ID   GPR_ECO57               Reviewed;         346 AA.
AC   Q8X529;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=L-glyceraldehyde 3-phosphate reductase;
DE            Short=GAP reductase;
DE            EC=1.1.1.-;
GN   Name=gpr; Synonyms=yghZ; OrderedLocusNames=Z4354, ECs3885;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the stereospecific, NADPH-dependent reduction of L-
CC       glyceraldehyde 3-phosphate (L-GAP). The physiological role of gpr is
CC       the detoxification of L-GAP, which may be formed by non-enzymatic
CC       racemization of GAP. Also involved in the stress response as a
CC       methylglyoxal reductase which converts the toxic metabolite
CC       methylglyoxal to acetol in vitro and in vivo (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the shaker potassium channel beta subunit
CC       family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG58137.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37308.1; -; Genomic_DNA.
DR   PIR; E85959; E85959.
DR   PIR; E91114; E91114.
DR   RefSeq; NP_311912.1; NC_002695.1.
DR   RefSeq; WP_000262146.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8X529; -.
DR   SMR; Q8X529; -.
DR   STRING; 155864.EDL933_4223; -.
DR   EnsemblBacteria; AAG58137; AAG58137; Z4354.
DR   EnsemblBacteria; BAB37308; BAB37308; ECs_3885.
DR   GeneID; 916499; -.
DR   KEGG; ece:Z4354; -.
DR   KEGG; ecs:ECs_3885; -.
DR   PATRIC; fig|386585.9.peg.4053; -.
DR   eggNOG; COG0667; Bacteria.
DR   HOGENOM; CLU_023205_2_0_6; -.
DR   OMA; YSMINRW; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; ISS:UniProtKB.
DR   GO; GO:0009438; P:methylglyoxal metabolic process; ISS:UniProtKB.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR005399; K_chnl_volt-dep_bsu_KCNAB-rel.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   PANTHER; PTHR43150; PTHR43150; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   SUPFAM; SSF51430; SSF51430; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..346
FT                   /note="L-glyceraldehyde 3-phosphate reductase"
FT                   /id="PRO_0000201332"
FT   SITE            61
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            66
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            97
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            138
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   346 AA;  38815 MW;  94E871F8E6596D5A CRC64;
     MVWLANPERY GQMQYRYCGK SGLRLPALSL GLWHNFGHVN ALESQRAILR KAFDLGITHF
     DLANNYGPPP GSAEENFGRL LREDFAAYRD ELIISTKAGY DMWPGPYGSG GSRKYLLASL
     DQSLKRMGLE YVDIFYSHRV DENTPMEETA SALAHAVQSG KALYVGISSY SPERTQKMVE
     LLHEWKIPLL IHQPSYNLLN RWVDKSGLLD TLQNNGVGCI AFTPLAQGLL TGKYLNGIPE
     DSRMHREGNK VRGLTPKMLT EANLNSLRLL NEMAQQRGQS MAQMALSWLL KDERVTSVLV
     GASRAEQLEE NVQALNNLTF STEELAQIDQ HIADGELNLW QASSDK