ID   GRDD_PEPAC              Reviewed;         385 AA.
AC   Q47878; Q9R5L3;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 2.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Glycine/sarcosine/betaine reductase complex component C subunit alpha;
DE            Short=Protein PC alpha;
DE            EC=1.21.4.2;
DE            EC=1.21.4.3;
DE            EC=1.21.4.4;
GN   Name=grdD;
OS   Peptoclostridium acidaminophilum (Eubacterium acidaminophilum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoclostridium.
OX   NCBI_TaxID=1731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF CYS-98 AND CYS-359.
RC   STRAIN=ATCC 49065 / DSM 3953 / al-2;
RX   PubMed=11737196; DOI=10.1046/j.0014-2956.2001.02590.x;
RA   Kohlstock U.-M., Rucknaegel K.P., Reuter M., Schierhorn A., Andreesen J.R.,
RA   Soehling B.;
RT   "Cys359 of GrdD is the active-site thiol that catalyses the final step of
RT   acetyl phosphate formation by glycine reductase from Eubacterium
RT   acidaminophilum.";
RL   Eur. J. Biochem. 268:6417-6425(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-210, AND PROTEIN SEQUENCE OF 2-30.
RC   STRAIN=ATCC 49065 / DSM 3953 / al-2;
RX   PubMed=1587286; DOI=10.1111/j.1432-1033.1992.tb16903.x;
RA   Schraeder T., Andreesen J.R.;
RT   "Purification and characterization of protein PC, a component of glycine
RT   reductase from Eubacterium acidaminophilum.";
RL   Eur. J. Biochem. 206:79-85(1992).
CC   -!- FUNCTION: In the first step of glycine, betaine and sarcosine
CC       reductases, the substrate is bound to component PB via a Schiff base
CC       intermediate. Then the PB-activated substrate is nucleophilically
CC       attacked by the selenol anion of component PA to transform it to a
CC       carboxymethylated selenoether and the respective amine. By action of
CC       component PC, acetyl phosphate is formed, leaving component PA in its
CC       oxidized state. Finally component PA becomes reduced by the thioredoxin
CC       system to start a new catalytic cycle of reductive deamination.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + acetyl phosphate + H2O + NH4(+) =
CC         [thioredoxin]-dithiol + glycine + H(+) + phosphate;
CC         Xref=Rhea:RHEA:12232, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:22191,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29950, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:57305; EC=1.21.4.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + acetyl phosphate + H2O + methylamine
CC         = [thioredoxin]-dithiol + H(+) + phosphate + sarcosine;
CC         Xref=Rhea:RHEA:12825, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:22191,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:43474, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57433, ChEBI:CHEBI:59338; EC=1.21.4.3;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + acetyl phosphate + H2O +
CC         trimethylamine = [thioredoxin]-dithiol + glycine betaine + H(+) +
CC         phosphate; Xref=Rhea:RHEA:11848, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17750,
CC         ChEBI:CHEBI:22191, ChEBI:CHEBI:29950, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:58389; EC=1.21.4.4;
CC   -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits. Component
CC       of the glycine, sarcosine and betaine reductase complexes, together
CC       with proteins A and B.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L04500; AAB93307.1; -; Genomic_DNA.
DR   PIR; S21222; S21222.
DR   AlphaFoldDB; Q47878; -.
DR   SMR; Q47878; -.
DR   BioCyc; MetaCyc:MON-20605; -.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0033795; F:betaine reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030699; F:glycine reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033794; F:sarcosine reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR003664; FA_synthesis.
DR   InterPro; IPR012116; Gly_reductase_pC_asu.
DR   Pfam; PF02504; FA_synthesis; 1.
DR   PIRSF; PIRSF036593; GrdD; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase.
FT   CHAIN           1..385
FT                   /note="Glycine/sarcosine/betaine reductase complex
FT                   component C subunit alpha"
FT                   /id="PRO_0000087602"
FT   ACT_SITE        359
FT   MUTAGEN         98
FT                   /note="C->S: No effect."
FT                   /evidence="ECO:0000269|PubMed:11737196"
FT   MUTAGEN         359
FT                   /note="C->A: No activity."
FT                   /evidence="ECO:0000269|PubMed:11737196"
SQ   SEQUENCE   385 AA;  40054 MW;  D2A83C45DC153C40 CRC64;
     MSDIKQMIGK TFMEIADAIE TGSFAGKVKV GITTLGSEHG VENLVKGAEL AAKDAAGFDI
     VLIGPKVETS LEVVEVATEE EAHKKMEELL DSGYIHSCVT VHYNFPIGVS TVGRVVTPGM
     GKEMFIATTT GTSAAQRVEA MVRNALYGII TAKSMGIENP TVGILNLDGA RAVERALKEL
     AGNGYPITFA ESLRADGGSV MRGNDLLGGA ADVMVTDSLT GNIMMKVFSS YTTGGSYEGL
     GYGYGPGIGD GYNRTILILS RASGVPVAAN AIKYAAKLAQ NNVKAIAAAE FKAAKAAGLE
     SILAGLSKDT KKASTEEEVK MPPKEVVTGT ISGVDVMDLE DAQKVLWKAG IYAESGMGCT
     GPIVMVNEAK VEEAAKILKD AGIVA