ID   GRDA2_PHOPR             Reviewed;         161 AA.
AC   Q6LH19;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   02-JUN-2021, entry version 84.
DE   RecName: Full=Glycine/sarcosine/betaine reductase complex component A2;
DE            EC=1.21.4.2;
DE            EC=1.21.4.3;
DE            EC=1.21.4.4;
DE   AltName: Full=Selenoprotein PA 2;
DE   AltName: Full=Thioredoxin reductase complex selenoprotein A 2;
GN   Name=grdA2; OrderedLocusNames=PBPRB1549;
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=CAG23411.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR378679; CAG23411.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; WP_006229103.1; NC_006371.1.
DR   STRING; 298386.PBPRB1549; -.
DR   EnsemblBacteria; CAG23411; CAG23411; PBPRB1549.
DR   KEGG; ppr:PBPRB1549; -.
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..161
FT                   /note="Glycine/sarcosine/betaine reductase complex
FT                   component A2"
FT                   /id="PRO_0000249762"
FT   ACT_SITE        42
FT                   /evidence="ECO:0000250"
FT   NON_STD         42
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   161 AA;  17193 MW;  660CA11CAFD073AB CRC64;
     MLKDKKVIIL GDRDGIPGQA IEACIKSAGA HVLFSTTECF VUTSAGAMDL ENQKRIKGFA
     EEFGAENILI VLGGAEAEAS GLACETVTNG DPTFAGPLAG VQLGLSCYHV VEPEIKNNVD
     ADVYDEQIGM MEMVLDVDAI IAEIKGYREQ FGKYVLAEAE V