GRDA1_PHOPR
ID GRDA1_PHOPR Reviewed; 158 AA.
AC Q6LH20;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 02-JUN-2021, entry version 87.
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; OrderedLocusNames=PBPRB1548;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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 (By
CC similarity). {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GrdA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG23410.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR378679; CAG23410.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; WP_011221569.1; NC_006371.1.
DR STRING; 298386.PBPRB1548; -.
DR EnsemblBacteria; CAG23410; CAG23410; PBPRB1548.
DR KEGG; ppr:PBPRB1548; -.
DR eggNOG; ENOG50313TT; Bacteria.
DR HOGENOM; CLU_142275_0_0_6; -.
DR Proteomes; UP000000593; Chromosome 2.
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 A1"
FT /id="PRO_0000249761"
FT ACT_SITE 46
FT /evidence="ECO:0000250"
FT NON_STD 46
FT /note="Selenocysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 16749 MW; 430B761F82E5F652 CRC64;
MNKEVFATKT AIILGDRDGI PGQAIEACIK TTGAHVAFST TECFVUTSAG AMDLENQKRI
KALADEFGAE NIIVILGGAE AEASGLACET VTTGDPTFAG PLAGVQLGLS CYHVVEDAIK
EAVDPAVYEE QIGMMEMVLD VDAIKAEMQQ YREEPVEA
