GenomeNet

Database: UniProt
Entry: Q8Z7M6
LinkDB: Q8Z7M6
Original site: Q8Z7M6 
ID   GHRA_SALTI              Reviewed;         312 AA.
AC   Q8Z7M6; Q7C9A3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   13-FEB-2019, entry version 105.
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=STY1172, t1785;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P.,
RA   Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J.,
RA   Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K.,
RA   Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C.,
RA   Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K.,
RA   Whitehead S., Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella
RT   enterica serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/JB.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J.,
RA   Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2
RT   and CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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; AE014613; AAO69408.1; -; Genomic_DNA.
DR   EMBL; AL513382; CAD08259.1; -; Genomic_DNA.
DR   RefSeq; NP_455629.1; NC_003198.1.
DR   RefSeq; WP_000402555.1; NZ_UFRG01000003.1.
DR   ProteinModelPortal; Q8Z7M6; -.
DR   SMR; Q8Z7M6; -.
DR   STRING; 220341.STY1172; -.
DR   EnsemblBacteria; AAO69408; AAO69408; t1785.
DR   EnsemblBacteria; CAD08259; CAD08259; CAD08259.
DR   GeneID; 1247578; -.
DR   KEGG; stt:t1785; -.
DR   KEGG; sty:STY1172; -.
DR   PATRIC; fig|220341.7.peg.1172; -.
DR   eggNOG; ENOG4105JPG; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000136694; -.
DR   KO; K12972; -.
DR   BioCyc; GCF_001048035:AC754_RS15335-MONOMER; -.
DR   BioCyc; GCF_001048375:AC768_RS10430-MONOMER; -.
DR   BioCyc; GCF_001079465:ADV44_RS13105-MONOMER; -.
DR   BioCyc; GCF_001088345:AEZ18_RS11800-MONOMER; -.
DR   BioCyc; GCF_001095585:AD238_RS10790-MONOMER; -.
DR   BioCyc; GCF_001104165:AE704_RS10430-MONOMER; -.
DR   BioCyc; GCF_001104885:AEZ38_RS11145-MONOMER; -.
DR   BioCyc; GCF_001106745:AE121_RS13120-MONOMER; -.
DR   BioCyc; GCF_001118185:AE086_RS14250-MONOMER; -.
DR   BioCyc; GCF_001119245:AE140_RS14180-MONOMER; -.
DR   BioCyc; GCF_001121865:AE338_RS11380-MONOMER; -.
DR   BioCyc; GCF_001127485:AE735_RS14420-MONOMER; -.
DR   BioCyc; GCF_001135805:AEG73_RS10640-MONOMER; -.
DR   BioCyc; GCF_001148125:AEN24_RS11390-MONOMER; -.
DR   BioCyc; GCF_001148305:AEN67_RS15945-MONOMER; -.
DR   BioCyc; GCF_001157245:AER93_RS10650-MONOMER; -.
DR   BioCyc; GCF_001163025:AFA50_RS10435-MONOMER; -.
DR   BioCyc; GCF_001165785:AFA97_RS14250-MONOMER; -.
DR   BioCyc; GCF_001240865:ALC23_RS11685-MONOMER; -.
DR   BioCyc; GCF_001356455:AQJ76_RS10415-MONOMER; -.
DR   BioCyc; GCF_001357935:AQL34_RS02410-MONOMER; -.
DR   BioCyc; GCF_001359015:AQL50_RS02410-MONOMER; -.
DR   BioCyc; GCF_001360555:AQK88_RS10420-MONOMER; -.
DR   BioCyc; GCF_001361075:AQM75_RS13850-MONOMER; -.
DR   BioCyc; GCF_001362095:AQO19_RS14610-MONOMER; -.
DR   BioCyc; GCF_001362135:AQN73_RS12005-MONOMER; -.
DR   BioCyc; GCF_001362175:AQN68_RS10415-MONOMER; -.
DR   BioCyc; GCF_001362195:AQN87_RS23165-MONOMER; -.
DR   BioCyc; GCF_001362335:AQN99_RS15925-MONOMER; -.
DR   BioCyc; GCF_001364695:AQQ97_RS03020-MONOMER; -.
DR   BioCyc; GCF_900185485:CDZ80_RS13500-MONOMER; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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_0000348371.
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;  34988 MW;  5CCF91E2D1BEF90D CRC64;
     MEIIFYHPTF NAAWWVNALE KALPHARVRE WKVGDNNPAD YALVWQPPVE MLAGRRLKAV
     FVLGAGVDAI LSKLNAHPEM LDASIPLFRL EDTGMGLQMQ EYAASQVLHW FRRFDDYQAL
     KNQALWKPLP EYTREEFSVG IIGAGVLGAK VAESLQAWGF PLRCWSRSRK SWPGVESYVG
     REELRAFLNQ TRVLINLLPN TAQTVGIINS ELLDQLPDGA YVLNLARGVH VQEADLLAAL
     DSGKLKGAML DVFSQEPLPQ ESPLWRHPRV AMTPHIAAVT RPAEAIDYIS RTITQLEKGE
     PVTGQVDRAR GY
//
DBGET integrated database retrieval system