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Database: UniProt
Entry: A9MH27
LinkDB: A9MH27
Original site: A9MH27 
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   13-FEB-2019, entry version 66.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   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.,
RA   Nash W., 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
CC       and 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;
CC         EC=1.1.1.79; 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;
CC         EC=1.1.1.81; Evidence={ECO:0000255|HAMAP-Rule:MF_01666};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) +
CC         NADPH; Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16659, ChEBI:CHEBI:17180, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.81; Evidence={ECO:0000255|HAMAP-
CC         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}.
DR   EMBL; CP000880; ABX21747.1; -; Genomic_DNA.
DR   RefSeq; WP_000402558.1; NC_010067.1.
DR   ProteinModelPortal; A9MH27; -.
DR   SMR; A9MH27; -.
DR   STRING; 882884.SARI_01863; -.
DR   EnsemblBacteria; ABX21747; ABX21747; SARI_01863.
DR   KEGG; ses:SARI_01863; -.
DR   eggNOG; ENOG4105JPG; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000136694; -.
DR   KO; K12972; -.
DR   OMA; VQMAEYV; -.
DR   OrthoDB; 1435073at2; -.
DR   BioCyc; SENT882884:G1GAH-1817-MONOMER; -.
DR   Proteomes; UP000002084; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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.
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   Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    312       Glyoxylate/hydroxypyruvate reductase A.
FT                                /FTId=PRO_0000348367.
FT   ACT_SITE    227    227       {ECO:0000255|HAMAP-Rule:MF_01666}.
FT   ACT_SITE    275    275       Proton donor. {ECO:0000255|HAMAP-
FT                                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
//
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