{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A1W6SAB2","uniProtkbId":"A0A1W6SAB2_9MAGN","entryAudit":{"firstPublicDate":"2017-07-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-07-05","entryVersion":21,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Beauprea gracilis","taxonId":1820304,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ARO77614.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Proteales","Proteaceae","Beauprea"]},"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":"ARO77614.1"}],"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":1,"modifier":"EXACT"},"end":{"value":89,"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":99,"modifier":"EXACT"},"end":{"value":371,"modifier":"EXACT"}},"description":"Ribulose bisphosphate carboxylase large subunit C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00016"}]},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"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":146,"modifier":"EXACT"},"end":{"value":146,"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":"ARO77614.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":371,"modifier":"EXACT"},"end":{"value":371,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ARO77614.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ARO77614.1"}],"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":"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":"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":"ARO77614.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"}],"references":[{"referenceNumber":1,"citation":{"id":"27386508","citationType":"journal article","authors":["He T.","Lamont B.B.","Fogliani B."],"citationCrossReferences":[{"database":"PubMed","id":"27386508"}],"title":"Pre-Gondwanan-breakup origin of Beauprea (Proteaceae) explains its historical presence in New Caledonia and New Zealand.","publicationDate":"2016","journal":"Sci. Adv.","firstPage":"E1501648","lastPage":"E1501648","volume":"2"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ARO77614.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KT956872","properties":[{"key":"ProteinId","value":"ARO77614.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A1W6SAB2","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":"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":"AVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEESQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTAYIKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEA","length":371,"molWeight":41088,"crc64":"5059EB692FEE9808","md5":"AD32A2C2F3FF79C58977D11DFF3B0EFF"},"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":"UPI000A2A04B6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A1W6SAA1","uniProtkbId":"A0A1W6SAA1_9MAGN","entryAudit":{"firstPublicDate":"2017-07-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-07-05","entryVersion":29,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Beauprea gracilis","taxonId":1820304,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ARO77606.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Proteales","Proteaceae","Beauprea"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003553"}],"value":"ATP synthase subunit beta"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003553"}],"value":"7.1.2.2"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ARO77606.1"}],"value":"atpB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00037290"}],"value":"Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57720"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"7.1.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048383"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10106"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003553"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003553"}],"value":"F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(9-12)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004170"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004170"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008936"}],"value":"Belongs to the ATPase alpha/beta chains family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"Site","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"Required for activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10106"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ARO77606.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":434,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ARO77606.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ARO77606.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023310"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003553"}],"id":"KW-0066","category":"Biological process","name":"ATP synthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003553"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023196"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003553"}],"id":"KW-0139","category":"Cellular component","name":"CF(1)"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ARO77606.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022781"}],"id":"KW-0375","category":"Biological process","name":"Hydrogen ion transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023065"}],"id":"KW-0406","category":"Biological process","name":"Ion transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003553"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022640"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ARO77606.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"27386508","citationType":"journal article","authors":["He T.","Lamont B.B.","Fogliani B."],"citationCrossReferences":[{"database":"PubMed","id":"27386508"}],"title":"Pre-Gondwanan-breakup origin of Beauprea (Proteaceae) explains its historical presence in New Caledonia and New Zealand.","publicationDate":"2016","journal":"Sci. Adv.","firstPage":"E1501648","lastPage":"E1501648","volume":"2"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ARO77606.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KT956858","properties":[{"key":"ProteinId","value":"ARO77606.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A1W6SAA1","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009535","properties":[{"key":"GoTerm","value":"C:chloroplast thylakoid membrane"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005739","properties":[{"key":"GoTerm","value":"C:mitochondrion"},{"key":"GoEvidenceType","value":"IEA:GOC"}]},{"database":"GO","id":"GO:0045259","properties":[{"key":"GoTerm","value":"C:proton-transporting ATP synthase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0046933","properties":[{"key":"GoTerm","value":"F:proton-transporting ATP synthase activity, rotational mechanism"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042776","properties":[{"key":"GoTerm","value":"P:proton motive force-driven mitochondrial ATP synthesis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd18110","properties":[{"key":"EntryName","value":"ATP-synt_F1_beta_C"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18115","properties":[{"key":"EntryName","value":"ATP-synt_F1_beta_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01133","properties":[{"key":"EntryName","value":"F1-ATPase_beta_CD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1140.10:FF:000001","properties":[{"key":"EntryName","value":"ATP synthase subunit beta"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000004","properties":[{"key":"EntryName","value":"ATP synthase subunit beta"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.10.170:FF:000002","properties":[{"key":"EntryName","value":"ATP synthase subunit beta, chloroplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.10.170","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1140.10","properties":[{"key":"EntryName","value":"Bovine Mitochondrial F1-atpase, Atp Synthase Beta Chain, Chain D, domain 3"},{"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_01347","properties":[{"key":"EntryName","value":"ATP_synth_beta_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR055190","properties":[{"key":"EntryName","value":"ATP-synt_VA_C"}]},{"database":"InterPro","id":"IPR005722","properties":[{"key":"EntryName","value":"ATP_synth_F1_bsu"}]},{"database":"InterPro","id":"IPR020003","properties":[{"key":"EntryName","value":"ATPase_a/bsu_AS"}]},{"database":"InterPro","id":"IPR050053","properties":[{"key":"EntryName","value":"ATPase_alpha/beta_chains"}]},{"database":"InterPro","id":"IPR004100","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_N"}]},{"database":"InterPro","id":"IPR036121","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_N_sf"}]},{"database":"InterPro","id":"IPR000194","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_nucl-bd"}]},{"database":"InterPro","id":"IPR024034","properties":[{"key":"EntryName","value":"ATPase_F1/V1_b/a_C"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"TIGR01039","properties":[{"key":"EntryName","value":"atpD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR15184","properties":[{"key":"EntryName","value":"ATP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR15184:SF71","properties":[{"key":"EntryName","value":"ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00006","properties":[{"key":"EntryName","value":"ATP-synt_ab"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02874","properties":[{"key":"EntryName","value":"ATP-synt_ab_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22919","properties":[{"key":"EntryName","value":"ATP-synt_VA_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47917","properties":[{"key":"EntryName","value":"C-terminal domain of alpha and beta subunits of F1 ATP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50615","properties":[{"key":"EntryName","value":"N-terminal domain of alpha and beta subunits of F1 ATP synthase"},{"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":"PS00152","properties":[{"key":"EntryName","value":"ATPASE_ALPHA_BETA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"QMPNIYNALVIKGRDTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGFTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQ","length":434,"molWeight":46936,"crc64":"D4044B0972DA490D","md5":"0E8E56E54B4708766EBD67A7008B28AA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Site":1,"Non-terminal residue":2},"uniParcId":"UPI000A29FE7A"}}]}