBI:CHEBI:58437","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58437"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"ligand":{"name":"deamido-NAD(+)","id":"ChEBI:CHEBI:58437","note":"ligand shared between two neighboring subunits"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00193"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41608.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41608.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000035","properties":[{"key":"ProteinId","value":"KZL41608.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056996844.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000035.1"}]},{"database":"AlphaFoldDB","id":"A0A161V6K2","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.1810","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9803818at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00253","properties":[{"key":"RectionId","value":"UER00333"}]},{"database":"Proteomes","id":"UP000076480","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003952","properties":[{"key":"GoTerm","value":"F:NAD+ synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008795","properties":[{"key":"GoTerm","value":"F:NAD+ synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009435","properties":[{"key":"GoTerm","value":"P:NAD+ biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00553","properties":[{"key":"EntryName","value":"NAD_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000015","properties":[{"key":"EntryName","value":"NH(3)-dependent NAD(+) synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00193","properties":[{"key":"EntryName","value":"NadE_ammonia_dep"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022310","properties":[{"key":"EntryName","value":"NAD/GMP_synthase"}]},{"database":"InterPro","id":"IPR003694","properties":[{"key":"EntryName","value":"NAD_synthase"}]},{"database":"InterPro","id":"IPR022926","properties":[{"key":"EntryName","value":"NH(3)-dep_NAD(+)_synth"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"NF001979","properties":[{"key":"EntryName","value":"nadE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00552","properties":[{"key":"EntryName","value":"nadE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23090","properties":[{"key":"EntryName","value":"NH 3 /GLUTAMINE-DEPENDENT NAD + SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23090:SF7","properties":[{"key":"EntryName","value":"NH(3)-DEPENDENT NAD(+) SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02540","properties":[{"key":"EntryName","value":"NAD_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52402","properties":[{"key":"EntryName","value":"Adenine nucleotide alpha hydrolases-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRKLQAEIIDALKVSPSIDPETEIRRSVDFLKAYLKKSGLKGLVLGISGGQDSTLAGKLSELAMTELRHETGSNDYKFIAVRLPYGVQADESDAMKAIDFMDADQVDRVDIKPATDAMTQAVEANSETISDFNKGNIKARERMTAQFAIAGANQAAVVGTDHAAEAVTGFYTKFGDGAADITPLWRLNKRQGKQLLAYLNAPEELYKKVPTADLEDDRPALPDEAALGVRYDDIDDYLEGKTISDKAAETIENWYVKTSHKRHLPINVYDTFWK","length":274,"molWeight":30292,"crc64":"BD69490E3BB683E8","md5":"47555FC8EDFCE9ADB6F3D0C95B9AA16C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":10},"uniParcId":"UPI0006EF004E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161V6Q9","uniProtkbId":"A0A161V6Q9_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-07-06","entryVersion":42,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41702.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Ribose-phosphate pyrophosphokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"RPPK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"2.7.6.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"5-phospho-D-ribosyl alpha-1-diphosphate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Phosphoribosyl diphosphate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Phosphoribosyl pyrophosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"P-Rib-PP synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"PRPP synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"PRPPase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"prs"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41702.1"}],"value":"TY91_05655"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054914"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P)"}],"commentType":"FUNCTION"},{"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"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Binds 2 Mg(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004996"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"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":"HAMAP-Rule","id":"MF_00583"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061444"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41702.1"}],"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":10,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"Ribose-phosphate pyrophosphokinase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF13793"}]},{"type":"Active site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}]},{"type":"Binding site","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346"}},{"type":"Binding site","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346"}},{"type":"Binding site","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022727"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"id":"KW-0545","category":"Biological process","name":"Nucleotide biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"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_00583"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41702.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41702.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000034","properties":[{"key":"ProteinId","value":"KZL41702.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_054760688.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000034.1"}]},{"database":"AlphaFoldDB","id":"A0A161V6Q9","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.1676","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9777067at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00087","properties":[{"key":"RectionId","value":"UER00172"}]},{"database":"Proteomes","id":"UP000076480","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:0002189","properties":[{"key":"GoTerm","value":"C:ribose phosphate diphosphokinase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004749","properties":[{"key":"GoTerm","value":"F:ribose phosphate diphosphokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006015","properties":[{"key":"GoTerm","value":"P:5-phosphoribose 1-diphosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006164","properties":[{"key":"GoTerm","value":"P:purine nucleotide biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"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:000001","properties":[{"key":"EntryName","value":"Ribose-phosphate pyrophosphokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00583_B","properties":[{"key":"EntryName","value":"RibP_PPkinase_B"},{"key":"MatchStatus","value":"1"}]},{"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":"IPR037515","properties":[{"key":"EntryName","value":"Rib-P_diPkinase_bac"}]},{"database":"NCBIfam","id":"NF002320","properties":[{"key":"EntryName","value":"PRK01259.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002618","properties":[{"key":"EntryName","value":"PRK02269.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01251","properties":[{"key":"EntryName","value":"ribP_PPkin"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10210","properties":[{"key":"EntryName","value":"RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10210:SF41","properties":[{"key":"EntryName","value":"RIBOSE-PHOSPHATE PYROPHOSPHOKINASE 1, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14572","properties":[{"key":"EntryName","value":"Pribosyl_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13793","properties":[{"key":"EntryName","value":"Pribosyltran_N"},{"key":"MatchStatus","value":"1"}]},{"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":"PROSITE","id":"PS00114","properties":[{"key":"EntryName","value":"PRPP_SYNTHASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSEKYNDPKLKIFALNSNKPLAQRIADEVGVDLGKTSVDRFSDGEIRINIEESIRGCHVYVIQSTSAPVNDNLMELLIMVDALRRASAETINVVIPYYGYARQDRKARSREPITAKLVANMLETAGITRVVALDLHAAQIQGFFDVPVDHLMGAPLLADYFINHGIDKDAVVVSPDHGGVTRARALAEFLKAPIAIIDKRRPRANVAEIMNIIGDVKGKRCIMIDDMIDTAGTITLGAQALMDAGASEVYASCTHPVLSGPAIERIANSPIKQLVVTDSIQLPKEKQIDKLKQISVGPLIGDAIKRIYENKPVSPLFHNRFHGAE","length":325,"molWeight":35581,"crc64":"79356B7F06FCC778","md5":"501F0DAD14D98C5246EBCEB4D7B281C0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":7},"uniParcId":"UPI0006D1689F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161V6U1","uniProtkbId":"A0A161V6U1_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-07-06","entryVersion":24,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41769.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"value":"Ethanolamine ammonia-lyase large subunit"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"value":"EAL large subunit"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"value":"4.3.1.7"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"value":"eutB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41769.1"}],"value":"TY91_05505"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"value":"Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of vitamin B12"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ethanolamine = acetaldehyde + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15313"},{"database":"ChEBI","id":"CHEBI:15343"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:57603"}],"ecNumber":"4.3.1.7","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"adenosylcob(III)alamin","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18408"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"value":"Binds between the large and small subunits."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"value":"Amine and polyamine degradation; ethanolamine degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"value":"The basic unit is a heterodimer which dimerizes to form tetramers. The heterotetramers trimerize; 6 large subunits form a core ring with 6 small subunits projecting outwards"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"value":"Bacterial microcompartment","id":"SL-0544"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"value":"Belongs to the EutB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41769.1"}],"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":160,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18408"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"ligand":{"name":"adenosylcob(III)alamin","id":"ChEBI:CHEBI:18408"}},{"type":"Binding site","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18408"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"ligand":{"name":"adenosylcob(III)alamin","id":"ChEBI:CHEBI:18408"}},{"type":"Binding site","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18408"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"ligand":{"name":"adenosylcob(III)alamin","id":"ChEBI:CHEBI:18408"}},{"type":"Binding site","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":401,"modifier":"EXACT"},"end":{"value":401,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18408"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"ligand":{"name":"adenosylcob(III)alamin","id":"ChEBI:CHEBI:18408"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"id":"KW-1283","category":"Cellular component","name":"Bacterial microcompartment"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"id":"KW-0846","category":"Ligand","name":"Cobalamin"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"}],"id":"KW-0170","category":"Ligand","name":"Cobalt"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00861"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41769.1"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41769.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41769.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000033","properties":[{"key":"ProteinId","value":"KZL41769.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056996523.