ID   GHRA_SERP5              Reviewed;         313 AA.
AC   A8GD46;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=Spro_1933;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-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 + 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; CP000826; ABV41036.1; -; Genomic_DNA.
DR   RefSeq; WP_012006357.1; NC_009832.1.
DR   AlphaFoldDB; A8GD46; -.
DR   SMR; A8GD46; -.
DR   STRING; 399741.Spro_1933; -.
DR   EnsemblBacteria; ABV41036; ABV41036; Spro_1933.
DR   KEGG; spe:Spro_1933; -.
DR   eggNOG; COG0111; Bacteria.
DR   HOGENOM; CLU_019796_1_0_6; -.
DR   OMA; VQMAEYV; -.
DR   OrthoDB; 1435073at2; -.
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..313
FT                   /note="Glyoxylate/hydroxypyruvate reductase A"
FT                   /id="PRO_0000348373"
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;  34642 MW;  EDEDACA97CA14D1C CRC64;
     MNIIFYHPFF NAEEWLAGLS QRLPQAQVRA WQPGDDRPAD YALVWRPPHE MLANRGRLKG
     VFALGAGVDA ILEQERAYPG TLPAGVPLLR LEDTGMAQQM QEYALSYVLR YFRRFDEYQL
     LQQQQEWRPL DPHQQDNFTI GILGAGVLGK SVAQKLTAFG FNVRCWSRSP KQIDGVQSFA
     GAEQRAAFLD GVQLLINLLP NTPETAGILN QQLFAHLAPG AYLINLARGA HLVEDDLLQA
     LEQGQLAAAT LDVFVTEPLP QAHPFWRHPR VTITPHIAAI TLPQAAMDQI AANILALEAG
     QTPAGVVDVL LGY