{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2C9PIJ8","uniProtkbId":"A0A2C9PIJ8_9LAMI","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-12-20","entryVersion":13,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Utricularia triloba","taxonId":192321,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATL77014.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Lamiales","Lentibulariaceae","Utricularia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01390"}],"value":"Maturase K"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01390"}],"value":"Intron maturase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01390"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATL77014.1"}],"value":"matK"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01390"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004226"}],"value":"Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01390"}],"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006621"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01390"}],"value":"Belongs to the intron maturase 2 family. MatK subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"Maturase MatK N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01824"}]},{"type":"Domain","location":{"start":{"value":358,"modifier":"EXACT"},"end":{"value":467,"modifier":"EXACT"}},"description":"Domain X","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01348"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATL77014.1"}],"geneEncodingType":"Chloroplast"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004226"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATL77014.1"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022664"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01390"}],"id":"KW-0507","category":"Biological process","name":"mRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022640"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004226"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01390"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01390"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"28935893","citationType":"journal article","authors":["Westermeier A.S.","Fleischmann A.","Muller K.","Schaferhoff B.","Rubach C.","Speck T.","Poppinga S."],"citationCrossReferences":[{"database":"PubMed","id":"28935893"},{"database":"DOI","id":"10.1038/s41598-017-12324-4"}],"title":"Trap diversity and character evolution in carnivorous bladderworts (Utricularia, Lentibulariaceae).","publicationDate":"2017","journal":"Sci. Rep.","firstPage":"12052","lastPage":"12052","volume":"7"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATL77014.1"}]},{"referenceNumber":2,"citation":{"id":"CI-1PS2RRSJFV9E3","citationType":"submission","authors":["de Groot N.N."],"publicationDate":"AUG-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATL77014.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"MF765528","properties":[{"key":"ProteinId","value":"ATL77014.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A2C9PIJ8","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:0006397","properties":[{"key":"GoTerm","value":"P:mRNA processing"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008380","properties":[{"key":"GoTerm","value":"P:RNA splicing"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"HAMAP","id":"MF_01390","properties":[{"key":"EntryName","value":"MatK"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR024937","properties":[{"key":"EntryName","value":"Domain_X"}]},{"database":"InterPro","id":"IPR002866","properties":[{"key":"EntryName","value":"Maturase_MatK"}]},{"database":"InterPro","id":"IPR024942","properties":[{"key":"EntryName","value":"Maturase_MatK_N"}]},{"database":"PANTHER","id":"PTHR34811","properties":[{"key":"EntryName","value":"MATURASE K"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34811:SF1","properties":[{"key":"EntryName","value":"MATURASE K"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01348","properties":[{"key":"EntryName","value":"Intron_maturas2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01824","properties":[{"key":"EntryName","value":"MatK_N"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEDIKNYLQTERFKQKDFLYPLMFQESIYAFAHDRGFDRSNFTGCGNKFSFLIVKRIITRMHQQNKLIISHNNSSQNPFFLFNTNLYSRIISEGFAFFVEIPFYLRGIYGIKGKKVIKSHNLRSIHSIFPFVEDNFSHLNFVLDTEIPYSVHAEILVQALRYWLKDASSLHLLRFFLSECWNGNSLININTKKNSFSKKNQRVFLLLYNSHVYEYESTLIFLCNQSVHLRSTSFELFLERIYFYRKMELLVKVFGKVSDFQFNLWLVKEPCIHYVRSQKKYILSSKGMSRFLKKWKCYLVNFWQWYFSLWFSAKKISINQLANHSVEFWGYFSSVQIKLLLVRSQSIENSFIMNNAIKKCDTLVPIIPLLGTLSKAQFCNVLGHPISKPSWADLGDSTIIDRFGRICRNLFHYYSGSSAKKSLYRLKYILQLSCARTLACKPKSPVRTFFKRLDLGLLGEFFMSTEDILFVIATKASFPLRGVHRDRVWYLDIISLDDLFNQKK","length":504,"molWeight":59519,"crc64":"967D5C31B4833082","md5":"BA896B8D51FE46F38AB6E8D423D2B74A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2},"uniParcId":"UPI000C059617"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2D1PG21","uniProtkbId":"A0A2D1PG21_9LAMI","entryAudit":{"firstPublicDate":"2018-01-31","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-01-31","entryVersion":30,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Utricularia triloba","taxonId":192321,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATO92142.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Lamiales","Lentibulariaceae","Utricularia"]},"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"},"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":"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":2,"modifier":"EXACT"},"end":{"value":122,"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":132,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"Ribulose bisphosphate carboxylase large subunit C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00016"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATO92142.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATO92142.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATO92142.1"}],"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":"RuleBase","id":"RU000302"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"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":"ATO92142.