GenomeNet

Database: UniProt
Entry: B5XMZ4
LinkDB: B5XMZ4
Original site: B5XMZ4 
ID   GHRB_KLEP3              Reviewed;         323 AA.
AC   B5XMZ4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   16-JAN-2019, entry version 63.
DE   RecName: Full=Glyoxylate/hydroxypyruvate reductase B {ECO:0000255|HAMAP-Rule:MF_01667};
DE            EC=1.1.1.79 {ECO:0000255|HAMAP-Rule:MF_01667};
DE            EC=1.1.1.81 {ECO:0000255|HAMAP-Rule:MF_01667};
GN   Name=ghrB {ECO:0000255|HAMAP-Rule:MF_01667};
GN   OrderedLocusNames=KPK_0190;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J.,
RA   Mohamoud Y., Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C.,
RA   Triplett E.W., Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in
RT   mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate
CC       and hydroxypyruvate into glycolate and glycerate, respectively.
CC       {ECO:0000255|HAMAP-Rule:MF_01667}.
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_01667};
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_01667};
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_01667};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01667}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01667}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. GhrB subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01667}.
DR   EMBL; CP000964; ACI11687.1; -; Genomic_DNA.
DR   RefSeq; WP_012540338.1; NC_011283.1.
DR   ProteinModelPortal; B5XMZ4; -.
DR   SMR; B5XMZ4; -.
DR   PRIDE; B5XMZ4; -.
DR   EnsemblBacteria; ACI11687; ACI11687; KPK_0190.
DR   KEGG; kpe:KPK_0190; -.
DR   HOGENOM; HOG000136700; -.
DR   KO; K00090; -.
DR   OMA; KWIAHNG; -.
DR   OrthoDB; 1638924at2; -.
DR   Proteomes; UP000001734; 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_01667; 2_Hacid_dh_C_GhrB; 1.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR023756; Glyo/OHPyrv_Rdtase_B.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase.
FT   CHAIN         1    323       Glyoxylate/hydroxypyruvate reductase B.
FT                                /FTId=PRO_1000187293.
FT   ACT_SITE    237    237       {ECO:0000255|HAMAP-Rule:MF_01667}.
FT   ACT_SITE    266    266       {ECO:0000255|HAMAP-Rule:MF_01667}.
FT   ACT_SITE    285    285       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01667}.
SQ   SEQUENCE   323 AA;  35390 MW;  1B2F49FB5041EFBA CRC64;
     MKPSVILYKT LPDDLLQRLE EHFSVTQVKN LRPETVSQHA EAFAQAEGLL GSSEKVDAAL
     LEKMPKLRAT STVSVGYDNF DVEALNARRV LLMHTPTVLT ETVADTVMAL VLSTARRVVE
     VAERVKAGEW TKSIGPDWFG SDVHHKTLGI VGMGRIGMAL AQRAHFGFGM PILYNARRQH
     PQAEERFNAR YCDLDTLLQE ADFVCLILPL SEETHHLFGQ AQFAKMKSSA IFINAGRGPV
     VDEQALIAAL QAGEIHAAGL DVFEHEPLAK DSPLLTLPNV VALPHIGSAT HETRYNMAAC
     AVDNLIDALN GNVEKNCVNP QVK
//
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