GRDA_TREDE
ID GRDA_TREDE Reviewed; 157 AA.
AC Q73PQ2;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 91.
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; OrderedLocusNames=TDE_0745;
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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}.
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DR EMBL; AE017226; AAS11237.1; -; Genomic_DNA.
DR RefSeq; NP_971356.1; NC_002967.9.
DR RefSeq; WP_010956809.1; NC_002967.9.
DR STRING; 243275.TDE_0745; -.
DR GeneID; 2740299; -.
DR KEGG; tde:TDE_0745; -.
DR PATRIC; fig|243275.7.peg.720; -.
DR eggNOG; ENOG50313TT; Bacteria.
DR HOGENOM; CLU_142275_0_0_12; -.
DR OMA; IAMMEMV; -.
DR OrthoDB; 1960942at2; -.
DR Proteomes; UP000008212; 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..157
FT /note="Glycine/sarcosine/betaine reductase complex
FT component A"
FT /id="PRO_0000249764"
FT ACT_SITE 44
FT /evidence="ECO:0000250"
FT NON_STD 44
FT /note="Selenocysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 157 AA; 16711 MW; 832BF2DDF8053BD1 CRC64;
MVDLKTKKVI IIGDRDGVPG EAIKLCAESA GAEVVYAATE CFVUTSAGAM DLENQKRVKD
LAEKYGPENV IVLLGGAEAE SSGLACETVT VGDPTFAGPL AGVSLGLLCY HVAEPEIKSQ
IDPAVYEEQV SMMEMVMDVN AIIAEISEYR NKGCKFL