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000033.1"}]},{"database":"AlphaFoldDB","id":"A0A161V6U1","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.1645","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9770909at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00560","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000076480","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:0009350","properties":[{"key":"GoTerm","value":"C:ethanolamine ammonia-lyase complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0031471","properties":[{"key":"GoTerm","value":"C:ethanolamine degradation polyhedral organelle"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0031419","properties":[{"key":"GoTerm","value":"F:cobalamin binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008851","properties":[{"key":"GoTerm","value":"F:ethanolamine ammonia-lyase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006520","properties":[{"key":"GoTerm","value":"P:amino acid metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0046336","properties":[{"key":"GoTerm","value":"P:ethanolamine catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.20.20.70:FF:000055","properties":[{"key":"EntryName","value":"Ethanolamine ammonia-lyase heavy chain"},{"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":"2.30.170.30","properties":[{"key":"EntryName","value":"ethanolamine ammonia-lyase heavy chain domain like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.220.70","properties":[{"key":"EntryName","value":"lyase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00861","properties":[{"key":"EntryName","value":"EutB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR010628","properties":[{"key":"EntryName","value":"EutB"}]},{"database":"InterPro","id":"IPR044939","properties":[{"key":"EntryName","value":"EutB_dom_2_sf"}]},{"database":"InterPro","id":"IPR044941","properties":[{"key":"EntryName","value":"EutB_N_sf"}]},{"database":"NCBIfam","id":"NF011649","properties":[{"key":"EntryName","value":"eutB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR39329","properties":[{"key":"EntryName","value":"ETHANOLAMINE AMMONIA-LYASE HEAVY CHAIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR39329:SF1","properties":[{"key":"EntryName","value":"ETHANOLAMINE AMMONIA-LYASE LARGE SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06751","properties":[{"key":"EntryName","value":"EutB"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF018788","properties":[{"key":"EntryName","value":"EutB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MILKVTLSGKRYTFRTVKEVMAKANEEKSGDLLAGIAAASMQERVAAKVVLSQLTLDDIYNHPGVDYDKDEVTRMIIDDIDADVFSQIKRWTVEQLREWLLALDTDNQKIHYISRGLTSEMIAAVCKLMTNMDLVMAAKKITNEKTANTTIGCPGTFSSRLQPNHPADDVRGIMASTMEGLSMGVGDAVIGVNPVTDSVDNVTEILKQFHDFISKWQVPTQTCVLAHVTTQMAAIEQGAPAGLIFQSIAGSEKGNTAFGINAKMIAEANRMGHEKLETVGPNVMYFETGQGSELSADANFDNDQVTMEARCYGFARHYDPFIVNTVVGFIGPEYLYDAKQVTRAGLEDHFMGKLSGLAMGCDVCYTNHMQADQNDIENLAVLLANAGCTYMMGVPQADDIMLNYQSTGYQETATLRELLGTRPIKQFDAWLERMGITNEGHLTPLAGDASLFLDSVADSVKA","length":462,"molWeight":50589,"crc64":"D7D5C1B185375FA6","md5":"C1128AABCA61475B23721422854A3A5C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Binding site":8},"uniParcId":"UPI0006F09122"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161V6Z7","uniProtkbId":"A0A161V6Z7_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-07-06","entryVersion":27,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42116.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"value":"Ethanolamine ammonia-lyase small subunit"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"value":"EAL small subunit"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"value":"4.3.1.7"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"value":"eutC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42116.1"}],"value":"TY91_05015"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"value":"Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ethanolamine = acetaldehyde + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15313"},{"database":"ChEBI","id":"CHEBI:15343"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:57603"}],"ecNumber":"4.3.1.7","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"adenosylcob(III)alamin","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18408"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"value":"Binds between the large and small subunits."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"value":"Amine and polyamine degradation; ethanolamine degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"value":"The basic unit is a heterodimer which dimerizes to form tetramers. The heterotetramers trimerize; 6 large subunits form a core ring with 6 small subunits projecting outwards"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"value":"Bacterial microcompartment","id":"SL-0544"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"value":"Belongs to the EutC family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42116.1"}],"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":183,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18408"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"ligand":{"name":"adenosylcob(III)alamin","id":"ChEBI:CHEBI:18408"}},{"type":"Binding site","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18408"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"ligand":{"name":"adenosylcob(III)alamin","id":"ChEBI:CHEBI:18408"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024446"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"id":"KW-1283","category":"Cellular component","name":"Bacterial microcompartment"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"id":"KW-0846","category":"Ligand","name":"Cobalamin"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023285"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"id":"KW-0170","category":"Ligand","name":"Cobalt"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00601"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42116.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42116.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000029","properties":[{"key":"ProteinId","value":"KZL42116.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A161V6Z7","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.1483","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"114248at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00560","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000076480","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0009350","properties":[{"key":"GoTerm","value":"C:ethanolamine ammonia-lyase complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0031471","properties":[{"key":"GoTerm","value":"C:ethanolamine degradation polyhedral organelle"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0031419","properties":[{"key":"GoTerm","value":"F:cobalamin binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008851","properties":[{"key":"GoTerm","value":"F:ethanolamine ammonia-lyase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006520","properties":[{"key":"GoTerm","value":"P:amino acid metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0046336","properties":[{"key":"GoTerm","value":"P:ethanolamine catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.40.50.11240","properties":[{"key":"EntryName","value":"Ethanolamine ammonia-lyase light chain (EutC)"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.30.40","properties":[{"key":"EntryName","value":"Ethanolamine ammonia-lyase light chain (EutC), N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00601","properties":[{"key":"EntryName","value":"EutC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR009246","properties":[{"key":"EntryName","value":"EutC"}]},{"database":"InterPro","id":"IPR042251","properties":[{"key":"EntryName","value":"EutC_C"}]},{"database":"InterPro","id":"IPR042255","properties":[{"key":"EntryName","value":"EutC_N"}]},{"database":"NCBIfam","id":"NF003971","properties":[{"key":"EntryName","value":"eutC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR39330","properties":[{"key":"EntryName","value":"ETHANOLAMINE AMMONIA-LYASE LIGHT CHAIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR39330:SF1","properties":[{"key":"EntryName","value":"ETHANOLAMINE AMMONIA-LYASE SMALL SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05985","properties":[{"key":"EntryName","value":"EutC"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF018982","properties":[{"key":"EntryName","value":"EutC"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPMLTPPKIKPIPVDKTGALIDIRAIDQHEILGVTDPVNAEDYLALKRSTTAHLGLGRVGTRYTTRSVLRLRADHAAAKDSVWSDVAPEFVTKMGFIPIQSTCKTETEYLTRPDHGRAIAASALDKVKRAYSKQPRVLIAVGDGLSSAAIEANVAEAIPAIKQGLALAHIDVGPVPFIRFARVATEDYLGEALKADVVCLLIGERPGLVTAKSMSAYIAYRPTVGMPESRRTVISNIHPGGVPAVEAGAYIAEVIQEMLTQKASGLELIAQS","length":272,"molWeight":29112,"crc64":"FB3F08B31292E91C","md5":"31F72F9B1B9EE4600E83F14A18D43263"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Binding site":2},"uniParcId":"UPI0007AE3C8A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161V722","uniProtkbId":"A0A161V722_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-07-06","entryVersion":41,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42373.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"value":"Lipoyl synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"value":"2.8.1.8"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"value":"Lip-syn"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"value":"LS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"value":"Lipoate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"value":"Lipoic acid synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"value":"Sulfur insertion protein LipA"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"value":"lipA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42373.1"}],"value":"TY91_04875"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"value":"Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine + 4 H(+) = [[Fe-S] cluster scaffold protein] + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 5'-deoxyadenosine + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16585"},{"database":"Rhea","id":"RHEA-COMP:9928"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10475"},{"database":"Rhea","id":"RHEA-COMP:14568"},{"database":"Rhea","id":"RHEA-COMP:14569"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:29034"},{"database":"ChEBI","id":"CHEBI:29919"},{"database":"ChEBI","id":"CHEBI:33722"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:78809"},{"database":"ChEBI","id":"CHEBI:83100"}],"ecNumber":"2.8.1.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047326"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"value":"Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"value":"Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"value":"Belongs to the radical SAM superfamily. Lipoyl synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42373.1"}],"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":56,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Binding site","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}},{"type":"Binding site","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}},{"type":"Binding site","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}},{"type":"Binding site","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00206"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"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_00206"}],"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_00206"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42373.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42373.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000026","properties":[{"key":"ProteinId","value":"KZL42373.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_054762524.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000026.1"}]},{"database":"AlphaFoldDB","id":"A0A161V722","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.1452","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9787898at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00538","properties":[{"key":"RectionId","value":"UER00593"}]},{"database":"Proteomes","id":"UP000076480","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:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016992","properties":[{"key":"GoTerm","value":"F:lipoate synthase activity"},{"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:0009249","properties":[{"key":"GoTerm","value":"P:protein lipoylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00206","properties":[{"key":"EntryName","value":"Lipoyl_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR006638","properties":[{"key":"EntryName","value":"Elp3/MiaA/NifB-like_rSAM"}]},{"database":"InterPro","id":"IPR003698","properties":[{"key":"EntryName","value":"Lipoyl_synth"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"NCBIfam","id":"TIGR00510","properties":[{"key":"EntryName","value":"lipA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004019","properties":[{"key":"EntryName","value":"PRK05481.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009544","properties":[{"key":"EntryName","value":"PRK12928.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10949","properties":[{"key":"EntryName","value":"LIPOYL SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10949:SF0","properties":[{"key":"EntryName","value":"LIPOYL SYNTHASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005963","properties":[{"key":"EntryName","value":"Lipoyl_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00271","properties":[{"key":"EntryName","value":"lipoyl_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01058","properties":[{"key":"EntryName","value":"lipoyl_synthase_like"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00729","properties":[{"key":"EntryName","value":"Elp3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAKHEHAKVAVAATKPTWLKVTYDQKKVDKMEDMLKGMKLNTVCAEANCPNLGECFGSGTASFIILGPNCTRACRFCDIPHGNPQEVDLFEPLRVAQATKKLELSHVVVTSVDRDDLPDLGADQFVRTINAIRELNPDTTIEVLTPDFQGRTDCLDKVIAAKPDVFNHNMETVRSITPKVRNRATYDCSLGVLKYVKEHAPKETYVKTGIMLGLGEKDEEVYQLMDDLRAVDVDFLTIGQYVQPGPKNYRLREWVPMERYQKYYKEAMSRGFKFVASSPLVRSSYKAKEELEAVYNK","length":297,"molWeight":33607,"crc64":"9DE2F39FB8EEFA5F","md5":"6C6AB601117C19A0BEC842E84259396A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":10},"uniParcId":"UPI0006CF41AA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161V779","uniProtkbId":"A0A161V779_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-07-06","entryVersion":40,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42533.