{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A140GM34","uniProtkbId":"A0A140GM34_9MYRT","entryAudit":{"firstPublicDate":"2016-05-11","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-05-11","entryVersion":30,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Galpinia transvaalica","taxonId":312920,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN14392.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Myrtales","Lythraceae","Galpinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00017725"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"value":"Ribulose bisphosphate carboxylase large chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012287"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"value":"4.1.1.39"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN14392.1"}],"value":"rbcL"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025664"}],"value":"RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 (2R)-3-phosphoglycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO2 + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23124"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57870"},{"database":"ChEBI","id":"CHEBI:58272"}],"ecNumber":"4.1.1.39","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049469"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10114"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribulose 1,5-bisphosphate + O2 = 2-phosphoglycolate + (2R)-3-phosphoglycerate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:36631"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57870"},{"database":"ChEBI","id":"CHEBI:58033"},{"database":"ChEBI","id":"CHEBI:58272"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048059"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"value":"Heterohexadecamer of 8 large chains and 8 small chains"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004229"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006204"}],"value":"Belongs to the RuBisCO large chain family. Type I subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"Ribulose bisphosphate carboxylase large subunit ferrodoxin-like N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02788"}]},{"type":"Domain","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"Ribulose bisphosphate carboxylase large subunit C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00016"}]},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10114"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Modified residue","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10114"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN14392.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":402,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN14392.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN14392.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022567"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0113","category":"Biological process","name":"Calvin cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023300"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0120","category":"Biological process","name":"Carbon dioxide fixation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022528"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022481"}],"id":"KW-0488","category":"PTM","name":"Methylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023033"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0503","category":"Molecular function","name":"Monooxygenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023238"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0601","category":"Biological process","name":"Photorespiration"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022531"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000302"}],"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022640"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN14392.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"}],"references":[{"referenceNumber":1,"citation":{"id":"26585030","citationType":"journal article","authors":["Berger B.A.","Kriebel R.","Spalink D.","Sytsma K.J."],"citationCrossReferences":[{"database":"PubMed","id":"26585030"},{"database":"DOI","id":"10.1016/j.ympev.2015.10.001"}],"title":"Divergence times, historical biogeography, and shifts in speciation rates of Myrtales.","publicationDate":"2016","journal":"Mol. Phylogenet. Evol.","firstPage":"116","lastPage":"136","volume":"95"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN14392.1"}],"value":"Leaves","type":"TISSUE"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN14392.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KU761902","properties":[{"key":"ProteinId","value":"AMN14392.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A140GM34","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016984","properties":[{"key":"GoTerm","value":"F:ribulose-bisphosphate carboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0015977","properties":[{"key":"GoTerm","value":"P:carbon fixation"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.20.20.110:FF:000003","properties":[{"key":"EntryName","value":"Ribulose bisphosphate carboxylase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.150:FF:000001","properties":[{"key":"EntryName","value":"Ribulose bisphosphate carboxylase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.110","properties":[{"key":"EntryName","value":"Ribulose bisphosphate carboxylase, large subunit, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.150","properties":[{"key":"EntryName","value":"RuBisCO large subunit, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR033966","properties":[{"key":"EntryName","value":"RuBisCO"}]},{"database":"InterPro","id":"IPR020878","properties":[{"key":"EntryName","value":"RuBisCo_large_chain_AS"}]},{"database":"InterPro","id":"IPR000685","properties":[{"key":"EntryName","value":"RuBisCO_lsu_C"}]},{"database":"InterPro","id":"IPR036376","properties":[{"key":"EntryName","value":"RuBisCO_lsu_C_sf"}]},{"database":"InterPro","id":"IPR017443","properties":[{"key":"EntryName","value":"RuBisCO_lsu_fd_N"}]},{"database":"InterPro","id":"IPR036422","properties":[{"key":"EntryName","value":"RuBisCO_lsu_N_sf"}]},{"database":"NCBIfam","id":"NF003252","properties":[{"key":"EntryName","value":"PRK04208.