{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P54935","uniProtkbId":"GRDC_PEPAC","entryAudit":{"firstPublicDate":"1996-10-01","lastAnnotationUpdateDate":"2025-06-18","lastSequenceUpdateDate":"1997-11-01","entryVersion":76,"sequenceVersion":2},"annotationScore":3.0,"organism":{"scientificName":"Peptoclostridium acidaminophilum","commonName":"Eubacterium acidaminophilum","taxonId":1731,"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Peptostreptococcales","Peptoclostridiaceae","Peptoclostridium"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Glycine/sarcosine/betaine reductase complex component C subunit beta"},"shortNames":[{"value":"Protein PC beta"}],"ecNumbers":[{"value":"1.21.4.2"},{"value":"1.21.4.3"},{"value":"1.21.4.4"}]}},"genes":[{"geneName":{"value":"grdC"}}],"comments":[{"texts":[{"value":"In the first step of glycine, betaine and sarcosine reductases, the substrate is bound to component PB via a Schiff base intermediate. Then the PB-activated substrate is nucleophilically attacked by the selenol anion of component PA to transform it to a carboxymethylated selenoether and the respective amine. By action of component PC, acetyl phosphate is formed, leaving component PA in its oxidized state. Finally component PA becomes reduced by the thioredoxin system to start a new catalytic cycle of reductive deamination"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"acetyl phosphate + [thioredoxin]-disulfide + NH4(+) + H2O = [thioredoxin]-dithiol + glycine + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12232"},{"database":"Rhea","id":"RHEA-COMP:10698"},{"database":"Rhea","id":"RHEA-COMP:10700"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:22191"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:50058"},{"database":"ChEBI","id":"CHEBI:57305"}],"ecNumber":"1.21.4.2"}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"acetyl phosphate + methylamine + [thioredoxin]-disulfide + H2O = sarcosine + [thioredoxin]-dithiol + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12825"},{"database":"Rhea","id":"RHEA-COMP:10698"},{"database":"Rhea","id":"RHEA-COMP:10700"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:22191"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:50058"},{"database":"ChEBI","id":"CHEBI:57433"},{"database":"ChEBI","id":"CHEBI:59338"}],"ecNumber":"1.21.4.3"}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"acetyl phosphate + trimethylamine + [thioredoxin]-disulfide + H2O = glycine betaine + [thioredoxin]-dithiol + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11848"},{"database":"Rhea","id":"RHEA-COMP:10698"},{"database":"Rhea","id":"RHEA-COMP:10700"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17750"},{"database":"ChEBI","id":"CHEBI:22191"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:50058"},{"database":"ChEBI","id":"CHEBI:58389"}],"ecNumber":"1.21.4.4"}},{"texts":[{"value":"Heterooctamer of four alpha and four beta subunits. Component of the glycine, sarcosine and betaine reductase complexes, together with proteins A and B"}],"commentType":"SUBUNIT"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":513,"modifier":"EXACT"}},"description":"Glycine/sarcosine/betaine reductase complex component C subunit beta","featureId":"PRO_0000087601"}],"keywords":[{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-89ES2F6D3K6E9","citationType":"submission","authors":["Luebbers M.","Andreesen J.R."],"publicationDate":"MAY-1996","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"al-2 / ATCC 49065 / DSM 3953Z","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"8223622","citationType":"journal article","authors":["Luebbers M.","Andreesen J.R."],"citationCrossReferences":[{"database":"PubMed","id":"8223622"},{"database":"DOI","id":"10.1111/j.1432-1033.1993.tb18307.x"}],"title":"Components of glycine reductase from Eubacterium acidaminophilum. Cloning, sequencing and identification of the genes for thioredoxin reductase, thioredoxin and selenoprotein PA.","publicationDate":"1993","journal":"Eur. J. Biochem.","firstPage":"791","lastPage":"798","volume":"217"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23"],"referenceComments":[{"value":"al-2 / ATCC 49065 / DSM 3953Z","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"1587286","citationType":"journal article","authors":["Schraeder T.","Andreesen J.R."],"citationCrossReferences":[{"database":"PubMed","id":"1587286"},{"database":"DOI","id":"10.1111/j.1432-1033.1992.tb16903.x"}],"title":"Purification and characterization of protein PC, a component of glycine reductase from Eubacterium acidaminophilum.","publicationDate":"1992","journal":"Eur. J. Biochem.","firstPage":"79","lastPage":"85","volume":"206"},"referencePositions":["PROTEIN SEQUENCE OF 1-23"],"referenceComments":[{"value":"al-2 / ATCC 49065 / DSM 3953Z","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"L04500","properties":[{"key":"ProteinId","value":"AAB93306.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S38991","properties":[{"key":"EntryName","value":"S38991"}]},{"database":"AlphaFoldDB","id":"P54935","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P54935","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:MONOMER-20604","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0004315","properties":[{"key":"GoTerm","value":"F:3-oxoacyl-[acyl-carrier-protein] synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0033795","properties":[{"key":"GoTerm","value":"F:betaine reductase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0030699","properties":[{"key":"GoTerm","value":"F:glycine reductase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0033794","properties":[{"key":"GoTerm","value":"F:sarcosine reductase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006633","properties":[{"key":"GoTerm","value":"P:fatty acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00827","properties":[{"key":"EntryName","value":"init_cond_enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.47.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013751","properties":[{"key":"EntryName","value":"ACP_syn_III_N"}]},{"database":"InterPro","id":"IPR045984","properties":[{"key":"EntryName","value":"DUF5940"}]},{"database":"InterPro","id":"IPR017236","properties":[{"key":"EntryName","value":"Gly/sarc/bet/_Rdtase_C_bsu"}]},{"database":"InterPro","id":"IPR016039","properties":[{"key":"EntryName","value":"Thiolase-like"}]},{"database":"NCBIfam","id":"NF040746","properties":[{"key":"EntryName","value":"reduct_C_beta"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08545","properties":[{"key":"EntryName","value":"ACP_syn_III"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF19364","properties":[{"key":"EntryName","value":"DUF5940"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF037559","properties":[{"key":"EntryName","value":"Gly_sarc_betain_red_a"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53901","properties":[{"key":"EntryName","value":"Thiolase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNFPVLKGAGYVLVHTPDMIMHNGTTQTTEKIVNPESEYLKKLPEHLRSFEDVVAYAPNQTYIGSMTPEALGEIAMPWWTEDKKVAGADRYGKLGEIMPQDEFLALMSASDVFDLVLFEKEFIEGAKAKLAAHPVVGNLAESVNAGVELAEIEKQLSEFHAEGLYNNGKLVGCVKRAHDVDVNLNSHTMLENLAVKASGVLALANLIAKNNVNPAEVDYIIECSEEACGDMNQRGGGNFAKALAEMTGCVNATGSDMRGFCAGPTHALIAAAALVKSGVYKNVIIAAGGATAKLGMNGKDHVKKEMPILEDCLGGFAVLVSENDGVNPILRTDLVGRHTVATGSAPQAVIGSLVLSPLKAGGLKITDVDKYSVEMQNPDITKPAGAGDVPEANYKMIAALAVMGKEIERADIAAFVEKHGMVGWAPTQGHIPSGVPYIGFAISDLTEGSVNRTMIVGKGSLFLGRMTNLFDGVSIVAERNTGKVESGSSVSTEEIRKMIAESMKDFAAHLLAE","length":513,"molWeight":54458,"crc64":"957DC65C9EB2CC99","md5":"61460F6F885E3E405EAFECB2BD63B41E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"SUBUNIT":1},"countByFeatureType":{"Chain":1},"uniParcId":"UPI000012BA8F"}}