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"value":"Thiamine-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"value":"TP synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"value":"TPS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"value":"2.5.1.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"value":"Thiamine-phosphate pyrophosphorylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"value":"TMP pyrophosphorylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"value":"TMP-PPase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"value":"thiE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42533.1"}],"value":"TY91_04545"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"value":"Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = thiamine phosphate + CO2 + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47848"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:37575"},{"database":"ChEBI","id":"CHEBI:57841"},{"database":"ChEBI","id":"CHEBI:62890"}],"ecNumber":"2.5.1.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047851"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003826"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = thiamine phosphate + CO2 + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47844"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:37575"},{"database":"ChEBI","id":"CHEBI:57841"},{"database":"ChEBI","id":"CHEBI:62899"}],"ecNumber":"2.5.1.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047883"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003826"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-methyl-5-(2-phosphooxyethyl)-thiazole + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + H(+) = thiamine phosphate + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22328"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:37575"},{"database":"ChEBI","id":"CHEBI:57841"},{"database":"ChEBI","id":"CHEBI:58296"}],"ecNumber":"2.5.1.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047334"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003826"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005165"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004253"}],"value":"Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003826"}],"value":"Belongs to the thiamine-phosphate synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42533.1"}],"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":188,"modifier":"EXACT"}},"description":"Thiamine phosphate synthase/TenI","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02581"}]},{"type":"Binding site","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57841"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"ligand":{"name":"4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine","id":"ChEBI:CHEBI:57841"}},{"type":"Binding site","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57841"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"ligand":{"name":"4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine","id":"ChEBI:CHEBI:57841"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57841"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"ligand":{"name":"4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine","id":"ChEBI:CHEBI:57841"}},{"type":"Binding site","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:62899"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"ligand":{"name":"2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate","id":"ChEBI:CHEBI:62899"}},{"type":"Binding site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57841"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"ligand":{"name":"4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine","id":"ChEBI:CHEBI:57841"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:62899"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"ligand":{"name":"2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate","id":"ChEBI:CHEBI:62899"}},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:62899"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"ligand":{"name":"2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate","id":"ChEBI:CHEBI:62899"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022977"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"id":"KW-0784","category":"Biological process","name":"Thiamine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00097"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42533.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42533.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000024","properties":[{"key":"ProteinId","value":"KZL42533.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_054759118.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000024.1"}]},{"database":"AlphaFoldDB","id":"A0A161V779","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.1380","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9812206at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00060","properties":[{"key":"RectionId","value":"UER00141"}]},{"database":"Proteomes","id":"UP000076480","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004789","properties":[{"key":"GoTerm","value":"F:thiamine-phosphate diphosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009228","properties":[{"key":"GoTerm","value":"P:thiamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009229","properties":[{"key":"GoTerm","value":"P:thiamine diphosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00564","properties":[{"key":"EntryName","value":"TMP_TenI"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000096","properties":[{"key":"EntryName","value":"Thiamine-phosphate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00097","properties":[{"key":"EntryName","value":"TMP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR036206","properties":[{"key":"EntryName","value":"ThiamineP_synth_sf"}]},{"database":"InterPro","id":"IPR022998","properties":[{"key":"EntryName","value":"ThiamineP_synth_TenI"}]},{"database":"InterPro","id":"IPR034291","properties":[{"key":"EntryName","value":"TMP_synthase"}]},{"database":"NCBIfam","id":"TIGR00693","properties":[{"key":"EntryName","value":"thiE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20857","properties":[{"key":"EntryName","value":"THIAMINE-PHOSPHATE PYROPHOSPHORYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20857:SF15","properties":[{"key":"EntryName","value":"THIAMINE-PHOSPHATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02581","properties":[{"key":"EntryName","value":"TMP-TENI"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51391","properties":[{"key":"EntryName","value":"Thiamin phosphate synthase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MELTNKPLYLVTDRTGLTDNVFFQRLDLACQAGVDLVQLREKNLESRDYFQLAQRVKTITDRYAVPLVIDDRLDIAEAVEAAGVHVGQSDLPVAVVRQILGPDKLIGVTAKTVAQADLAVTEGADYLGVGAIFPTTTHVKTVRISVETLAEIKKRVPIPVYAIGGLKAHNVAVIQPAHVDGVAVVSAIMQAPDTVAETKALRTAVLKAL","length":209,"molWeight":22457,"crc64":"CB47C5F9597E9F48","md5":"C006DB1BDEEC46104B09C03A2C5DBC77"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":9},"uniParcId":"UPI0006CFCBD7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161V7I9","uniProtkbId":"A0A161V7I9_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-07-06","entryVersion":35,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42655.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"D-aminoacyl-tRNA deacylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"DTD"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"3.1.1.96"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"Gly-tRNA(Ala) deacylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"3.1.1.-"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"dtd"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42655.1"}],"value":"TY91_04160"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a D-aminoacyl-tRNA + H2O = a tRNA + a D-alpha-amino acid + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13953"},{"database":"Rhea","id":"RHEA-COMP:10123"},{"database":"Rhea","id":"RHEA-COMP:10124"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:59871"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:79333"}],"ecNumber":"3.1.1.96","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"glycyl-tRNA(Ala) + H2O = tRNA(Ala) + glycine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53744"},{"database":"Rhea","id":"RHEA-COMP:9657"},{"database":"Rhea","id":"RHEA-COMP:13640"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78522"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009673"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"value":"Belongs to the DTD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42655.1"}],"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":"Motif","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"Gly-cisPro motif, important for rejection of L-amino acids","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022555"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00518"}],"id":"KW-0820","category":"Molecular function","name":"tRNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42655.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42655.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000022","properties":[{"key":"ProteinId","value":"KZL42655.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_054762627.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000022.1"}]},{"database":"AlphaFoldDB","id":"A0A161V7I9","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.1297","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9801395at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000076480","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:0051500","properties":[{"key":"GoTerm","value":"F:D-tyrosyl-tRNA(Tyr) deacylase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0106026","properties":[{"key":"GoTerm","value":"F:Gly-tRNA(Ala) deacylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043908","properties":[{"key":"GoTerm","value":"F:Ser(Gly)-tRNA(Ala) hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019478","properties":[{"key":"GoTerm","value":"P:D-amino acid catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00563","properties":[{"key":"EntryName","value":"Dtyr_deacylase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.50.80.10:FF:000001","properties":[{"key":"EntryName","value":"D-aminoacyl-tRNA deacylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.80.10","properties":[{"key":"EntryName","value":"D-tyrosyl-tRNA(Tyr) deacylase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00518","properties":[{"key":"EntryName","value":"Deacylase_Dtd"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003732","properties":[{"key":"EntryName","value":"Daa-tRNA_deacyls_DTD"}]},{"database":"InterPro","id":"IPR023509","properties":[{"key":"EntryName","value":"DTD-like_sf"}]},{"database":"NCBIfam","id":"TIGR00256","properties":[{"key":"EntryName","value":"D-aminoacyl-tRNA deacylase"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10472:SF5","properties":[{"key":"EntryName","value":"D-AMINOACYL-TRNA DEACYLASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10472","properties":[{"key":"EntryName","value":"D-TYROSYL-TRNA TYR DEACYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02580","properties":[{"key":"EntryName","value":"Tyr_Deacylase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF69500","properties":[{"key":"EntryName","value":"DTD-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRVVLQRVSSASVSIDEKQVGAINQGYMLLVGAEDTDGAEEIDYLVRKISRLRVFSDDAGKMNLSIQDIHGSILSVSQFTLYADTKKGNRPSFVKAGNPDHADKIYQQFNTQLKQEGIPVETGEFGADMQVSLVNDGPVTIVFDTDNK","length":148,"molWeight":16254,"crc64":"13FD3B6A7F9D60BB","md5":"80828B8FC47F2817112727DE70782C2C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Motif":1},"uniParcId":"UPI0006D1D0A3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161V7S6","uniProtkbId":"A0A161V7S6_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-07-06","entryVersion":37,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42765.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015655"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"}],"value":"UDP-N-acetylmuramoylalanine--D-glutamate ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012212"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"}],"value":"6.3.2.