{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P06960","secondaryAccessions":["P78308","Q2MCE9"],"uniProtkbId":"OTC2_ECOLI","entryAudit":{"firstPublicDate":"1988-04-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-01-23","entryVersion":193,"sequenceVersion":4},"annotationScore":4.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"789338"}],"value":"Ornithine carbamoyltransferase subunit F"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"789338"}],"value":"OTCase-2"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"value":"2.1.3.3"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"789338"}],"value":"argF"},"orderedLocusNames":[{"value":"b0273"},{"value":"JW0266"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"789338"}],"value":"Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"carbamoyl phosphate + L-ornithine = L-citrulline + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19513"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46911"},{"database":"ChEBI","id":"CHEBI:57743"},{"database":"ChEBI","id":"CHEBI:58228"}],"ecNumber":"2.1.3.3","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":0.02,"unit":"mM","substrate":"carbamoyl phosphate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"789338"}]},{"constant":5.0,"unit":"mM","substrate":"L-ornithine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"789338"}]}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4558857"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"789338"}],"value":"In E.coli strain K12, trimer of identical or non-identical chains are composed of ArgI (I) and/or ArgF (F). The trimer has the following composition: FFI, FFF, FII, III. E.coli strains B and W, which are known to contain only ArgI, produce only a trimer of identical chains (III)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"4558857"}],"value":"ArgF might be the product of a relatively recent event (duplication or transposition) peculiar to E.coli strain K-12"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3968036"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"Ornithine carbamoyltransferase subunit F","featureId":"PRO_0000112919"},{"type":"Binding site","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":83,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46911"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"L-ornithine","id":"ChEBI:CHEBI:46911"}},{"type":"Binding site","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46911"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"L-ornithine","id":"ChEBI:CHEBI:46911"}},{"type":"Binding site","location":{"start":{"value":236,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46911"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"L-ornithine","id":"ChEBI:CHEBI:46911"}},{"type":"Binding site","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01109"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Sequence conflict","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"in Ref. 1; CAA25329","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"A","alternativeSequences":["P"]}}],"keywords":[{"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"6382166","citationType":"journal article","authors":["van Vliet F.","Cunin R.","Jacobs A.","Piette J.","Gigot D.","Lauwereys M.","Pierard A.","Glansdorff N."],"citationCrossReferences":[{"database":"PubMed","id":"6382166"},{"database":"DOI","id":"10.1093/nar/12.15.6277"}],"title":"Evolutionary divergence of genes for ornithine and aspartate carbamoyl-transferases -- complete sequence and mode of regulation of the Escherichia coli argF gene; comparison of argF with argI and pyrB.","publicationDate":"1984","journal":"Nucleic Acids Res.","firstPage":"6277","lastPage":"6289","volume":"12"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":2,"citation":{"id":"CI-B1UJ6TNQ0SAS1","citationType":"submission","authors":["Chung E.","Allen E.","Araujo R.","Aparicio A.M.","Davis K.","Duncan M.","Federspiel N.","Hyman R.","Kalman S.","Komp C.","Kurdi O.","Lew H.","Lin D.","Namath A.","Oefner P.","Roberts D.","Schramm S.","Davis R.W."],"title":"Sequence of minutes 4-25 of Escherichia coli.","publicationDate":"JAN-1997","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / MG1655 / ATCC 47076","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"9278503","citationType":"journal article","authors":["Blattner F.R.","Plunkett G. III","Bloch C.A.","Perna N.T.","Burland V.","Riley M.","Collado-Vides J.","Glasner J.D.","Rode C.K.","Mayhew G.F.","Gregor J.","Davis N.W.","Kirkpatrick