ID   GRDA2_PEPAC             Reviewed;         158 AA.
AC   O32518;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   02-JUN-2021, entry version 67.
DE   RecName: Full=Glycine/sarcosine/betaine reductase complex component A2;
DE            EC=1.21.4.2;
DE            EC=1.21.4.3;
DE            EC=1.21.4.4;
DE   AltName: Full=Selenoprotein PA 2;
DE   AltName: Full=Thioredoxin reductase complex selenoprotein A 2;
GN   Name=grdA2;
OS   Peptoclostridium acidaminophilum (Eubacterium acidaminophilum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoclostridium.
OX   NCBI_TaxID=1731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49065 / DSM 3953 / al-2;
RX   PubMed=10091582; DOI=10.1046/j.1432-1327.1999.00107.x;
RA   Wagner M., Sonntag D., Grimm R., Pich A., Eckerskorn C., Soehling B.,
RA   Andreesen J.R.;
RT   "Substrate-specific selenoprotein B of glycine reductase from Eubacterium
RT   acidaminophilum. Biochemical and molecular analysis.";
RL   Eur. J. Biochem. 260:38-49(1999).
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: Monomer. Component of the glycine, sarcosine and betaine
CC       reductase complexes, together with components B and C.
CC   -!- SIMILARITY: Belongs to the GrdA family. {ECO:0000305}.
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DR   EMBL; Y14275; CAA74650.1; -; Genomic_DNA.
DR   KEGG; ag:CAA74650; -.
DR   GO; GO:0030700; C:glycine reductase complex; IEA:InterPro.
DR   GO; GO:0033795; F:betaine reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030699; F:glycine reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0033794; F:sarcosine reductase activity; IEA:UniProtKB-EC.
DR   HAMAP; MF_00826; GRDA; 1.
DR   InterPro; IPR006812; GRDA.
DR   Pfam; PF04723; GRDA; 1.
DR   PIRSF; PIRSF000181; Grc_selenoprot_A; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Selenocysteine.
FT   CHAIN           1..158
FT                   /note="Glycine/sarcosine/betaine reductase complex
FT                   component A2"
FT                   /id="PRO_0000194468"
FT   ACT_SITE        44
FT   NON_STD         44
FT                   /note="Selenocysteine"
SQ   SEQUENCE   158 AA;  16814 MW;  D88329839E0D8C99 CRC64;
     MSIFDGKKVI IIGDRDGIPG PAMAECLKGT GAEVVYSATE CFVUTAAGAM DLENQNRVKS
     FTEQYGAENM IVLVGAAEAE SAGLAAETVT AGDPTFAGPL AGVQLGLRVF HAVEPEFKDS
     VDSAVYDEQI GMMEMVLDVD SIIAEMKSIR EQFGKYND