GRDA1_PEPAC
ID GRDA1_PEPAC Reviewed; 158 AA.
AC P50972;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Glycine/sarcosine/betaine reductase complex component A1;
DE EC=1.21.4.2;
DE EC=1.21.4.3;
DE EC=1.21.4.4;
DE AltName: Full=Selenoprotein PA 1;
DE AltName: Full=Thioredoxin reductase complex selenoprotein A 1;
GN Name=grdA1; Synonyms=grdA;
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=8223622; DOI=10.1111/j.1432-1033.1993.tb18307.x;
RA Luebbers M., Andreesen J.R.;
RT "Components of glycine reductase from Eubacterium acidaminophilum. Cloning,
RT sequencing and identification of the genes for thioredoxin reductase,
RT thioredoxin and selenoprotein PA.";
RL Eur. J. Biochem. 217:791-798(1993).
RN [2]
RP PROTEIN SEQUENCE OF 2-49, AND SELENOCYSTEINE AT SEC-44.
RC STRAIN=ATCC 49065 / DSM 3953 / al-2;
RX PubMed=1917832; DOI=10.1128/jb.173.19.5983-5991.1991;
RA Dietrichs D., Meyer M., Rieth M., Andreesen J.R.;
RT "Interaction of selenoprotein PA and the thioredoxin system, components of
RT the NADPH-dependent reduction of glycine in Eubacterium acidaminophilum and
RT Clostridium litorale.";
RL J. Bacteriol. 173:5983-5991(1991).
RN [3]
RP ERRATUM OF PUBMED:1917832.
RA Dietrichs D., Meyer M., Rieth M., Andreesen J.R.;
RL J. Bacteriol. 174:1432-1432(1992).
RN [4]
RP PROTEIN SEQUENCE OF 2-45, AND SELENOCYSTEINE AT SEC-44.
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; L04500; AAB93305.2; -; Genomic_DNA.
DR PIR; S38990; S38990.
DR BioCyc; MetaCyc:MON-20600; -.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10091582,
FT ECO:0000269|PubMed:1917832"
FT CHAIN 2..158
FT /note="Glycine/sarcosine/betaine reductase complex
FT component A1"
FT /id="PRO_0000194467"
FT ACT_SITE 44
FT NON_STD 44
FT /note="Selenocysteine"
SQ SEQUENCE 158 AA; 16656 MW; 841421989007258E CRC64;
MSLFDGKKVI IIGDRDGIPG PAIAECLKGT AAEVVYSATE CFVUTAAGAM DLENQNRVKG
FADQFGAENL VVLVGAAEAE SAGLAAETVT AGDPTFAGPL AGVQLGLRVF HAVEPEFKDA
VDSAVYDEQI GMMEMVLDVD SIIAEMKSIR EQFGKFND