H.A.","Goeden M.A.","Rose D.J.","Mau B.","Shao Y."],"citationCrossReferences":[{"database":"PubMed","id":"9278503"},{"database":"DOI","id":"10.1126/science.277.5331.1453"}],"title":"The complete genome sequence of Escherichia coli K-12.","publicationDate":"1997","journal":"Science","firstPage":"1453","lastPage":"1462","volume":"277"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / MG1655 / ATCC 47076","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"16738553","citationType":"journal article","authors":["Hayashi K.","Morooka N.","Yamamoto Y.","Fujita K.","Isono K.","Choi S.","Ohtsubo E.","Baba T.","Wanner B.L.","Mori H.","Horiuchi T."],"citationCrossReferences":[{"database":"PubMed","id":"16738553"},{"database":"DOI","id":"10.1038/msb4100049"}],"title":"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.","publicationDate":"2006","journal":"Mol. Syst. Biol.","firstPage":"E1","lastPage":"E5","volume":"2"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":5,"citation":{"id":"3968036","citationType":"journal article","authors":["Falmagne P.","Portetelle D.","Stalon V."],"citationCrossReferences":[{"database":"PubMed","id":"3968036"},{"database":"DOI","id":"10.1128/jb.161.2.714-719.1985"}],"title":"Immunological and structural relatedness of catabolic ornithine carbamoyltransferases and the anabolic enzymes of enterobacteria.","publicationDate":"1985","journal":"J. Bacteriol.","firstPage":"714","lastPage":"719","volume":"161"},"referencePositions":["PROTEIN SEQUENCE OF 2-41"]},{"referenceNumber":6,"citation":{"id":"4558857","citationType":"journal article","authors":["Legrain C.","Halleux P.","Stalon V.","Glansdorff N."],"citationCrossReferences":[{"database":"PubMed","id":"4558857"},{"database":"DOI","id":"10.1111/j.1432-1033.1972.tb01814.x"}],"title":"The dual genetic control of ornithine carbamolytransferase in Escherichia coli. A case of bacterial hybrid enzymes.","publicationDate":"1972","journal":"Eur. J. Biochem.","firstPage":"93","lastPage":"102","volume":"27"},"referencePositions":["SUBUNIT"]},{"referenceNumber":7,"citation":{"id":"789338","citationType":"journal article","authors":["Legrain C.","Stalon V.","Glansdorff N."],"citationCrossReferences":[{"database":"PubMed","id":"789338"},{"database":"DOI","id":"10.1128/jb.128.1.35-38.1976"}],"title":"Escherichia coli ornithine carbamolytransferase isoenzymes: evolutionary significance and the isolation of lambdaargF and lambdaargI transducing bacteriophages.","publicationDate":"1976","journal":"J. Bacteriol.","firstPage":"35","lastPage":"38","volume":"128"},"referencePositions":["FUNCTION","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X00759","properties":[{"key":"ProteinId","value":"CAA25329.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"U70214","properties":[{"key":"ProteinId","value":"AAB08694.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"U00096","properties":[{"key":"ProteinId","value":"AAC73376.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AP009048","properties":[{"key":"ProteinId","value":"BAE76057.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"A64753","properties":[{"key":"EntryName","value":"OWECF"}]},{"database":"RefSeq","id":"NP_414807.1","properties":[{"key":"NucleotideSequenceId","value":"NC_000913.3"}]},{"database":"RefSeq","id":"WP_001281825.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP009789.1"}]},{"database":"AlphaFoldDB","id":"P06960","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P06960","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"4261491","properties":[{"key":"Interactions","value":"21"}]},{"database":"ComplexPortal","id":"CPX-5625","properties":[{"key":"EntryName","value":"Ornithine transcarbamoylase complex, argFII variant"}]},{"database":"ComplexPortal","id":"CPX-5626","properties":[{"key":"EntryName","value":"Ornithine transcarbamoylase complex, argFFI variant"}]},{"database":"ComplexPortal","id":"CPX-5627","properties":[{"key":"EntryName","value":"Ornithine transcarbamoylase complex, argFFF variant"}]},{"database":"FunCoup","id":"P06960","properties":[{"key":"Number of