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032324"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"}],"value":"D-glutamic acid-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030398"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"}],"value":"UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42765.1"}],"value":"murD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42765.1"}],"value":"TY91_03650"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002734"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003664"}],"value":"Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanine + D-glutamate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16429"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29986"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:83898"},{"database":"ChEBI","id":"CHEBI:83900"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.9","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047632"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003664"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004752"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003664"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003664"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010416"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"}],"value":"Belongs to the MurCDEF family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42765.1"}],"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":118,"modifier":"EXACT"},"end":{"value":294,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":316,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Binding site","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003664"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003664"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00639"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42765.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL42765.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000020","properties":[{"key":"ProteinId","value":"KZL42765.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056996715.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000020.1"}]},{"database":"AlphaFoldDB","id":"A0A161V7S6","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.1183","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9809796at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00219","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000076480","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:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008764","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051301","properties":[{"key":"GoTerm","value":"P:cell division"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008360","properties":[{"key":"GoTerm","value":"P:regulation of cell shape"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"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":"HAMAP","id":"MF_00639","properties":[{"key":"EntryName","value":"MurD"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"InterPro","id":"IPR005762","properties":[{"key":"EntryName","value":"MurD"}]},{"database":"NCBIfam","id":"TIGR01087","properties":[{"key":"EntryName","value":"murD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43692","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43692:SF1","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21799","properties":[{"key":"EntryName","value":"MurD-like_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51984","properties":[{"key":"EntryName","value":"MurCD N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKAIKTYQGKKVIVVGLAKSGFNAAKLLHQLGAVVTVSDQQPLDKNTEAQELTATGNFTVLTGKQTPDQLDAGFDLMVKNPGIPYDVPIVQAALEQKLPIITEIELASEINEAELIAVTGSNGKTTTTTMITKMLNQERTAGRSAYAGNIGIPASKVAETMTSDDTLVLETSSFMLLGVTAFHPHVAVLINIFSNHLDYHKTRENYVKAKMRITMNQTADDYFVVNFDSKELIGLSKQSKAKIVPFSREGVTHEGAYESDGNLYFKDELVMAAADIKVPGDHNVENALAAIAVAKIHGKSNEAIKHVLTTFGGVRHRTQYVLTSEGRQFYNDSKATDMEATEMALKGFKQPVVLLAGGLDRGYTFERLVPFFKAHVKGIVLFGETKDLLKDAAEQAGVPTIKMSENAETAVPTAYEMSAPGDVILLSPANASWDQYPNFEVRGDKFIQAVETLTGKKEEQ","length":460,"molWeight":50093,"crc64":"6F51BD8D09269C0E","md5":"2837D94EFBA20C243A6BC6E2A58AD992"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Binding site":1},"uniParcId":"UPI0006F10729"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161V8G3","uniProtkbId":"A0A161V8G3_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-07-06","entryVersion":34,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL43065.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"value":"3-dehydroquinate dehydratase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"value":"3-dehydroquinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"value":"4.2.1.10"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"value":"Type I DHQase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"value":"Type I dehydroquinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"value":"DHQ1"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"value":"aroD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL43065.1"}],"value":"TY91_01810"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"value":"Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate"}],"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":"ARBA","id":"ARBA00001864"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"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_00214"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"value":"Belongs to the type-I 3-dehydroquinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL43065.1"}],"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":"Active site","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}]},{"type":"Active site","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}]},{"type":"Binding site","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:32364"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"ligand":{"name":"3-dehydroquinate","id":"ChEBI:CHEBI:32364"}},{"type":"Binding site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:32364"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"ligand":{"name":"3-dehydroquinate","id":"ChEBI:CHEBI:32364"}},{"type":"Binding site","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:32364"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"ligand":{"name":"3-dehydroquinate","id":"ChEBI:CHEBI:32364"}},{"type":"Binding site","location":{"start":{"value":233,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:32364"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"ligand":{"name":"3-dehydroquinate","id":"ChEBI:CHEBI:32364"}},{"type":"Binding site","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:32364"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"ligand":{"name":"3-dehydroquinate","id":"ChEBI:CHEBI:32364"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"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_00214"}],"id":"KW-0057","category":"Biological process","name":"Aromatic amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023270"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00214"}],"id":"KW-0704","category":"Ligand","name":"Schiff base"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL43065.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL43065.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000015","properties":[{"key":"ProteinId","value":"KZL43065.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_054759130.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000015.1"}]},{"database":"AlphaFoldDB","id":"A0A161V8G3","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.736","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"UniPathway","id":"UPA00053","properties":[{"key":"RectionId","value":"UER00086"}]},{"database":"Proteomes","id":"UP000076480","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0003855","properties":[{"key":"GoTerm","value":"F:3-dehydroquinate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046279","properties":[{"key":"GoTerm","value":"P:3,4-dihydroxybenzoate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"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":"FunFam","id":"3.20.20.70:FF:000047","properties":[{"key":"EntryName","value":"3-dehydroquinate dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00214","properties":[{"key":"EntryName","value":"AroD"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR001381","properties":[{"key":"EntryName","value":"DHquinase_I"}]},{"database":"InterPro","id":"IPR050146","properties":[{"key":"EntryName","value":"Type-I_3-dehydroquinase"}]},{"database":"NCBIfam","id":"TIGR01093","properties":[{"key":"EntryName","value":"aroD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43699","properties":[{"key":"EntryName","value":"3-DEHYDROQUINATE DEHYDRATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43699:SF1","properties":[{"key":"EntryName","value":"3-DEHYDROQUINATE DEHYDRATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01487","properties":[{"key":"EntryName","value":"DHquinase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51569","properties":[{"key":"EntryName","value":"Aldolase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MANPTVKVGNTVLGSGRPKIAVPITGKTEEDILTQAADIKAAQPDVVEWRIDFFEGVLDASALAQTGKKLHDAIGDLALLTTFRTNGEGGELVLDDAGYFQVCENVIAGQFTDALDVERYHEESAVKGIIEKAHAQKVVIIMSNHDFDKTPAEDDIVGRLTSMVEYGADVAKMAVMPNSVQDVITLLKATHRASLSLSKPIITMSMGDLGKVSRMAGEVFGSSLSFGTVGAASAPGQVALDHLKVELEDLKLS","length":253,"molWeight":26880,"crc64":"FB91C26CB94696A3","md5":"78CE72D3D4068FFAFD16A7F7363E70BD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Active site":2,"Binding site":5},"uniParcId":"UPI0006D16FDE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161V8R9","uniProtkbId":"A0A161V8R9_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-07-06","entryVersion":39,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL43205.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"value":"3-phosphoshikimate 1-carboxyvinyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"value":"2.5.1.19"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"value":"5-enolpyruvylshikimate-3-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"value":"EPSP synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"value":"EPSPS"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"value":"aroA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL43205.1"}],"value":"TY91_00950"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"value":"Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate"}],"commentType":"FUNCTION"},{"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"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004811"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"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_00210"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009948"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"value":"Belongs to the EPSP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL43205.1"}],"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":424,"modifier":"EXACT"}},"description":"Enolpyruvate transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00275"}]},{"type":"Active site","location":{"start":{"value":314,"modifier":"EXACT"},"end":{"value":314,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}]},{"type":"Binding site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:145989"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"ligand":{"name":"3-phosphoshikimate","id":"ChEBI:CHEBI:145989"}},{"type":"Binding site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58702"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"ligand":{"name":"phosphoenolpyruvate","id":"ChEBI:CHEBI:58702"}},{"type":"Binding site","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:145989"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"ligand":{"name":"3-phosphoshikimate","id":"ChEBI:CHEBI:145989"}},{"type":"Binding site","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:145989"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"ligand":{"name":"3-phosphoshikimate","id":"ChEBI:CHEBI:145989"}},{"type":"Binding site","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58702"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"ligand":{"name":"phosphoenolpyruvate","id":"ChEBI:CHEBI:58702"}},{"type":"Binding site","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58702"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"ligand":{"name":"phosphoenolpyruvate","id":"ChEBI:CHEBI:58702"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:145989"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"ligand":{"name":"3-phosphoshikimate","id":"ChEBI:CHEBI:145989"}},{"type":"Binding site","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:145989"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"ligand":{"name":"3-phosphoshikimate","id":"ChEBI:CHEBI:145989"}},{"type":"Binding site","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58702"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"ligand":{"name":"phosphoenolpyruvate","id":"ChEBI:CHEBI:58702"}},{"type":"Binding site","location":{"start":{"value":314,"modifier":"EXACT"},"end":{"value":314,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:145989"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"ligand":{"name":"3-phosphoshikimate","id":"ChEBI:CHEBI:145989"}},{"type":"Binding site","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:145989"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"ligand":{"name":"3-phosphoshikimate","id":"ChEBI:CHEBI:145989"}},{"type":"Binding site","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58702"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"ligand":{"name":"phosphoenolpyruvate","id":"ChEBI:CHEBI:58702"}},{"type":"Binding site","location":{"start":{"value":389,"modifier":"EXACT"},"end":{"value":389,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58702"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"ligand":{"name":"phosphoenolpyruvate","id":"ChEBI:CHEBI:58702"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"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_00210"}],"id":"KW-0057","category":"Biological process","name":"Aromatic amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00210"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"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_00210"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL43205.