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"}],"references":[{"referenceNumber":1,"citation":{"id":"29054811","citationType":"journal article","authors":["Silva S.R.","Gibson R.","Adamec L.","Dominguez Y.","Miranda V.F.O."],"citationCrossReferences":[{"database":"PubMed","id":"29054811"},{"database":"DOI","id":"10.1016/j.ympev.2017.10.010"}],"title":"Molecular phylogeny of bladderworts: A wide approach of Utricularia (Lentibulariaceae) species relationships based on six plastidial and nuclear DNA sequences.","publicationDate":"2018","journal":"Mol. Phylogenet. Evol.","firstPage":"244","lastPage":"264","volume":"118"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATO92142.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"MF991560","properties":[{"key":"ProteinId","value":"ATO92142.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A2D1PG21","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":"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":"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":"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":"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"}]}],"sequence":{"value":"TYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYNIEPVPGETDQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLR","length":172,"molWeight":19140,"crc64":"95380CFE323E2980","md5":"558DAFCD4EC7B2DE48194100BF241643"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Non-terminal residue":2},"uniParcId":"UPI000C5A3A75"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2D1PG23","uniProtkbId":"A0A2D1PG23_9LAMI","entryAudit":{"firstPublicDate":"2018-01-31","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-01-31","entryVersion":30,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Utricularia triloba","taxonId":192321,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATO92141.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Lamiales","Lentibulariaceae","Utricularia"]},"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"},"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":"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":2,"modifier":"EXACT"},"end":{"value":122,"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":132,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"Ribulose bisphosphate carboxylase large subunit C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00016"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATO92141.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATO92141.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATO92141.1"}],"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":"RuleBase","id":"RU000302"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"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":"ATO92141.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"}],"references":[{"referenceNumber":1,"citation":{"id":"29054811","citationType":"journal article","authors":["Silva S.R.","Gibson R.","Adamec L.","Dominguez Y.","Miranda V.F.O."],"citationCrossReferences":[{"database":"PubMed","id":"29054811"},{"database":"DOI","id":"10.1016/j.ympev.2017.10.010"}],"title":"Molecular phylogeny of bladderworts: A wide approach of Utricularia (Lentibulariaceae) species relationships based on six plastidial and nuclear DNA sequences.","publicationDate":"2018","journal":"Mol. Phylogenet. Evol.","firstPage":"244","lastPage":"264","volume":"118"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATO92141.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"MF991559","properties":[{"key":"ProteinId","value":"ATO92141.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A2D1PG23","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":"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":"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":"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":"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"}]}],"sequence":{"value":"TYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYNIEPVPGETDQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGG","length":174,"molWeight":19254,"crc64":"529085380CFE323E","md5":"89761FA1C37D0264AECAC7AC59832257"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Non-terminal residue":2},"uniParcId":"UPI000C6B15CD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2D1PG24","uniProtkbId":"A0A2D1PG24_9LAMI","entryAudit":{"firstPublicDate":"2018-01-31","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-01-31","entryVersion":30,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Utricularia triloba","taxonId":192321,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATO92140.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Lamiales","Lentibulariaceae","Utricularia"]},"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"},"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":"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":2,"modifier":"EXACT"},"end":{"value":122,"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":132,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"Ribulose bisphosphate carboxylase large subunit C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00016"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATO92140.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATO92140.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATO92140.1"}],"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":"RuleBase","id":"RU000302"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"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":"ATO92140.1"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"}],"references":[{"referenceNumber":1,"citation":{"id":"29054811","citationType":"journal article","authors":["Silva S.R.","Gibson R.","Adamec L.","Dominguez Y.","Miranda V.F.O."],"citationCrossReferences":[{"database":"PubMed","id":"29054811"},{"database":"DOI","id":"10.1016/j.ympev.2017.10.010"}],"title":"Molecular phylogeny of bladderworts: A wide approach of Utricularia (Lentibulariaceae) species relationships based on six plastidial and nuclear DNA sequences.","publicationDate":"2018","journal":"Mol. Phylogenet. Evol.","firstPage":"244","lastPage":"264","volume":"118"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATO92140.