{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P54205","uniProtkbId":"RBL_SYNY3","entryAudit":{"firstPublicDate":"1996-10-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-10-01","entryVersion":164,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)","taxonId":1111708,"lineage":["Bacteria","Bacillati","Cyanobacteriota","Cyanophyceae","Synechococcales","Merismopediaceae","Synechocystis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"Ribulose bisphosphate carboxylase large chain"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"RuBisCO large subunit"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"4.1.1.39"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"cbbL"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11859847"}],"value":"rbcL"}],"orderedLocusNames":[{"value":"slr0009"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"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:0000255","source":"HAMAP-Rule","id":"MF_01338"}]}},{"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:0000255","source":"HAMAP-Rule","id":"MF_01338"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17993516"}],"value":"Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers (By similarity). RuBisCO interacts with the C-terminus of CcmM, and can be found in complexes that also include carbonic anhydrase (ccaA). RuBisCO associates with both the internal and shell portion of carboxysomes (PubMed:17993516)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P54205","intActId":"EBI-862277"},"interactantTwo":{"uniProtKBAccession":"P52231","geneName":"trxA","intActId":"EBI-862916"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q31NB3"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17993516"}],"value":"This cyanobacterium makes beta-type carboxysomes (PubMed:17993516). In the carboxysome RuBisCO is organized into a paracrystalline array (By similarity)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11859847"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17993516"}],"value":"Carboxysome","id":"SL-0034"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"The basic functional RuBisCO is composed of a large chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric 'cap' on each end of the 'barrel'"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"value":"Belongs to the RuBisCO large chain family. Type I subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":470,"modifier":"EXACT"}},"description":"Ribulose bisphosphate carboxylase large chain","featureId":"PRO_0000062655"},{"type":"Active site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}]},{"type":"Active site","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}]},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"in homodimeric partner","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"via carbamate group","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":322,"modifier":"EXACT"},"end":{"value":322,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":374,"modifier":"EXACT"},"end":{"value":374,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":329,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}]},{"type":"Modified residue","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}]},{"type":"Disulfide bond","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"Interchain; in linked form","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01338"}]}],"keywords":[{"id":"KW-1283","category":"Cellular component","name":"Bacterial microcompartment"},{"id":"KW-0113","category":"Biological process","name":"Calvin cycle"},{"id":"KW-0120","category":"Biological process","name":"Carbon dioxide fixation"},{"id":"KW-1282","category":"Cellular component","name":"Carboxysome"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0503","category":"Molecular function","name":"Monooxygenase"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0601","category":"Biological process","name":"Photorespiration"},{"id":"KW-0602","category":"Biological process","name":"Photosynthesis"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"8219082","citationType":"journal article","authors":["Amichay D.","Levitz R.","Gurevitz M."],"citationCrossReferences":[{"database":"PubMed","id":"8219082"},{"database":"DOI","id":"10.1007/bf00019295"}],"title":"Construction of a Synechocystis PCC6803 mutant suitable for the study of variant hexadecameric ribulose bisphosphate carboxylase/oxygenase enzymes.","publicationDate":"1993","journal":"Plant Mol. Biol.","firstPage":"465","lastPage":"476","volume":"23"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":2,"citation":{"id":"8590279","citationType":"journal article","authors":["Kaneko T.","Tanaka A.","Sato S.","Kotani H.","Sazuka T.","Miyajima N.","Sugiura M.","Tabata S."],"citationCrossReferences":[{"database":"PubMed","id":"8590279"},{"database":"DOI","id":"10.1093/dnares/2.4.153"}],"title":"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome.","publicationDate":"1995","journal":"DNA Res.","firstPage":"153","lastPage":"166","volume":"2"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 27184 / PCC 