GenomeNet

Database: UniProt
Entry: Q5PGZ3
LinkDB: Q5PGZ3
Original site: Q5PGZ3 
ID   GHRA_SALPA              Reviewed;         312 AA.
AC   Q5PGZ3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   05-DEC-2018, 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};
GN   OrderedLocusNames=SPA1716;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P.,
RA   Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M.,
RA   Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G.,
RA   Kohlberg S., Strong C., Du F., Carter J., Kremizki C., Layman D.,
RA   Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P.,
RA   Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L.,
RA   Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV77639.1; -; Genomic_DNA.
DR   RefSeq; WP_000402552.1; NC_006511.1.
DR   ProteinModelPortal; Q5PGZ3; -.
DR   SMR; Q5PGZ3; -.
DR   EnsemblBacteria; AAV77639; AAV77639; SPA1716.
DR   KEGG; spt:SPA1716; -.
DR   HOGENOM; HOG000136694; -.
DR   KO; K12972; -.
DR   OMA; VQMAEYV; -.
DR   BioCyc; SENT295319:G1G44-1809-MONOMER; -.
DR   Proteomes; UP000008185; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase.
FT   CHAIN         1    312       Glyoxylate/hydroxypyruvate reductase A.
FT                                /FTId=PRO_0000348369.
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;  35006 MW;  A46D750625A7A501 CRC64;
     MEIIFYHPTF NAAWWVNALE KALPHARVRE WKVGDNNPAD YALVWQPPVE MLAGRRLKAV
     FALGAGVDAI LSKLNAHPEM LDASIPLFRL EDTGMGLQMQ EYAVSQVLHW FRRFDDYQAL
     KNQALWKPLP EYTREEFSVG IMGAGVLGAK VAESLQAWGF PLRCWSRSRK SWPGVESYVG
     REELRAFLNQ TRVLINLLPN TAQTVGIINS ELLDQLPDGA YVLNLARGVH VQEADLLAAL
     DSGKLKGAML DVFSQEPLPQ ESPLWRHPRV AMTPHIAAVT RPAEAIDYIS RTITQLEKGE
     PVTGQVDRAR GY
//
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