ID   GRDA_CLOBL              Reviewed;         158 AA.
AC   A7GCV1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   02-JUN-2021, entry version 60.
DE   RecName: Full=Glycine/sarcosine/betaine reductase complex component A {ECO:0000255|HAMAP-Rule:MF_00826};
DE            EC=1.21.4.2 {ECO:0000255|HAMAP-Rule:MF_00826};
DE            EC=1.21.4.3 {ECO:0000255|HAMAP-Rule:MF_00826};
DE            EC=1.21.4.4 {ECO:0000255|HAMAP-Rule:MF_00826};
DE   AltName: Full=Selenoprotein PA {ECO:0000255|HAMAP-Rule:MF_00826};
DE   AltName: Full=Thioredoxin reductase complex selenoprotein A {ECO:0000255|HAMAP-Rule:MF_00826};
GN   Name=grdA {ECO:0000255|HAMAP-Rule:MF_00826}; OrderedLocusNames=CLI_1346;
OS   Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Langeland / NCTC 10281 / Type F;
RA   Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA   Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000255|HAMAP-Rule:MF_00826}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00826};
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00826};
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00826};
CC   -!- SUBUNIT: Monomer. Component of the glycine, sarcosine and betaine
CC       reductase complexes, together with components B and C.
CC       {ECO:0000255|HAMAP-Rule:MF_00826}.
CC   -!- SIMILARITY: Belongs to the GrdA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00826}.
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DR   EMBL; CP000728; ABS41814.1; -; Genomic_DNA.
DR   KEGG; cbf:CLI_1346; -.
DR   HOGENOM; CLU_142275_0_0_9; -.
DR   Proteomes; UP000002410; 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; Selenocysteine.
FT   CHAIN           1..158
FT                   /note="Glycine/sarcosine/betaine reductase complex
FT                   component A"
FT                   /id="PRO_1000062706"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00826"
FT   NON_STD         44
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   158 AA;  17221 MW;  D2E231B6FE1204A9 CRC64;
     MSLFEGKKVI IIGDRDGIPG PAIEKCIEGT GAEVVFSSTE CFVUTAAGAM DLENQKRVKT
     LTEKHGAENI LVILGAAEGE AAGLAAETVT NGDPTFAGPL SNVQLGLRVY HAVEPEFKEE
     VNEEVYEEEI GMMEMVLEVD EIIEEMTDIR TEFCKFLD