GRDA_ALKMQ
ID GRDA_ALKMQ Reviewed; 158 AA.
AC A6TU46;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 66.
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=Amet_3592;
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF;
RX PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
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; CP000724; ABR49714.1; -; Genomic_DNA.
DR STRING; 293826.Amet_3592; -.
DR PRIDE; A6TU46; -.
DR KEGG; amt:Amet_3592; -.
DR eggNOG; ENOG50313TT; Bacteria.
DR HOGENOM; CLU_142275_0_0_9; -.
DR Proteomes; UP000001572; 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..158
FT /note="Glycine/sarcosine/betaine reductase complex
FT component A"
FT /id="PRO_1000062704"
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; 16991 MW; C12515841284C79D CRC64;
MSLFDGKKVI IIGDRDGIPG PAMEECLKGT GAEVVYSSTE CFVUTAAGAM DLENQKRVMD
LTEKHNAENV VVILGAAEAE AAGLAAETVT NGDPTFAGPL AGVQLGLRVY HAVEPQFKDA
VNAEVYEDQI GMMEMVLEVD AIIEEMSNIR NEFGKFKD