interactors","value":"603"}]},{"database":"IntAct","id":"P06960","properties":[{"key":"Interactions","value":"7"}]},{"database":"STRING","id":"511145.b0273","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"511145-b0273","properties":[{"key":"Description","value":"-"}]},{"database":"EnsemblBacteria","id":"AAC73376","properties":[{"key":"ProteinId","value":"AAC73376"},{"key":"GeneId","value":"b0273"}]},{"database":"GeneID","id":"944844","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecj:JW0266","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"eco:b0273","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecoc:C3026_01325","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1411691.4.peg.2007","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"EchoBASE","id":"EB0065","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG0078","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"HOGENOM","id":"CLU_043846_3_1_6","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"P06960","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"CISHKHF","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"OrthoDB","id":"9802587at2","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"P06960","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"EcoCyc:CHAINF-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:CHAINF-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"SABIO-RK","id":"P06960","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00068","properties":[{"key":"RectionId","value":"UER00112"}]},{"database":"PRO","id":"PR:P06960","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000000625","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"AbasyAtlas","id":"P06960","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0016597","properties":[{"key":"GoTerm","value":"F:amino acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004585","properties":[{"key":"GoTerm","value":"F:ornithine carbamoyltransferase activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"4558857"}]},{"database":"GO","id":"GO:0006974","properties":[{"key":"GoTerm","value":"P:DNA damage response"},{"key":"GoEvidenceType","value":"IEP:EcoliWiki"}],"evidences":[{"evidenceCode":"ECO:0000270","source":"PubMed","id":"11967071"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019240","properties":[{"key":"GoTerm","value":"P:L-citrulline biosynthetic process"},{"key":"GoEvidenceType","value":"IDA:ComplexPortal"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"4558857"}]},{"database":"FunFam","id":"3.40.50.1370:FF:000004","properties":[{"key":"EntryName","value":"Ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1370","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01109","properties":[{"key":"EntryName","value":"OTCase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006132","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoyltranf_P-bd"}]},{"database":"InterPro","id":"IPR006130","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase"}]},{"database":"InterPro","id":"IPR036901","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase_sf"}]},{"database":"InterPro","id":"IPR006131","properties":[{"key":"EntryName","value":"Asp_carbamoyltransf_Asp/Orn-bd"}]},{"database":"InterPro","id":"IPR002292","properties":[{"key":"EntryName","value":"Orn/put_carbamltrans"}]},{"database":"InterPro","id":"IPR024904","properties":[{"key":"EntryName","value":"OTCase_ArgI"}]},{"database":"NCBIfam","id":"TIGR00658","properties":[{"key":"EntryName","value":"orni_carb_tr"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009213","properties":[{"key":"EntryName","value":"PRK12562.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45753:SF4","properties":[{"key":"EntryName","value":"ORNITHINE CARBAMOYLTRANSFERASE SUBUNIT F-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45753","properties":[{"key":"EntryName","value":"ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00185","properties":[{"key":"EntryName","value":"OTCace"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02729","properties":[{"key":"EntryName","value":"OTCace_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00100","properties":[{"key":"EntryName","value":"AOTCASE"}]},{"database":"PRINTS","id":"PR00102","properties":[{"key":"EntryName","value":"OTCASE"}]},{"database":"SUPFAM","id":"SSF53671","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00097","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSDLYKKHFLKLLDFTPAQFTSLLTLAAQLKADKKNGKEVQKLTGKNIALIFEKDSTRTRCSFEVAAFDQGARVTYLGPSGSQIGHKESIKDTARVLGRMYDGIQYRGHGQEVVETLAQYAGVPVWNGLTNEFHPTQLLADLMTMQEHLPGKAFNEMTLVYAGDARNNMGNSMLEAAALTGLDLRLLAPKACWPEESLVAECSALAEKHGGKITLTEDVAAGVKGADFIYTDVWVSMGEAKEKWAERIALLRGYQVNAQMMALTDNPNVKFLHCLPAFHDDQTTLGKQMAKEFDLHGGMEVTDEVFESAASIVFDQAENRMHTIKAVMMATLGE","length":334,"molWeight":36827,"crc64":"C1EA07CD2AFC39C4","md5":"54625B44F67ED33FF02E0B4BE34A5262"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Binding site":9,"Sequence conflict":1},"uniParcId":"UPI000016801A"}}