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42704","properties":[{"key":"EntryName","value":"RIBULOSE BISPHOSPHATE CARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42704:SF15","properties":[{"key":"EntryName","value":"RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00016","properties":[{"key":"EntryName","value":"RuBisCO_large"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02788","properties":[{"key":"EntryName","value":"RuBisCO_large_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01052","properties":[{"key":"EntryName","value":"RuBisCO"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00014","properties":[{"key":"EntryName","value":"RuBisCO"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG00301","properties":[{"key":"EntryName","value":"RuBisCO-like_proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51649","properties":[{"key":"EntryName","value":"RuBisCo, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54966","properties":[{"key":"EntryName","value":"RuBisCO, large subunit, small (N-terminal) domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00157","properties":[{"key":"EntryName","value":"RUBISCO_LARGE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"GVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTAYIKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGAPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGA","length":402,"molWeight":44625,"crc64":"48788D1D9696B9C5","md5":"12A843F8003ABE8B497D971CA80FD8F5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Binding site":1,"Modified residue":1,"Non-terminal residue":2},"uniParcId":"UPI00078BAFB1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A140GM56","uniProtkbId":"A0A140GM56_9MYRT","entryAudit":{"firstPublicDate":"2016-05-11","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-05-11","entryVersion":32,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Galpinia transvaalica","taxonId":312920,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN14414.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Myrtales","Lythraceae","Galpinia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00018648"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"value":"NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"value":"7.1.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"value":"NADH-plastoquinone oxidoreductase subunit 5"}}],"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN14414.1"}],"value":"ndhF"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004059"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"value":"NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a plastoquinone + NADH + (n+1) H(+)(in) = a plastoquinol + NAD(+) + n H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42608"},{"database":"Rhea","id":"RHEA-COMP:9561"},{"database":"Rhea","id":"RHEA-COMP:9562"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17757"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:62192"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048026"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a plastoquinone + NADPH + (n+1) H(+)(in) = a plastoquinol + NADP(+) + n H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42612"},{"database":"Rhea","id":"RHEA-COMP:9561"},{"database":"Rhea","id":"RHEA-COMP:9562"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17757"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:62192"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047726"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011199"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"value":"NDH is composed of at least 16 different subunits, 5 of which are encoded in the nucleus"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004454"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"value":"Plastid, chloroplast thylakoid membrane","id":"SL-0058"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004454"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008200"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"value":"Belongs to the complex I subunit 5 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}]},{"type":"Transmembrane","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}]},{"type":"Transmembrane","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}]},{"type":"Transmembrane","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"NADH:quinone oxidoreductase/Mrp antiporter transmembrane","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00361"}]},{"type":"Domain","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"NADH:ubiquinone/plastoquinone oxidoreductase chloroplast chain 5 C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01010"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN14414.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN14414.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN14414.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022528"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN14414.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022957"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"id":"KW-0618","category":"Ligand","name":"Plastoquinone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022719"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"id":"KW-0874","category":"PTM","name":"Quinone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023078"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"id":"KW-0793","category":"Cellular component","name":"Thylakoid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364062"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"26585030","citationType":"journal article","authors":["Berger B.A.","Kriebel R.","Spalink D.","Sytsma K.J."],"citationCrossReferences":[{"database":"PubMed","id":"26585030"},{"database":"DOI","id":"10.1016/j.ympev.2015.10.001"}],"title":"Divergence times, historical biogeography, and shifts in speciation rates of Myrtales.","publicationDate":"2016","journal":"Mol. Phylogenet. Evol.","firstPage":"116","lastPage":"136","volume":"95"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN14414.1"}],"value":"Leaves","type":"TISSUE"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN14414.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KU761924","properties":[{"key":"ProteinId","value":"AMN14414.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A140GM56","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0008137","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase (ubiquinone) activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042773","properties":[{"key":"GoTerm","value":"P:ATP synthesis coupled electron transport"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0015990","properties":[{"key":"GoTerm","value":"P:electron transport coupled proton transport"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"InterPro","id":"IPR002128","properties":[{"key":"EntryName","value":"NADH_UbQ_OxRdtase_chlpt_su5_C"}]},{"database":"InterPro","id":"IPR001750","properties":[{"key":"EntryName","value":"ND/Mrp_TM"}]},{"database":"InterPro","id":"IPR003945","properties":[{"key":"EntryName","value":"NU5C-like"}]},{"database":"PANTHER","id":"PTHR42829","properties":[{"key":"EntryName","value":"NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42829:SF2","properties":[{"key":"EntryName","value":"NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01010","properties":[{"key":"EntryName","value":"Proton_antipo_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00361","properties":[{"key":"EntryName","value":"Proton_antipo_M"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01435","properties":[{"key":"EntryName","value":"NPOXDRDTASE5"}]}],"sequence":{"value":"HAYSKALLFLGSGSIIHSMESIVGYSPDKSQNMVLMGGLKKHVPITKTAFLVGTLSLCGIPPLACFWSKDEILNDSWLYSPIFAIIACSTAGLTAFYMFRVYLLTFEGHLNVQFQNYSGQKSSSFYSISLWGKEIPKTIKKKFRLLTLLAMDNNERASFFWNKTYQIDGNVKRIISPFLTIIHFRTKNTFSYPHESDNTMIFPIFLLVLFTLFVGAIGIPFNQDESDLDILSKLLNPSINLLHQNSNNSVNWEEFVTNASFSLSIAFGGIFLATFLYKPIYSSLQNLNS","length":289,"molWeight":32616,"crc64":"C755EB55D16B25A2","md5":"5DDFED18B9CF2A869A1C73E6CED9FCA9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":4,"Domain":2,"Non-terminal residue":2},"uniParcId":"UPI00078CCF1E"}}]}