GenomeNet

Database: UniProt
Entry: Q8X9K1
LinkDB: Q8X9K1
Original site: Q8X9K1 
ID   GHRA_ECO57              Reviewed;         312 AA.
AC   Q8X9K1; Q7AFB5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   05-DEC-2018, entry version 106.
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=Z1666, ECs1410;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG55779.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB34833.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE005174; AAG55779.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB34833.1; ALT_INIT; Genomic_DNA.
DR   PIR; B90805; B90805.
DR   PIR; G85664; G85664.
DR   RefSeq; NP_309437.1; NC_002695.1.
DR   RefSeq; WP_000351284.1; NZ_NOKN01000002.1.
DR   ProteinModelPortal; Q8X9K1; -.
DR   SMR; Q8X9K1; -.
DR   STRING; 155864.Z1666; -.
DR   EnsemblBacteria; AAG55779; AAG55779; Z1666.
DR   EnsemblBacteria; BAB34833; BAB34833; BAB34833.
DR   GeneID; 914357; -.
DR   KEGG; ece:Z1666; -.
DR   KEGG; ecs:ECs1410; -.
DR   PATRIC; fig|386585.9.peg.1509; -.
DR   eggNOG; ENOG4105JPG; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000136694; -.
DR   KO; K12972; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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_0000348354.
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;  35359 MW;  095F3989AA589A05 CRC64;
     MDIIFYHPTF DTQWWIEALR KAIPQARVRA WKSGDNDSAD YALAWHPPVE MLAGRDLKAV
     FALGAGVDSI LSKLQAHPEM LKPSVPLFRL EDTGMGEQMQ EYAVSQVLHW FRRFDDYRIQ
     QNSSHWQPLP EYHREDFTIG ILGAGVLGSK VAQSLQTWRF PLRCWSRTRK SWPGVQSFAG
     WEELSAFLSQ CRVLINLLPN TPETVGIINQ QLLEKLPDGA YLLNLARGVH VVEDDLLAAL
     DSGKVKGAML DVFNREPLPP ESPLWQHPRV TITPHVAAIT RPAEAVEYIS RTIAQLEKGE
     RVCGQVDRAR GY
//
DBGET integrated database retrieval system