ID   GHRA_ECOSM              Reviewed;         312 AA.
AC   B1LIY1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   16-JUN-2009, entry version 10.
DE   RecName: Full=Glyoxylate/hydroxypyruvate reductase A;
DE            EC=1.1.1.79;
DE            EC=1.1.1.81;
DE   AltName: Full=2-ketoacid reductase;
GN   Name=ghrA; OrderedLocusNames=EcSMS35_2100;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18708504; DOI=10.1128/JB.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia
RT   coli SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate
CC       and hydroxypyruvate into glycolate and glycerate, respectively (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Glycolate + NADP(+) = glyoxylate + NADPH.
CC   -!- CATALYTIC ACTIVITY: D-glycerate + NAD(P)(+) = hydroxypyruvate +
CC       NAD(P)H.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. GhrA subfamily.
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DR   EMBL; CP000970; ACB18295.1; -; Genomic_DNA.
DR   RefSeq; YP_001744152.1; -.
DR   GeneID; 6146252; -.
DR   GenomeReviews; CP000970_GR; EcSMS35_2100.
DR   KEGG; ecm:EcSMS35_2100; -.
DR   OMA; B1LIY1; YALVWRA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:HAMAP.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0030267; F:glyoxylate reductase (NADP) activity; IEA:HAMAP.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01666; -; 1.
DR   InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; FALSE_NEG.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; FALSE_NEG.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase.
FT   CHAIN         1    312       Glyoxylate/hydroxypyruvate reductase A.
FT                                /FTId=PRO_0000348361.
FT   ACT_SITE    227    227       By similarity.
FT   ACT_SITE    275    275       Proton donor (By similarity).
SQ   SEQUENCE   312 AA;  35328 MW;  31302F9C69DBED08 CRC64;
     MDIIFYHPTF DTQWWIEALR KAIPQARVRA WKSGDNVSAD YALVWHPPVE MLAGRDLKAV
     FALGAGVDSI LSKLQAHPEM LKPSVPLFRL EDTGMGEQMQ EYAVSQVLHW FRRFDDYRIQ
     QNSSHWQPLP EYHREDFTIG ILGAGVLGSK VAQSLQTWRF PLRCWSRTRK SWPGVQSFAG
     REELSAFLSQ CRVLINLLPN TPETVGIINQ QLLEKLPDGA YLLNLARGVH VVEDDLLAAL
     DSGKVKGAML DVFNREPLPP ESPLWQHPRV TITPHVAAIT RPAEAVDYIS RTIAQLEKGE
     RVCGQVDRAR GY
//