GRDA_PEPLI
ID GRDA_PEPLI Reviewed; 158 AA.
AC P52216;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 02-JUN-2021, entry version 75.
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 Peptoclostridium litorale (Clostridium litorale).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptoclostridium.
OX NCBI_TaxID=1557;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SELENOCYSTEINE AT SEC-44.
RC STRAIN=ATCC 49638 / DSM 5388 / W6;
RX PubMed=8529640; DOI=10.1111/j.1432-1033.1995.192_c.x;
RA Kreimer S., Andreesen J.R.;
RT "Glycine reductase of Clostridium litorale. Cloning, sequencing, and
RT molecular analysis of the grdAB operon that contains two in-frame TGA
RT codons for selenium incorporation.";
RL Eur. J. Biochem. 234:192-199(1995).
RN [2]
RP PROTEIN SEQUENCE OF 1-38.
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).
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; U24268; AAC43573.2; -; Genomic_DNA.
DR PIR; S63987; S63987.
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..158
FT /note="Glycine/sarcosine/betaine reductase complex
FT component A"
FT /id="PRO_0000194464"
FT ACT_SITE 44
FT NON_STD 44
FT /note="Selenocysteine"
FT CONFLICT 2
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="M -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30..33
FT /note="INVE -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 16909 MW; 86FA601E64A4EF38 CRC64;
MSLFDGKKVI IIGDRDGIPG PAMAECLKGI NVEVVYSATE CFVUTAAGAM DLENQNWVKN
FTDQYGAENI IVLVGAAEAE SAGLAAETVT AGDPTFAGPL AGVQLGLRVF HAVEPEFKGA
VDSAIYDEQI GMMEMVLDVD SIIEEMKSIR ADYCKFND