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL43205.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000010","properties":[{"key":"ProteinId","value":"KZL43205.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056995969.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000010.1"}]},{"database":"AlphaFoldDB","id":"A0A161V8R9","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.42","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9809920at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00053","properties":[{"key":"RectionId","value":"UER00089"}]},{"database":"Proteomes","id":"UP000076480","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:0003866","properties":[{"key":"GoTerm","value":"F:3-phosphoshikimate 1-carboxyvinyltransferase 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:InterPro"}]},{"database":"GO","id":"GO:0009423","properties":[{"key":"GoTerm","value":"P:chorismate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01556","properties":[{"key":"EntryName","value":"EPSP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.65.10.10:FF:000005","properties":[{"key":"EntryName","value":"3-phosphoshikimate 1-carboxyvinyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.65.10.10","properties":[{"key":"EntryName","value":"Enolpyruvate transferase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00210","properties":[{"key":"EntryName","value":"EPSP_synth"},{"key":"MatchStatus","value":"1"}]},{"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":"IPR013792","properties":[{"key":"EntryName","value":"RNA3'P_cycl/enolpyr_Trfase_a/b"}]},{"database":"NCBIfam","id":"TIGR01356","properties":[{"key":"EntryName","value":"aroA"},{"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":"PF00275","properties":[{"key":"EntryName","value":"EPSP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000505","properties":[{"key":"EntryName","value":"EPSPS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55205","properties":[{"key":"EntryName","value":"EPT/RTPC-like"},{"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"}]}],"sequence":{"value":"MKTLNGKPSTDLHGTLVVPGDKSISHRGIMLGAISEGTTHLSHFLTSADCLSTLAAFQQLGVHIERDGQDVTIHGVGLHGLKPSAQPLDMGNSGTTTRLISGLLAGQSFTSTLIGDASLSKRPMKRVSVPLSEMGANIETTDGHLPMTITGSPLHSVTYQLQVASAQVKSALILAALQADKPSTLVEQLPTRDHTERMLTQFGGDIATAADGVTITVQPQPHLTGQTMTVPGDMSSAAFFMVAASLVPNSKITLKDVGLNKTRTGLLNILQRMGGKVSIDAAPTDGEPIGDLTIETADLHPINIGAADIPAVIDELPLVALLAAKADGISRITGAEELRVKETDRIAAIVQEFTKLGINIEELPDGFVIDGRMPWHVTDNQLDAHDDHRIGMVLGVAGLLVDKPVQLAGADSVRISYPEFFDDLNTLLPKE","length":431,"molWeight":45538,"crc64":"2B3EF36CBFDBE872","md5":"01B303C4BF59B88D7136BA00CA264E24"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":13},"uniParcId":"UPI0006F1822E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161V910","uniProtkbId":"A0A161V910_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2025-10-08","lastSequenceUpdateDate":"2016-07-06","entryVersion":33,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL43325.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012965"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"}],"value":"Histidinol dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"}],"value":"HDH"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012965"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"}],"value":"1.1.1.23"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"}],"value":"hisD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL43325.1"}],"value":"TY91_00360"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003850"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"}],"value":"Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine"}],"commentType":"FUNCTION"},{"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":"HAMAP-Rule","id":"MF_01024"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-4"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-4"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"}],"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":"ARBA00010178"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000099"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004175"}],"value":"Belongs to the histidinol dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL43325.1"}],"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":"Active site","location":{"start":{"value":324,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-1"}]},{"type":"Active site","location":{"start":{"value":325,"modifier":"EXACT"},"end":{"value":325,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-1"}]},{"type":"Binding site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-2"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-2"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-2"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-3"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-4"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-3"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-4"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-3"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":325,"modifier":"EXACT"},"end":{"value":325,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-3"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":358,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-4"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":358,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-3"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":412,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-3"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":417,"modifier":"EXACT"},"end":{"value":417,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-4"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":417,"modifier":"EXACT"},"end":{"value":417,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-3"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"}],"id":"KW-0368","category":"Biological process","name":"Histidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000099-2"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01024"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL43325.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL43325.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000003","properties":[{"key":"ProteinId","value":"KZL43325.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_054761607.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000003.1"}]},{"database":"AlphaFoldDB","id":"A0A161V910","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.1525","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9805269at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00031","properties":[{"key":"RectionId","value":"UER00014"}]},{"database":"Proteomes","id":"UP000076480","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:0004399","properties":[{"key":"GoTerm","value":"F:histidinol dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"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":"FunFam","id":"3.40.50.1980:FF:000001","properties":[{"key":"EntryName","value":"Histidinol dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1980:FF:000026","properties":[{"key":"EntryName","value":"Histidinol dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.5.1300","properties":[{"key":"EntryName","value":"-"},{"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":"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":"IPR001692","properties":[{"key":"EntryName","value":"Histidinol_DH_CS"}]},{"database":"InterPro","id":"IPR022695","properties":[{"key":"EntryName","value":"Histidinol_DH_monofunct"}]},{"database":"InterPro","id":"IPR012131","properties":[{"key":"EntryName","value":"Hstdl_DH"}]},{"database":"NCBIfam","id":"TIGR00069","properties":[{"key":"EntryName","value":"hisD"},{"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":"PIRSF","id":"PIRSF000099","properties":[{"key":"EntryName","value":"Histidinol_dh"},{"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":"PROSITE","id":"PS00611","properties":[{"key":"EntryName","value":"HISOL_DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKILKNQTLDQLLEQVDRQTDQQANQPEVESTVAGIISNVIKNGDDALREYSKKFDKVELTDLRVPQSDIDAAYKNADQDLIDALNLAKNNIISYHKKEIQNGFVDAEQPGVVRGEKITPLAAVGLYVPGGTAAYPSSILMNVIPAKLAGVSKIVMVTPPQKDGIGQAVLTAAKIAGIDEVYQVGGAQAIAALAYGTESIPRVDKITGPGNIFVAVAKKQVFGQVDIDMIAGPSEIGVIADDSANPREVAADLLSQAEHDKLARPMMVTPSEKFAEAVSDQIDEQLKTLPRKEIAGASVQNKGFIAVTDTLDEAFTVMNAISPEHLEIELEDAMQYLNQIKNAGSVFLGFNASEPVGDYVAGPNHILPTGGTARFFSPLGVSDFVKRIQFVTYSKAALKKEEKAITTLARVEGLEAHARAVESRFKD","length":427,"molWeight":45912,"crc64":"FB2AA9F498CA6398","md5":"2B56147ED3C6A18B4239398CB99ED3AB"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Active site":2,"Binding site":14},"uniParcId":"UPI0006D20A81"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161VG90","uniProtkbId":"A0A161VG90_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-07-06","entryVersion":33,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL37154.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"tRNA modification GTPase MnmE"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"3.6.-.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"mnmE"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"trmE"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL37154.1"}],"value":"TY91_13045"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"value":"Binds 1 potassium ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"Homodimer. Heterotetramer of two MnmE and two MnmG subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011043"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003313"}],"value":"Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL37154.1"}],"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":224,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"TrmE-type G","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51709"}]},{"type":"Binding site","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57457"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"(6S)-5-formyl-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57457"}},{"type":"Binding site","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57457"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"(6S)-5-formyl-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57457"}},{"type":"Binding site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57457"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"(6S)-5-formyl-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57457"}},{"type":"Binding site","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":238,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":239,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":238,"modifier":"EXACT"},"end":{"value":238,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":281,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":338,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":364,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":463,"modifier":"EXACT"},"end":{"value":463,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57457"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"(6S)-5-formyl-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57457"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0630","category":"Ligand","name":"Potassium"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL37154.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL37154.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000083","properties":[{"key":"ProteinId","value":"KZL37154.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056996662.