ID   GHRA_SALAR              Reviewed;         312 AA.
AC   A9MH27;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   28-JAN-2026, entry version 91.
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=SARI_01863;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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 + NADPH + H(+);
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 + NADH + H(+);
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 + NADPH + H(+);
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; CP000880; ABX21747.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9MH27; -.
DR   SMR; A9MH27; -.
DR   STRING; 41514.SARI_01863; -.
DR   KEGG; ses:SARI_01863; -.
DR   HOGENOM; CLU_019796_1_0_6; -.
DR   Proteomes; UP000002084; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA.
DR   GO; GO:0030267; F:glyoxylate reductase (NADPH) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008465; F:hydroxypyruvate reductase (NADH) activity; IEA:RHEA.
DR   GO; GO:0120509; F:hydroxypyruvate reductase (NADPH) activity; IEA:RHEA.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   CDD; cd12164; GDH_like_2; 1.
DR   FunFam; 3.40.50.720:FF:000110; Glyoxylate/hydroxypyruvate reductase A; 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   NCBIfam; NF012013; PRK15469.1; 1.
DR   PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43333:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE NAD-BINDING 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_0000348367"
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;  35130 MW;  D960AB6E2EBAF63C CRC64;
     MEIIFYHPTF NAAWWVNALE KALPHVRVRE WKAGDNSPAD YALVWQPPVE MLAGRRLKAV
     FALGAGVDSI LSELNTHPEM LDASIPLFRL EDTGMGLQMQ EYAVSQVLHW FRRFDDYQAL
     KNQAIWKPLP EYTREEFSVG IMGAGILGSK VAESLQAWGF PLRCWSRSRK SWPGVESYAG
     REELDAFLNQ TRVLINLLPN TAQTVGIINR ELLNKLPDSA YVLNLARGVH VNEADLLAAL
     ESGKLKGAML DVFSQEPLPQ ESPLWRHSRV AMTPHIAAVT RPAEAIEYIS RTINQLERGE
     PVTGQVDRAR GY
//