ID   GHRA_YERE8              Reviewed;         313 AA.
AC   A1JRR3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=YE2422;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL12470.1; -; Genomic_DNA.
DR   RefSeq; WP_005161303.1; NC_008800.1.
DR   RefSeq; YP_001006636.1; NC_008800.1.
DR   AlphaFoldDB; A1JRR3; -.
DR   SMR; A1JRR3; -.
DR   STRING; 393305.YE2422; -.
DR   EnsemblBacteria; CAL12470; CAL12470; YE2422.
DR   KEGG; yen:YE2422; -.
DR   PATRIC; fig|393305.7.peg.2574; -.
DR   eggNOG; COG0111; Bacteria.
DR   HOGENOM; CLU_019796_1_0_6; -.
DR   OMA; VQMAEYV; -.
DR   Proteomes; UP000000642; Chromosome.
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; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; NADP; Oxidoreductase.
FT   CHAIN           1..313
FT                   /note="Glyoxylate/hydroxypyruvate reductase A"
FT                   /id="PRO_0000348378"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01666"
FT   ACT_SITE        276
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01666"
SQ   SEQUENCE   313 AA;  34854 MW;  29D79951FB1E61DD CRC64;
     MNIIFYHPFF EAKQWLSGLQ SRLPTANIRQ WRRGDTQPAD YALVWQPPQE MLASRVELKG
     VFALGAGVDA ILDQERRHPG TLPAGVPLVR LEDTGMSLQM QEYVVATVLR YFRRMDEYQL
     QQQQKLWQPL EPHQHDKFTI GILGAGVLGK SVAHKLAEFG FTVRCWSRTP KQIDGVTSFA
     GQEKLPAFIQ GTQLLINLLP HTPQTAGILN QSLFSQLNAN AYIINIARGA HLLERDLLAA
     MNAGQVAAAT LDVFAEEPLP SMHPFWSHPR VTITPHIAAV TLPEVAMDQV VANIQAMEAG
     REPVGLVDVV RGY