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000083.1"}]},{"database":"AlphaFoldDB","id":"A0A161VG90","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.3326","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9805918at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000076480","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:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003924","properties":[{"key":"GoTerm","value":"F:GTPase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030955","properties":[{"key":"GoTerm","value":"F:potassium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0002098","properties":[{"key":"GoTerm","value":"P:tRNA wobble uridine modification"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd04164","properties":[{"key":"EntryName","value":"trmE"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd14858","properties":[{"key":"EntryName","value":"TrmE_N"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.1360.120:FF:000003","properties":[{"key":"EntryName","value":"tRNA modification GTPase MnmE"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000494","properties":[{"key":"EntryName","value":"tRNA modification GTPase MnmE"},{"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":"3.30.1360.120","properties":[{"key":"EntryName","value":"Probable tRNA modification gtpase trme, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.120.430","properties":[{"key":"EntryName","value":"tRNA modification GTPase MnmE domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00379","properties":[{"key":"EntryName","value":"GTPase_MnmE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR031168","properties":[{"key":"EntryName","value":"G_TrmE"}]},{"database":"InterPro","id":"IPR006073","properties":[{"key":"EntryName","value":"GTP-bd"}]},{"database":"InterPro","id":"IPR018948","properties":[{"key":"EntryName","value":"GTP-bd_TrmE_N"}]},{"database":"InterPro","id":"IPR004520","properties":[{"key":"EntryName","value":"GTPase_MnmE"}]},{"database":"InterPro","id":"IPR027368","properties":[{"key":"EntryName","value":"MnmE_dom2"}]},{"database":"InterPro","id":"IPR025867","properties":[{"key":"EntryName","value":"MnmE_helical"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR005225","properties":[{"key":"EntryName","value":"Small_GTP-bd"}]},{"database":"InterPro","id":"IPR027266","properties":[{"key":"EntryName","value":"TrmE/GcvT-like"}]},{"database":"NCBIfam","id":"NF003661","properties":[{"key":"EntryName","value":"mnmE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00450","properties":[{"key":"EntryName","value":"mnmE_trmE_thdF"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00231","properties":[{"key":"EntryName","value":"small_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42714","properties":[{"key":"EntryName","value":"TRNA MODIFICATION GTPASE GTPBP3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42714:SF2","properties":[{"key":"EntryName","value":"TRNA MODIFICATION GTPASE GTPBP3, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01926","properties":[{"key":"EntryName","value":"MMR_HSR1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12631","properties":[{"key":"EntryName","value":"MnmE_helical"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10396","properties":[{"key":"EntryName","value":"TrmE_N"},{"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":"SSF116878","properties":[{"key":"EntryName","value":"TrmE connector domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51709","properties":[{"key":"EntryName","value":"G_TRME"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTATSEFDTIAAVATPPGEGGISIIRVSGDDVFDVVEPLFKGKNLKNVKTHTINYGHIIDPETQSEVDEVMVSVMRAPKTYTREDVLEINCHGGLMATNEILQLVLSNGARLAEPGEFTKRAFLNGRIDLSQAEAVMDLIRAKTDKSMKVALNQLDGSLSRLIKNLRQDILEVLAQVEVNIDYPEYDDVETMTTKLLLEKAQEVKASIQQLLKTAKQGKVLREGLATAIVGRPNVGKSSLLNQLLNEDKAIVTDVAGTTRDVIEEYVNVAGVPLKLIDTAGIRKTDDTVEKIGVERSRKAIGAADLVLLVLDTSEPLTDGDRQLLADTADEKRIIILNKTDLPLKLDMTELQHLAGDTKLIKTSMLQNQGVSELQEEIAHLFFDEGIESGQGNVMVTNARHIGLLHQASKALDDVMTGIAAGMPVDLVQIDMTRCWNYLGEITGDSYQDELLDQLFSQFCVGK","length":463,"molWeight":50707,"crc64":"ACB7D3AE10FB8551","md5":"CAD4C9C0124785FDDBC02585E9DBD0E7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":17},"uniParcId":"UPI0006EEFE4C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161VGF6","uniProtkbId":"A0A161VGF6_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2016-07-06","entryVersion":31,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL37738.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011893"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"value":"Adenine phosphoribosyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"value":"APRT"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011893"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"value":"2.4.2.7"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"value":"apt"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL37738.1"}],"value":"TY91_12430"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003968"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"value":"Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16609"},{"database":"ChEBI","id":"CHEBI:16708"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58017"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"2.4.2.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000868"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004659"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"value":"Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"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_00004"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008391"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"value":"Belongs to the purine/pyrimidine phosphoribosyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL37738.1"}],"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":40,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"Phosphoribosyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00156"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022726"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00004"}],"id":"KW-0660","category":"Biological process","name":"Purine salvage"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"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_00004"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL37738.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL37738.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000079","properties":[{"key":"ProteinId","value":"KZL37738.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_054759881.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000079.1"}]},{"database":"AlphaFoldDB","id":"A0A161VGF6","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.3169","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9803963at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00588","properties":[{"key":"RectionId","value":"UER00646"}]},{"database":"Proteomes","id":"UP000076480","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:0002055","properties":[{"key":"GoTerm","value":"F:adenine binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003999","properties":[{"key":"GoTerm","value":"F:adenine phosphoribosyltransferase 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:0006168","properties":[{"key":"GoTerm","value":"P:adenine salvage"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044209","properties":[{"key":"GoTerm","value":"P:AMP salvage"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006166","properties":[{"key":"GoTerm","value":"P:purine ribonucleoside salvage"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06223","properties":[{"key":"EntryName","value":"PRTases_typeI"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2020:FF:000004","properties":[{"key":"EntryName","value":"Adenine phosphoribosyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00004","properties":[{"key":"EntryName","value":"Aden_phosphoribosyltr"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005764","properties":[{"key":"EntryName","value":"Ade_phspho_trans"}]},{"database":"InterPro","id":"IPR029057","properties":[{"key":"EntryName","value":"PRTase-like"}]},{"database":"InterPro","id":"IPR000836","properties":[{"key":"EntryName","value":"PRTase_dom"}]},{"database":"InterPro","id":"IPR050054","properties":[{"key":"EntryName","value":"UPRTase/APRTase"}]},{"database":"NCBIfam","id":"TIGR01090","properties":[{"key":"EntryName","value":"apt"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002633","properties":[{"key":"EntryName","value":"PRK02304.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002634","properties":[{"key":"EntryName","value":"PRK02304.1-3"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002636","properties":[{"key":"EntryName","value":"PRK02304.1-5"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32315","properties":[{"key":"EntryName","value":"ADENINE PHOSPHORIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32315:SF3","properties":[{"key":"EntryName","value":"ADENINE PHOSPHORIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00156","properties":[{"key":"EntryName","value":"Pribosyltran"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53271","properties":[{"key":"EntryName","value":"PRTase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAIDLTDYIATVPDYPEPGVMFRDISPLMADGEAYRYATDQLVDYARGKNVEMIVGPEARGFIVGCPVAYELGVGFAPARKEGKLPRETVKATYSLEYGTSALYLHKDAIKPGQRVLVTDDLLATGGTIAATIQLVEDLGGIVVGTAFIIELKDLHGRDKIKGHDIFSLMEY","length":172,"molWeight":18729,"crc64":"3F03994E6773EADD","md5":"62651BFAFB5B51645B3F199C03E6FCD7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI0006D0A701"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161VHY2","uniProtkbId":"A0A161VHY2_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-07-06","entryVersion":35,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40199.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"value":"UDP-N-acetylglucosamine 1-carboxyvinyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"value":"2.5.1.7"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"value":"Enoylpyruvate transferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"value":"UDP-N-acetylglucosamine enolpyruvyl transferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"value":"EPT"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"value":"murA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40199.1"}],"value":"TY91_08735"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"value":"Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18681"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57705"},{"database":"ChEBI","id":"CHEBI:58702"},{"database":"ChEBI","id":"CHEBI:68483"}],"ecNumber":"2.5.1.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047527"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004752"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038367"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"value":"Belongs to the EPSP synthase family. MurA subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40199.1"}],"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":7,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"Enolpyruvate transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00275"}]},{"type":"Active site","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}]},{"type":"Binding site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58702"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"ligand":{"name":"phosphoenolpyruvate","id":"ChEBI:CHEBI:58702"}},{"type":"Binding site","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":307,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":329,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Modified residue","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"2-(S-cysteinyl)pyruvic acid O-phosphothioketal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022618"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00111"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"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_00111"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40199.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40199.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000041","properties":[{"key":"ProteinId","value":"KZL40199.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_063285439.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000041.1"}]},{"database":"AlphaFoldDB","id":"A0A161VHY2","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.2337","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9803760at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00219","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000076480","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:0008760","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019277","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylgalactosamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd01555","properties":[{"key":"EntryName","value":"UdpNAET"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.65.10.10:FF:000001","properties":[{"key":"EntryName","value":"UDP-N-acetylglucosamine 1-carboxyvinyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.65.10.10","properties":[{"key":"EntryName","value":"Enolpyruvate transferase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00111","properties":[{"key":"EntryName","value":"MurA"},{"key":"MatchStatus","value":"1"}]},{"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":"IPR013792","properties":[{"key":"EntryName","value":"RNA3'P_cycl/enolpyr_Trfase_a/b"}]},{"database":"InterPro","id":"IPR005750","properties":[{"key":"EntryName","value":"UDP_GlcNAc_COvinyl_MurA"}]},{"database":"NCBIfam","id":"TIGR01072","properties":[{"key":"EntryName","value":"murA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF006873","properties":[{"key":"EntryName","value":"PRK09369.