6803","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"8905231","citationType":"journal article","authors":["Kaneko T.","Sato S.","Kotani H.","Tanaka A.","Asamizu E.","Nakamura Y.","Miyajima N.","Hirosawa M.","Sugiura M.","Sasamoto S.","Kimura T.","Hosouchi T.","Matsuno A.","Muraki A.","Nakazaki N.","Naruo K.","Okumura S.","Shimpo S.","Takeuchi C.","Wada T.","Watanabe A.","Yamada M.","Yasuda M.","Tabata S."],"citationCrossReferences":[{"database":"PubMed","id":"8905231"},{"database":"DOI","id":"10.1093/dnares/3.3.109"}],"title":"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions.","publicationDate":"1996","journal":"DNA Res.","firstPage":"109","lastPage":"136","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 27184 / PCC 6803 / Kazusa","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"11859847","citationType":"journal article","authors":["So A.K.","John-McKay M.","Espie G.S."],"citationCrossReferences":[{"database":"PubMed","id":"11859847"},{"database":"DOI","id":"10.1007/s004250100638"}],"title":"Characterization of a mutant lacking carboxysomal carbonic anhydrase from the cyanobacterium Synechocystis PCC6803.","publicationDate":"2002","journal":"Planta","firstPage":"456","lastPage":"467","volume":"214"},"referencePositions":["SUBCELLULAR LOCATION"],"referenceComments":[{"value":"ATCC 27184 / PCC 6803 / Kazusa","type":"STRAIN"}]},{"referenceNumber":5,"citation":{"id":"17993516","citationType":"journal article","authors":["Cot S.S.","So A.K.","Espie G.S."],"citationCrossReferences":[{"database":"PubMed","id":"17993516"},{"database":"DOI","id":"10.1128/jb.01283-07"}],"title":"A multiprotein bicarbonate dehydration complex essential to carboxysome function in cyanobacteria.","publicationDate":"2008","journal":"J. Bacteriol.","firstPage":"936","lastPage":"945","volume":"190"},"referencePositions":["INTERACTION WITH CCMM","SUBCELLULAR LOCATION"],"referenceComments":[{"value":"ATCC 27184 / PCC 6803 / Kazusa","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X65960","properties":[{"key":"ProteinId","value":"CAA46773.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"BA000022","properties":[{"key":"ProteinId","value":"BAA10190.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S39561","properties":[{"key":"EntryName","value":"S39561"}]},{"database":"AlphaFoldDB","id":"P54205","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P54205","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"P54205","properties":[{"key":"Number of interactors","value":"132"}]},{"database":"IntAct","id":"P54205","properties":[{"key":"Interactions","value":"4"}]},{"database":"STRING","id":"1148.gene:10499687","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"1148-gene:10499687","properties":[{"key":"Description","value":"-"}]},{"database":"EnsemblBacteria","id":"BAA10190","properties":[{"key":"ProteinId","value":"BAA10190"},{"key":"GeneId","value":"BAA10190"}]},{"database":"KEGG","id":"syn:slr0009","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG1850","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"InParanoid","id":"P54205","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"P54205","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:MONOMER-750","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"4.1.1.39","properties":[{"key":"OrganismId","value":"382"}]},{"database":"SABIO-RK","id":"P54205","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000001425","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0031470","properties":[{"key":"GoTerm","value":"C:carboxysome"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"17993516"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016984","properties":[{"key":"GoTerm","value":"F:ribulose-bisphosphate carboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019253","properties":[{"key":"GoTerm","value":"P:reductive pentose-phosphate cycle"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd08212","properties":[{"key":"EntryName","value":"RuBisCO_large_I"},{"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":"HAMAP","id":"MF_01338","properties":[{"key":"EntryName","value":"RuBisCO_L_type1"},{"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":"InterPro","id":"IPR020888","properties":[{"key":"EntryName","value":"RuBisCO_lsuI"}]},{"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:SF17","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":"MVQAKAGFKAGVQDYRLTYYTPDYTPKDTDLLACFRMTPQPGVPAEEAAAAVAAESSTGTWTTVWTDNLTDLDRYKGRCYDLEAVPNEDNQYFAFIAYPLDLFEEGSVTNVLTSLVGNVFGFKALRALRLEDIRFPVALIKTFQGPPHGITVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVQEAIEKAQAETNEMKGHYLNVTAGTCEEMMKRAEFAKEIGTPIIMHDFFTGGFTANTTLARWCRDNGILLHIHRAMHAVVDRQKNHGIHFRVLAKCLRLSGGDHLHSGTVVGKLEGERGITMGFVDLMREDYVEEDRSRGIFFTQDYASMPGTMPVASGGIHVWHMPALVEIFGDDSCLQFGGGTLGHPWGNAPGATANRVALEACVQARNEGRNLAREGNDVIREACRWSPELAAACELWKEIKFEFEAMDTL","length":470,"molWeight":52491,"crc64":"45B9322482745B2B","md5":"92235BEE2FE1DD84C1423B9CDCA9D7FA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"INTERACTION":1,"SUBCELLULAR LOCATION":1,"PTM":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":2,"Binding site":9,"Site":1,"Modified residue":1,"Disulfide bond":1},"uniParcId":"UPI0000133362"}}