GPR_ECOLI
ID GPR_ECOLI Reviewed; 346 AA.
AC Q46851; Q2M9J6;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=L-glyceraldehyde 3-phosphate reductase;
DE Short=GAP reductase;
DE EC=1.1.1.-;
GN Name=gpr; Synonyms=mgrA, yghZ; OrderedLocusNames=b3001, JW2970;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION IN THE METHYLGLYOXAL DETOXIFICATION AND AS A REDUCTASE.
RX PubMed=12583903; DOI=10.1111/j.1574-6968.2003.tb11503.x;
RA Grant A.W., Steel G., Waugh H., Ellis E.M.;
RT "A novel aldo-keto reductase from Escherichia coli can increase resistance
RT to methylglyoxal toxicity.";
RL FEMS Microbiol. Lett. 218:93-99(2003).
RN [4]
RP FUNCTION IN THE METHYLGLYOXAL DETOXIFICATION AND DISRUPTION PHENOTYPE, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16077126; DOI=10.1128/jb.187.16.5782-5789.2005;
RA Ko J., Kim I., Yoo S., Min B., Kim K., Park C.;
RT "Conversion of methylglyoxal to acetol by Escherichia coli aldo-keto
RT reductases.";
RL J. Bacteriol. 187:5782-5789(2005).
RN [5]
RP FUNCTION AS A GLYCERALDEHYDE 3-PHOSPHATE REDUCTASE.
RX PubMed=18620424; DOI=10.1021/bi801054v;
RA Desai K.K., Miller B.G.;
RT "A metabolic bypass of the triosephosphate isomerase reaction.";
RL Biochemistry 47:7983-7985(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND SUBUNIT.
RX PubMed=22393408; DOI=10.1371/journal.pone.0032498;
RA Totir M., Echols N., Nanao M., Gee C.L., Moskaleva A., Gradia S.,
RA Iavarone A.T., Berger J.M., May A.P., Zubieta C., Alber T.;
RT "Macro-to-micro structural proteomics: native source proteins for high-
RT throughput crystallization.";
RL PLoS ONE 7:E32498-E32498(2012).
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.
CC {ECO:0000269|PubMed:12583903, ECO:0000269|PubMed:16077126,
CC ECO:0000269|PubMed:18620424}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.06 mM for 4-nitrobenzaldehyde (at pH 7 and at 25 degrees
CC Celsius) {ECO:0000269|PubMed:16077126};
CC KM=3.4 mM for methylglyoxal (at pH 7 and at 25 degrees Celsius)
CC {ECO:0000269|PubMed:16077126};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:22393408}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show 23% decrease in the
CC amount of acetol.
CC -!- SIMILARITY: Belongs to the shaker potassium channel beta subunit
CC family. {ECO:0000305}.
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DR EMBL; U28377; AAA69168.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76037.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77060.1; -; Genomic_DNA.
DR PIR; G65086; G65086.
DR RefSeq; NP_417474.1; NC_000913.3.
DR RefSeq; WP_000262172.1; NZ_SSZK01000023.1.
DR PDB; 3N6Q; X-ray; 1.80 A; A/B/C/D/E/F/G/H=1-346.
DR PDB; 4AST; X-ray; 2.38 A; A/B/C/D/E/F/G/H=1-346.
DR PDB; 4AUB; X-ray; 2.05 A; A/B/C/D/E/F/G/H=1-346.
DR PDBsum; 3N6Q; -.
DR PDBsum; 4AST; -.
DR PDBsum; 4AUB; -.
DR AlphaFoldDB; Q46851; -.
DR SMR; Q46851; -.
DR BioGRID; 4261416; 10.
DR BioGRID; 851798; 2.
DR DIP; DIP-36026N; -.
DR IntAct; Q46851; 6.
DR STRING; 511145.b3001; -.
DR jPOST; Q46851; -.
DR PaxDb; Q46851; -.
DR PRIDE; Q46851; -.
DR EnsemblBacteria; AAC76037; AAC76037; b3001.
DR EnsemblBacteria; BAE77060; BAE77060; BAE77060.
DR GeneID; 947480; -.
DR KEGG; ecj:JW2970; -.
DR KEGG; eco:b3001; -.
DR PATRIC; fig|1411691.4.peg.3727; -.
DR EchoBASE; EB2831; -.
DR eggNOG; COG0667; Bacteria.
DR HOGENOM; CLU_023205_2_0_6; -.
DR InParanoid; Q46851; -.
DR OMA; YSMINRW; -.
DR PhylomeDB; Q46851; -.
DR BioCyc; EcoCyc:G7558-MON; -.
DR BioCyc; MetaCyc:G7558-MON; -.
DR SABIO-RK; Q46851; -.
DR PRO; PR:Q46851; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0051596; P:methylglyoxal catabolic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase; Reference proteome.
FT CHAIN 1..346
FT /note="L-glyceraldehyde 3-phosphate reductase"
FT /id="PRO_0000201331"
FT SITE 61
FT /note="Important for catalysis"
FT SITE 66
FT /note="Important for catalysis"
FT SITE 97
FT /note="Important for catalysis"
FT SITE 138
FT /note="Important for catalysis"
FT TURN 7..10
FT /evidence="ECO:0007829|PDB:3N6Q"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:3N6Q"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:3N6Q"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:3N6Q"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:3N6Q"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3N6Q"
FT TURN 67..71
FT /evidence="ECO:0007829|PDB:3N6Q"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:3N6Q"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:3N6Q"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3N6Q"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:3N6Q"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3N6Q"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:3N6Q"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:3N6Q"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:3N6Q"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:3N6Q"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:3N6Q"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:3N6Q"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:3N6Q"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:3N6Q"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:3N6Q"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:3N6Q"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:3N6Q"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:3N6Q"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:4AUB"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:4AUB"
FT HELIX 261..276
FT /evidence="ECO:0007829|PDB:3N6Q"
FT HELIX 281..289
FT /evidence="ECO:0007829|PDB:3N6Q"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:3N6Q"
FT HELIX 305..312
FT /evidence="ECO:0007829|PDB:3N6Q"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:3N6Q"
FT HELIX 322..334
FT /evidence="ECO:0007829|PDB:3N6Q"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:4AUB"
SQ SEQUENCE 346 AA; 38832 MW; C70D4D43A3A57AFC CRC64;
MVWLANPERY GQMQYRYCGK SGLRLPALSL GLWHNFGHVN ALESQRAILR KAFDLGITHF
DLANNYGPPP GSAEENFGRL LREDFAAYRD ELIISTKAGY DMWPGPYGSG GSRKYLLASL
DQSLKRMGLE YVDIFYSHRV DENTPMEETA SALAHAVQSG KALYVGISSY SPERTQKMVE
LLREWKIPLL IHQPSYNLLN RWVDKSGLLD TLQNNGVGCI AFTPLAQGLL TGKYLNGIPQ
DSRMHREGNK VRGLTPKMLT EANLNSLRLL NEMAQQRGQS MAQMALSWLL KDDRVTSVLI
GASRAEQLEE NVQALNNLTF STKELAQIDQ HIADGELNLW QASSDK