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43783","properties":[{"key":"EntryName","value":"UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43783:SF1","properties":[{"key":"EntryName","value":"UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00275","properties":[{"key":"EntryName","value":"EPSP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55205","properties":[{"key":"EntryName","value":"EPT/RTPC-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEKIIVHGGNRLQGSVHIEGAKNAVLPILAASILAERDEMVLTNVPILSDVYTMNNVLKFLNLDVEFDEAHNTVRLNAAKKLSTQAPFEYVSKMRASIVVMGPLLARYGHTRVAMPGGCAIGSRPVDLHLKGFEALGATINQQDGYIEAKADQLVGTNIYLDFPSVGATQNIMMAATLAKGTTVIENVAREPEIVDLANVLNKMGAKVRGAGTETIRVEGVTALHGTTHHVVQDRIEAGTFMVAAALTQGDILVRDAISEHNKPLISKLEEMGVTVIDEDAGVRVIGPKVLKPTNVKTMPHPGFPTDMQPQMSVLQLAAKGTSTLTETVFENRFMHLEELRRMNANFKIEGRTVVLYGPTNFNGAEVAATDLRAAATLVLAGLVANGYTQVTNLKYLDRGYYDFHKKLASLGAEIERVSVPEQEEVVLKSKAQD","length":434,"molWeight":47032,"crc64":"C6D359D2C029317D","md5":"FC77D972DE49E77C82CAD3C001041528"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":5,"Modified residue":1},"uniParcId":"UPI0007AEE4E2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161VHZ0","uniProtkbId":"A0A161VHZ0_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-07-06","entryVersion":43,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40209.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00072146"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Uracil phosphoribosyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011894"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"2.4.2.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031082"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"UMP pyrophosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00079807"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"UPRTase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"upp"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40209.1"}],"value":"TY91_08785"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00056901"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + uracil","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13017"},{"database":"ChEBI","id":"CHEBI:17568"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57865"},{"database":"ChEBI","id":"CHEBI:58017"}],"ecNumber":"2.4.2.9","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052919"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Allosterically activated by GTP"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005180"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Belongs to the UPRTase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40209.1"}],"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":208,"modifier":"EXACT"}},"description":"Phosphoribosyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF14681"}]},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017"}},{"type":"Binding site","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017"}},{"type":"Binding site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017"}},{"type":"Binding site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17568"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"uracil","id":"ChEBI:CHEBI:17568"}},{"type":"Binding site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17568"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"uracil","id":"ChEBI:CHEBI:17568"}},{"type":"Binding site","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"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_01218"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40209.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40209.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000041","properties":[{"key":"ProteinId","value":"KZL40209.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056996278.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000041.1"}]},{"database":"AlphaFoldDB","id":"A0A161VHZ0","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.2347","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9781675at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00574","properties":[{"key":"RectionId","value":"UER00636"}]},{"database":"Proteomes","id":"UP000076480","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004845","properties":[{"key":"GoTerm","value":"F:uracil phosphoribosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0044206","properties":[{"key":"GoTerm","value":"P:UMP salvage"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006223","properties":[{"key":"GoTerm","value":"P:uracil salvage"},{"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:000003","properties":[{"key":"EntryName","value":"Uracil phosphoribosyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01218_B","properties":[{"key":"EntryName","value":"Upp_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029057","properties":[{"key":"EntryName","value":"PRTase-like"}]},{"database":"InterPro","id":"IPR000836","properties":[{"key":"EntryName","value":"PRTase_dom"}]},{"database":"InterPro","id":"IPR034332","properties":[{"key":"EntryName","value":"Upp_B"}]},{"database":"InterPro","id":"IPR005765","properties":[{"key":"EntryName","value":"UPRT"}]},{"database":"InterPro","id":"IPR050054","properties":[{"key":"EntryName","value":"UPRTase/APRTase"}]},{"database":"NCBIfam","id":"NF001097","properties":[{"key":"EntryName","value":"upp"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01091","properties":[{"key":"EntryName","value":"upp"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32315","properties":[{"key":"EntryName","value":"ADENINE PHOSPHORIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32315:SF4","properties":[{"key":"EntryName","value":"URACIL PHOSPHORIBOSYLTRANSFERASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14681","properties":[{"key":"EntryName","value":"UPRTase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53271","properties":[{"key":"EntryName","value":"PRTase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGKFQVMDHPLIQHKLTIIRNKNCGTKVFREVVDEITTLMAYDVARDMPLEDVEIETPIAKMTAKTLSGKKVAVVPILRAGIGMVDGILKLIPAAKVGHIGMYRDEETLEPHEYFVKLPADIEQRQVFVVDPMLATGGSAIMAIDALKKRGATNIKFVCLVSAPEGVKALREKHPDVDIYAAALDDHLNEDGYIVPGLGDAGDRLFGTK","length":209,"molWeight":22892,"crc64":"9CB7BABF82E81022","md5":"96FA7A461DC988D64461B0826665D2A9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":6},"uniParcId":"UPI0006F08CC6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161VI05","uniProtkbId":"A0A161VI05_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-07-06","entryVersion":37,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40219.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004517"}],"value":"Branched-chain-amino-acid aminotransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004517"}],"value":"2.6.1.42"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40219.1"}],"value":"TY91_08835"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24801"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:35146"},{"database":"ChEBI","id":"CHEBI:58045"}],"ecNumber":"2.6.1.42","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048798"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004517"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18321"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:17865"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:57427"}],"ecNumber":"2.6.1.42","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049229"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004517"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24813"},{"database":"ChEBI","id":"CHEBI:11851"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:57762"}],"ecNumber":"2.6.1.42","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048212"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004517"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004516"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004824"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004519"}],"value":"Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005072"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004519"}],"value":"Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004931"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004519"}],"value":"Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009320"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004106"}],"value":"Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40219.1"}],"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":"Modified residue","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR006468-1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004517"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022576"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004517"}],"id":"KW-0032","category":"Molecular function","name":"Aminotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023304"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004517"}],"id":"KW-0100","category":"Biological process","name":"Branched-chain amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004516"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004517"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40219.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40219.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000041","properties":[{"key":"ProteinId","value":"KZL40219.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_056996272.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000041.1"}]},{"database":"AlphaFoldDB","id":"A0A161VI05","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.2357","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9804984at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00047","properties":[{"key":"RectionId","value":"UER00058"}]},{"database":"UniPathway","id":"UPA00048","properties":[{"key":"RectionId","value":"UER00073"}]},{"database":"UniPathway","id":"UPA00049","properties":[{"key":"RectionId","value":"UER00062"}]},{"database":"Proteomes","id":"UP000076480","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0052656","properties":[{"key":"GoTerm","value":"F:L-isoleucine:2-oxoglutarate transaminase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0052654","properties":[{"key":"GoTerm","value":"F:L-leucine:2-oxoglutarate transaminase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0052655","properties":[{"key":"GoTerm","value":"F:L-valine:2-oxoglutarate transaminase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0009098","properties":[{"key":"GoTerm","value":"P:L-leucine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"GO","id":"GO:0009099","properties":[{"key":"GoTerm","value":"P:L-valine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd01557","properties":[{"key":"EntryName","value":"BCAT_beta_family"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.10.10:FF:000006","properties":[{"key":"EntryName","value":"Branched-chain amino acid aminotransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.10:FF:000004","properties":[{"key":"EntryName","value":"Branched-chain-amino-acid aminotransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.10.10","properties":[{"key":"EntryName","value":"D-amino Acid Aminotransferase, subunit A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001544","properties":[{"key":"EntryName","value":"Aminotrans_IV"}]},{"database":"InterPro","id":"IPR018300","properties":[{"key":"EntryName","value":"Aminotrans_IV_CS"}]},{"database":"InterPro","id":"IPR036038","properties":[{"key":"EntryName","value":"Aminotransferase-like"}]},{"database":"InterPro","id":"IPR005786","properties":[{"key":"EntryName","value":"B_amino_transII"}]},{"database":"InterPro","id":"IPR043132","properties":[{"key":"EntryName","value":"BCAT-like_C"}]},{"database":"InterPro","id":"IPR043131","properties":[{"key":"EntryName","value":"BCAT-like_N"}]},{"database":"InterPro","id":"IPR033939","properties":[{"key":"EntryName","value":"BCAT_family"}]},{"database":"NCBIfam","id":"TIGR01123","properties":[{"key":"EntryName","value":"ilvE_II"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009897","properties":[{"key":"EntryName","value":"PRK13357.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42825","properties":[{"key":"EntryName","value":"AMINO ACID AMINOTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42825:SF2","properties":[{"key":"EntryName","value":"BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE 3, CHLOROPLASTIC-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01063","properties":[{"key":"EntryName","value":"Aminotran_4"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006468","properties":[{"key":"EntryName","value":"BCAT1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56752","properties":[{"key":"EntryName","value":"D-aminoacid aminotransferase-like PLP-dependent enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00770","properties":[{"key":"EntryName","value":"AA_TRANSFER_CLASS_4"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAKAPEPSTIDWANLGFNYMDLPYRFLAHYSDGKWDDGELTEDATLHISEGSTGLHYGQADFEGLKAYRTKNGEINLFRPDRNAARMHKSCERLLMPAFPEDKFIAAVKSVVKANADYVPPYGTGGTLYLRPLMIGVGGNIGVHPAQEYIFTVFAMPVGAYYKGGVTPTNFTTSYYDRAAPHGTGQSKVGGNYGGSLLPGDEAHKAGYSDVIYLDPATHKKIEEAGSANFFGVTKDNEFVTPKSDSILPSITKYSLLYLAEHNLGMKPVQGDVFIDDLDRFTEAGAMGTAAVIAPIGGIEYHDKLHVFYSETEVGPVTQKLYDTLTGIQFGDVEAPEGWIQKVPLD","length":346,"molWeight":37773,"crc64":"2C8675509425E791","md5":"A3E2D41352C235BD399DEC23B75035D1"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":3,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Modified residue":1},"uniParcId":"UPI00070493D1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161VI73","uniProtkbId":"A0A161VI73_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2025-10-08","lastSequenceUpdateDate":"2016-07-06","entryVersion":38,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40509.