ID GHRA_ECOL6 Reviewed; 312 AA.
AC Q8FIT1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Glyoxylate/hydroxypyruvate reductase A {ECO:0000255|HAMAP-Rule:MF_01666};
DE EC=1.1.1.79 {ECO:0000255|HAMAP-Rule:MF_01666};
DE EC=1.1.1.81 {ECO:0000255|HAMAP-Rule:MF_01666};
DE AltName: Full=2-ketoacid reductase {ECO:0000255|HAMAP-Rule:MF_01666};
GN Name=ghrA {ECO:0000255|HAMAP-Rule:MF_01666}; OrderedLocusNames=c1295;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate and
CC hydroxypyruvate into glycolate and glycerate, respectively.
CC {ECO:0000255|HAMAP-Rule:MF_01666}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycolate + NADP(+) = glyoxylate + H(+) + NADPH;
CC Xref=Rhea:RHEA:10992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.79;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01666};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH;
CC Xref=Rhea:RHEA:17905, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:17180, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.81;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01666};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) + NADPH;
CC Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:17180, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.81;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01666};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01666}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. GhrA subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01666}.
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DR EMBL; AE014075; AAN79768.1; -; Genomic_DNA.
DR RefSeq; WP_000351287.1; NZ_CP051263.1.
DR AlphaFoldDB; Q8FIT1; -.
DR SMR; Q8FIT1; -.
DR STRING; 199310.c1295; -.
DR KEGG; ecc:c1295; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_0_6; -.
DR BioCyc; ECOL199310:C1295-MONOMER; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:RHEA.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12164; GDH_like_2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR HAMAP; MF_01666; 2_Hacid_dh_C_GhrA; 1.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR023514; GhrA_Enterobacterales.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..312
FT /note="Glyoxylate/hydroxypyruvate reductase A"
FT /id="PRO_0000348359"
FT ACT_SITE 227
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01666"
FT ACT_SITE 275
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01666"
SQ SEQUENCE 312 AA; 35388 MW; 4298427F9A928A75 CRC64;
MDIIFYHPTF DTQWWIEALR KAIPQARVRA WKSGDNDSAD YALVWHPPVE MLAGRDLKAV
FALGAGVDSI LSKLQAHPEM LKPSVPLFRL EDTGMGEQMQ EYAVSQVLHW FRRFDDYRIQ
QNSSHWQPLP EYHREDFTIG ILGAGVLGSK VAQSLQTWRF PLRCWSRTRK SWPGVQSFAG
REELSAFLSQ CRVLINLLPN TPETVGIINQ QLIEKLPDGA YLLNLARGVH VVEDDLLAAL
DSGKVKGAML DVFNREPLPP ESLLWQHPRV TITPHVAAIT RPAEAVEYIS RTIAQLEKGE
RLCGQVDRAR GY
//
