GHRA_ECO5E
ID GHRA_ECO5E Reviewed; 312 AA.
AC B5YVQ3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
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};
GN OrderedLocusNames=ECH74115_1411;
OS Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=444450;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC4115 / EHEC;
RX PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
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; CP001164; ACI38598.1; -; Genomic_DNA.
DR RefSeq; WP_000351284.1; NC_011353.1.
DR AlphaFoldDB; B5YVQ3; -.
DR SMR; B5YVQ3; -.
DR KEGG; ecf:ECH74115_1411; -.
DR HOGENOM; CLU_019796_1_0_6; -.
DR OMA; VQMAEYV; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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 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 Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; NADP; Oxidoreductase.
FT CHAIN 1..312
FT /note="Glyoxylate/hydroxypyruvate reductase A"
FT /id="PRO_1000187265"
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; 35359 MW; 095F3989AA589A05 CRC64;
MDIIFYHPTF DTQWWIEALR KAIPQARVRA WKSGDNDSAD YALAWHPPVE MLAGRDLKAV
FALGAGVDSI LSKLQAHPEM LKPSVPLFRL EDTGMGEQMQ EYAVSQVLHW FRRFDDYRIQ
QNSSHWQPLP EYHREDFTIG ILGAGVLGSK VAQSLQTWRF PLRCWSRTRK SWPGVQSFAG
WEELSAFLSQ CRVLINLLPN TPETVGIINQ QLLEKLPDGA YLLNLARGVH VVEDDLLAAL
DSGKVKGAML DVFNREPLPP ESPLWQHPRV TITPHVAAIT RPAEAVEYIS RTIAQLEKGE
RVCGQVDRAR GY