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"value":"tRNA dimethylallyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"value":"2.5.1.75"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"value":"Dimethylallyl diphosphate:tRNA dimethylallyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"value":"DMAPP:tRNA dimethylallyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"value":"DMATase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"value":"Isopentenyl-diphosphate:tRNA isopentenyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"value":"IPP transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"value":"IPPT"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"value":"IPTase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"value":"miaA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40509.1"}],"value":"TY91_08370"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003213"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003784"}],"value":"Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(37) in tRNA + dimethylallyl diphosphate = N(6)-dimethylallyladenosine(37) in tRNA + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26482"},{"database":"Rhea","id":"RHEA-COMP:10162"},{"database":"Rhea","id":"RHEA-COMP:10375"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57623"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74415"}],"ecNumber":"2.5.1.75","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049563"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003783"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003785"}],"value":"Belongs to the IPP transferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40509.1"}],"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":35,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"Interaction with substrate tRNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"Interaction with substrate tRNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}]},{"type":"Site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"Interaction with substrate tRNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"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_00185"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00185"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40509.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL40509.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000039","properties":[{"key":"ProteinId","value":"KZL40509.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A161VI73","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.2246","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9776390at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000076480","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0052381","properties":[{"key":"GoTerm","value":"F:tRNA dimethylallyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006400","properties":[{"key":"GoTerm","value":"P:tRNA modification"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"1.10.20.140","properties":[{"key":"EntryName","value":"-"},{"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_00185","properties":[{"key":"EntryName","value":"IPP_trans"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR039657","properties":[{"key":"EntryName","value":"Dimethylallyltransferase"}]},{"database":"InterPro","id":"IPR018022","properties":[{"key":"EntryName","value":"IPT"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"TIGR00174","properties":[{"key":"EntryName","value":"miaA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11088","properties":[{"key":"EntryName","value":"TRNA DIMETHYLALLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11088:SF60","properties":[{"key":"EntryName","value":"TRNA DIMETHYLALLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01715","properties":[{"key":"EntryName","value":"IPPT"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MMKKVMAIIGPTAVGKTALSIQLAQKFNGEVISGDSMQVYRGLDIGTAKVTAEEKQDVPHYLIDIKEPNERYSVADFVTSAEALIDEITARGHLPMIVGGTGFYLKALLYDMTLGGDKYEPSETVRRKWHQFAEANGQQALWDHLAGIDPEAAQKIPVSNERRVVRALEVYERTGILFSQQQSGTQLRYDPLIIGLNTDRALLYQRINQRVDQMLDEGLENEARQLFDAGGEQFAAGKGIGYREFFPYFNLQQTLPDTVAQIKQDTRHYAKRQLTWFRHQVPVTWFDIVQHPEQLPAIRETVSQWLQN","length":308,"molWeight":34998,"crc64":"B0006AD312AE1D6D","md5":"2608E486E42171E6C235C85E1D881F9A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Region":1,"Binding site":2,"Site":2},"uniParcId":"UPI000704E8A2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A161VI89","uniProtkbId":"A0A161VI89_SECCO","entryAudit":{"firstPublicDate":"2016-07-06","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-07-06","entryVersion":41,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Secundilactobacillus collinoides","commonName":"Lactobacillus collinoides","taxonId":33960,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41016.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Secundilactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002811"}],"value":"DNA primase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"}],"value":"2.7.7.101"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"}],"value":"dnaG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41016.1"}],"value":"TY91_07125"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002811"}],"value":"RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.","ecNumber":"2.7.7.101","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002811"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR002811-1"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002811"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR002811-1"}],"value":"Binds 1 zinc ion per monomer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"}],"value":"Monomer. Interacts with DnaB"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"}],"value":"Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR002811"}],"value":"Belongs to the DnaG primase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00995"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41016.1"}],"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":263,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"Toprim","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50880"}]},{"type":"Zinc finger","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"CHC2-type","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR002811-1"}]},{"type":"Region","location":{"start":{"value":439,"modifier":"EXACT"},"end":{"value":469,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":439,"modifier":"EXACT"},"end":{"value":448,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":469,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022705"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"}],"id":"KW-0235","category":"Biological process","name":"DNA replication"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022478"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"}],"id":"KW-0240","category":"Cellular component","name":"DNA-directed RNA polymerase"},{"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":"HAMAP-Rule","id":"MF_00974"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022515"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"}],"id":"KW-0639","category":"Cellular component","name":"Primosome"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022771"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00974"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8N601F3CEL4FF","citationType":"submission","authors":["Puertas A.I.","Spano G.","Capozzi V.","Lamontanara A.","Orru L.","Duenas M.T."],"title":"Draft genome sequence of Lactobacillus collinoides CUPV2371 isolated from a natural cider, the first genome sequence of a strain of this species.","publicationDate":"FEB-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41016.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}],"value":"237","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KZL41016.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000076480"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JYDC01000038","properties":[{"key":"ProteinId","value":"KZL41016.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_054758699.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JYDC01000038.1"}]},{"database":"AlphaFoldDB","id":"A0A161VI89","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|33960.6.peg.1983","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9803773at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000076480","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003899","properties":[{"key":"GoTerm","value":"F:DNA-directed RNA polymerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006269","properties":[{"key":"GoTerm","value":"P:DNA replication, synthesis of primer"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd03364","properties":[{"key":"EntryName","value":"TOPRIM_DnaG_primases"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.580.10:FF:000001","properties":[{"key":"EntryName","value":"DNA primase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1360.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.980.10","properties":[{"key":"EntryName","value":"DNA primase, catalytic core, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.860.10","properties":[{"key":"EntryName","value":"DNAb Helicase, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.580.10","properties":[{"key":"EntryName","value":"Zinc finger, CHC2-type domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00974","properties":[{"key":"EntryName","value":"DNA_primase_DnaG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016136","properties":[{"key":"EntryName","value":"DNA_helicase_N/primase_C"}]},{"database":"InterPro","id":"IPR037068","properties":[{"key":"EntryName","value":"DNA_primase_core_N_sf"}]},{"database":"InterPro","id":"IPR019475","properties":[{"key":"EntryName","value":"DNA_primase_DnaB-bd"}]},{"database":"InterPro","id":"IPR006295","properties":[{"key":"EntryName","value":"DNA_primase_DnaG"}]},{"database":"InterPro","id":"IPR036977","properties":[{"key":"EntryName","value":"DNA_primase_Znf_CHC2"}]},{"database":"InterPro","id":"IPR030846","properties":[{"key":"EntryName","value":"DnaG_bac"}]},{"database":"InterPro","id":"IPR013264","properties":[{"key":"EntryName","value":"DNAG_N"}]},{"database":"InterPro","id":"IPR050219","properties":[{"key":"EntryName","value":"DnaG_primase"}]},{"database":"InterPro","id":"IPR034151","properties":[{"key":"EntryName","value":"TOPRIM_DnaG_bac"}]},{"database":"InterPro","id":"IPR006171","properties":[{"key":"EntryName","value":"TOPRIM_dom"}]},{"database":"InterPro","id":"IPR002694","properties":[{"key":"EntryName","value":"Znf_CHC2"}]},{"database":"NCBIfam","id":"TIGR01391","properties":[{"key":"EntryName","value":"dnaG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30313","properties":[{"key":"EntryName","value":"DNA PRIMASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30313:SF2","properties":[{"key":"EntryName","value":"DNA PRIMASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10410","properties":[{"key":"EntryName","value":"DnaB_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08275","properties":[{"key":"EntryName","value":"DNAG_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13155","properties":[{"key":"EntryName","value":"Toprim_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01807","properties":[{"key":"EntryName","value":"Zn_ribbon_DnaG"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF002811","properties":[{"key":"EntryName","value":"DnaG"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00493","properties":[{"key":"EntryName","value":"TOPRIM"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00400","properties":[{"key":"EntryName","value":"ZnF_CHCC"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56731","properties":[{"key":"EntryName","value":"DNA primase core"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF57783","properties":[{"key":"EntryName","value":"Zinc beta-ribbon"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50880","properties":[{"key":"EntryName","value":"TOPRIM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAKIPEAVIEQVRDATDIVDFISQYVQLQKSGKNLFGLCPFHEERTPSFSVSEDKQIFHCFSCGRGGNVFKFIMELENIGFQEAVVKVAEFSHVDLPDSVANATYSGQARQDSPANHLIQLHEGAQKLYHHILMNTEIGQPALDYLHQRGLTDKTIEDFGLGFAPDQQLLKQYFDQQKVDYQELRHTGLFIENQSGELRDRFFNRVMYPIKNESGQPIAFSGRLLVKADDQPKYLNSPETDIFNKRRVLFNFDQARNVIRKEGAVILFEGFMDVMSAHQSGVGNGVASMGTSLTEEQIYAMQRVTKQVYVCYDGDTPGQRATNRALTILRDNSSLALGVIQMPEGMDPDEYRKKYGEEKLASALQSARETPIAFAMHYLKSEHDVNTDAGRLEYIDQVLNLLATVTSPVEQDVYLTQLANEYQLDKGSLKQQLLMIKPKPAKSSRPAPATNPYDGGYPQSGYQNQEPPAEVTQYQQAPPLSRTEKAERGLLLRMLHDHSVWLRVTGIENFSFESDDYELIYMLAQKYFQTHQTYAPAQFIDLITDDHLQNMVIELESLNINDEAADEEVDDYLRVIMNEAPLEKQLTQSQQALNEAKRLGDNDRVRQLVIEIIKLQQQKQSNKRA","length":625,"molWeight":71083,"crc64":"2BBB7D0450796CD8","md5":"E4B038621B4327DC20B60A816AE7182A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Zinc finger":1,"Region":1,"Compositional bias":2},"uniParcId":"UPI0006D10A2F"}}]}