GRDA_ACESD
ID GRDA_ACESD Reviewed; 158 AA.
AC P26971; E3PXR8; Q7B074;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 4.
DT 29-SEP-2021, entry version 109.
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=CLOST_1112;
OS Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS 9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Acetoanaerobium.
OX NCBI_TaxID=499177;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX PubMed=1429431; DOI=10.1128/jb.174.22.7080-7089.1992;
RA Garcia G.E., Stadtman T.C.;
RT "Clostridium sticklandii glycine reductase selenoprotein A gene: cloning,
RT sequencing, and expression in Escherichia coli.";
RL J. Bacteriol. 174:7080-7089(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX PubMed=11271425; DOI=10.1007/s002030000232;
RA Graentzdoerffer A., Pich A., Andreesen J.R.;
RT "Molecular analysis of the grd-operon encoded proteins of the glycine
RT reductase and thioredoxin system from Clostridium sticklandii.";
RL Arch. Microbiol. 175:8-18(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT its metabolism through its genome sequence.";
RL BMC Genomics 11:555-555(2010).
RN [4]
RP PROTEIN SEQUENCE OF 2-158, AND SELENOCYSTEINE AT SEC-44.
RX PubMed=7892245; DOI=10.1073/pnas.92.6.2189;
RA Kimura Y., Stadtman T.C.;
RT "Glycine reductase selenoprotein A is not a glycoprotein: the positive
RT periodic acid-Schiff reagent test is the result of peptide bond cleavage
RT and carbonyl group generation.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:2189-2193(1995).
RN [5]
RP PRELIMINARY PROTEIN SEQUENCE OF 41-56, AND SELENOCYSTEINE AT SEC-44.
RX PubMed=2963330; DOI=10.1073/pnas.85.2.368;
RA Sliwkowski M.X., Stadtman T.C.;
RT "Selenoprotein A of the clostridial glycine reductase complex: purification
RT and amino acid sequence of the selenocysteine-containing peptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:368-371(1988).
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; M60399; AAB02347.2; -; Genomic_DNA.
DR EMBL; AJ276209; CAC14300.1; -; Genomic_DNA.
DR EMBL; FP565809; CBH21233.1; -; Genomic_DNA.
DR PIR; A47011; A47011.
DR STRING; 1511.CLOST_1112; -.
DR KEGG; cst:CLOST_1112; -.
DR eggNOG; ENOG50313TT; Bacteria.
DR HOGENOM; CLU_142275_0_0_9; -.
DR OMA; FASTECF; -.
DR BRENDA; 1.21.4.2; 1522.
DR Proteomes; UP000007041; 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 1: Evidence at protein level;
KW Direct protein sequencing; Oxidoreductase; Reference proteome;
KW Selenocysteine.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7892245"
FT CHAIN 2..158
FT /note="Glycine/sarcosine/betaine reductase complex
FT component A"
FT /id="PRO_0000194466"
FT ACT_SITE 44
FT NON_STD 44
FT /note="Selenocysteine"
SQ SEQUENCE 158 AA; 17140 MW; 7E51D032C1B102E4 CRC64;
MSRFTGKKIV IIGDRDGIPG PAIEECLKPI DCEVIFSSTE CFVUTAAGAM DLENQKRIKE
ATEKFGAENL VVLIGAAEAE AAGLAAETVT AGDPTFAGPL AGVELGLRVY HAVEPEFKDE
VDAQIFDDQV GMMEMVLNVD EIIEEMQSIR SQFCKFND
