ID   GRDA_GOTPU              Reviewed;         150 AA.
AC   P26970;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Glycine/sarcosine/betaine reductase complex component A;
DE            EC=1.21.4.2;
DE            EC=1.21.4.3;
DE            EC=1.21.4.4;
DE   AltName: Full=Selenoprotein PA;
DE   AltName: Full=Thioredoxin reductase complex selenoprotein A;
GN   Name=grdA;
OS   Gottschalkia purinilytica (Clostridium purinilyticum).
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Gottschalkiaceae;
OC   Gottschalkia.
OX   NCBI_TaxID=1503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP   SELENOCYSTEINE AT SEC-43.
RC   STRAIN=ATCC 33906 / DSM 1384 / WA1;
RX   PubMed=1825826; DOI=10.1128/jb.173.6.2093-2098.1991;
RA   Garcia G.E., Stadtman T.C.;
RT   "Selenoprotein A component of the glycine reductase complex from
RT   Clostridium purinolyticum: nucleotide sequence of the gene shows that
RT   selenocysteine is encoded by UGA.";
RL   J. Bacteriol. 173:2093-2098(1991).
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; M64374; AAB02121.2; -; Genomic_DNA.
DR   PIR; A38540; A38540.
DR   BioCyc; MetaCyc:MON-13142; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase; Selenocysteine.
FT   CHAIN           1..150
FT                   /note="Glycine/sarcosine/betaine reductase complex
FT                   component A"
FT                   /id="PRO_0000194465"
FT   ACT_SITE        43
FT   NON_STD         43
FT                   /note="Selenocysteine"
FT   CONFLICT        14
FT                   /note="R -> D (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   150 AA;  15762 MW;  716C032DBB96766A CRC64;
     MILQGKKVIA IGDRDGIPGP AIEECVKSAG AEIAFSSTEC FVUTAAGAMD LEIQQKVKDA
     AESIGADNLV VVLGGAEAES SGLSAETVTT GDPTYAGPLA GVELGLKVYH VVEDELKAEF
     DEAIYEDQCG MMEMVLDVDG IKEEMNRVRG