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"MF991558","properties":[{"key":"ProteinId","value":"ATO92140.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"MF991561","properties":[{"key":"ProteinId","value":"ATO92143.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A2D1PG24","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":"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":"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":"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":"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"}]}],"sequence":{"value":"TYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYNIEPVPGETDQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRG","length":173,"molWeight":19197,"crc64":"B085380CFE323E29","md5":"4310D4975772CE03CB4E57F30C05CEB1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Non-terminal residue":2},"uniParcId":"UPI000C40DAB8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q5QG43","uniProtkbId":"Q5QG43_9LAMI","entryAudit":{"firstPublicDate":"2005-01-04","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2005-01-04","entryVersion":77,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Utricularia triloba","taxonId":192321,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAT02469.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Lamiales","Lentibulariaceae","Utricularia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Cytochrome c oxidase subunit 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"7.1.1.9"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAT02469.1"}],"value":"COXI"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4 Fe(II)-[cytochrome c] + O2 + 8 H(+)(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11436"},{"database":"Rhea","id":"RHEA-COMP:10350"},{"database":"Rhea","id":"RHEA-COMP:14399"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:29034"}],"ecNumber":"7.1.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Energy metabolism; oxidative phosphorylation"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Belongs to the heme-copper respiratory oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"Cytochrome oxidase subunit I profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50855"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAT02469.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":250,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAT02469.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAT02469.1"}],"geneEncodingType":"Mitochondrion"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAT02469.1"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0999","category":"Cellular component","name":"Mitochondrion inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"15596720","citationType":"journal article","authors":["Jobson R.W.","Nielsen R.","Laakkonen L.","Wikstrom M.","Albert V.A."],"citationCrossReferences":[{"database":"PubMed","id":"15596720"},{"database":"DOI","id":"10.1073/pnas.0408092101"}],"title":"Adaptive evolution of cytochrome c oxidase: Infrastructure for a carnivorous plant radiation.","publicationDate":"2004","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"18064","lastPage":"18068","volume":"101"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAT02469.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AY600131","properties":[{"key":"ProteinId","value":"AAT02469.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q5QG43","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00705","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0005743","properties":[{"key":"GoTerm","value":"C:mitochondrial inner membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004129","properties":[{"key":"GoTerm","value":"F:cytochrome-c oxidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"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":"GO","id":"GO:0006123","properties":[{"key":"GoTerm","value":"P:mitochondrial electron transport, cytochrome c to oxygen"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"1.20.210.10:FF:000027","properties":[{"key":"EntryName","value":"Cytochrome c oxidase subunit 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.210.10","properties":[{"key":"EntryName","value":"Cytochrome c oxidase-like, subunit I domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023616","properties":[{"key":"EntryName","value":"Cyt_c_oxase-like_su1_dom"}]},{"database":"InterPro","id":"IPR036927","properties":[{"key":"EntryName","value":"Cyt_c_oxase-like_su1_sf"}]},{"database":"InterPro","id":"IPR000883","properties":[{"key":"EntryName","value":"Cyt_C_Oxase_1"}]},{"database":"PANTHER","id":"PTHR10422","properties":[{"key":"EntryName","value":"CYTOCHROME C OXIDASE SUBUNIT 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10422:SF18","properties":[{"key":"EntryName","value":"CYTOCHROME C OXIDASE SUBUNIT 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00115","properties":[{"key":"EntryName","value":"COX1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01165","properties":[{"key":"EntryName","value":"CYCOXIDASEI"}]},{"database":"SUPFAM","id":"SSF81442","properties":[{"key":"EntryName","value":"Cytochrome c oxidase subunit I-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50855","properties":[{"key":"EntryName","value":"COX1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"HPEVYILILPGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPETLGQIHFWITFFGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSTISVVGICRFFVVVTITSSSGKNKRCAPSPWA","length":250,"molWeight":27485,"crc64":"E19152232F16A5BD","md5":"1FDCD708A9100C98E8C1C12E8845B50A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":6,"Domain":1,"Non-terminal residue":2},"uniParcId":"UPI000048E313"}}]}