ID   GRDA_CARHZ              Reviewed;         156 AA.
AC   Q3A9J5;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   07-APR-2021, entry version 79.
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; OrderedLocusNames=CHY_2392;
OS   Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS   Z-2901).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Carboxydothermus.
OX   NCBI_TaxID=246194;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX   PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA   Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA   Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA   Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT   "Life in hot carbon monoxide: the complete genome sequence of
RT   Carboxydothermus hydrogenoformans Z-2901.";
RL   PLoS Genet. 1:563-574(2005).
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 (By
CC       similarity). {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GrdA family. {ECO:0000305}.
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DR   EMBL; CP000141; ABB15572.1; -; Genomic_DNA.
DR   STRING; 246194.CHY_2392; -.
DR   KEGG; chy:CHY_2392; -.
DR   eggNOG; ENOG50313TT; Bacteria.
DR   HOGENOM; CLU_142275_0_0_9; -.
DR   OMA; FASTECF; -.
DR   Proteomes; UP000002706; Chromosome.
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; Reference proteome; Selenocysteine.
FT   CHAIN           1..156
FT                   /note="Glycine/sarcosine/betaine reductase complex
FT                   component A"
FT                   /id="PRO_0000249760"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000250"
FT   NON_STD         44
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   156 AA;  16198 MW;  51C3F41617919986 CRC64;
     MAILAGKKVI AVGDRDGVPG PAIAECAKSA GAEVVFATTE CFVUTAAGTM DLQNQARIKE
     LAEELGGENI VVLLGAAEPD TASLAAETVT LGDPTFAGPL AGVSLGLKVY HILEPEIKAE
     IDPAVYEEQA AMMEMVLDVD ALAAEVSKMR KEGSKY