GHRB_ENT38
ID GHRB_ENT38 Reviewed; 324 AA.
AC A4W577;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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}; OrderedLocusNames=Ent638_0167;
OS Enterobacter sp. (strain 638).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA Vangronsveld J., Newman L., Monchy S.;
RT "Genome sequence of the plant growth promoting endophytic bacterium
RT Enterobacter sp. 638.";
RL PLoS Genet. 6:E1000943-E1000943(2010).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate and
CC 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; EC=1.1.1.79;
CC 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; EC=1.1.1.81;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01667};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) + NADPH;
CC Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:17180, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.81;
CC Evidence={ECO:0000255|HAMAP-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}.
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DR EMBL; CP000653; ABP58857.1; -; Genomic_DNA.
DR RefSeq; WP_011915432.1; NC_009436.1.
DR AlphaFoldDB; A4W577; -.
DR SMR; A4W577; -.
DR STRING; 399742.Ent638_0167; -.
DR PRIDE; A4W577; -.
DR EnsemblBacteria; ABP58857; ABP58857; Ent638_0167.
DR KEGG; ent:Ent638_0167; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_6; -.
DR OMA; KMKPNCI; -.
DR OrthoDB; 1638924at2; -.
DR Proteomes; UP000000230; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:RHEA.
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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; NADP; Oxidoreductase.
FT CHAIN 1..324
FT /note="Glyoxylate/hydroxypyruvate reductase B"
FT /id="PRO_0000348381"
FT ACT_SITE 237
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01667"
FT ACT_SITE 266
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01667"
FT ACT_SITE 285
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01667"
SQ SEQUENCE 324 AA; 35661 MW; 1323B43A8356FC68 CRC64;
MKPSVILYKT LPDDLQKRLE EHFTVTQMKN LNPETVAEHA DAFASAAGLL GSSEKVDTAL
LEKMPKLRAT STISVGYDNF DVDALNTRKI LLMHTPYALT ETVADTLMAL VLSTARRVVE
VAERVKAGEW TKSIGPDWFG VDVHGKTLGI VGMGRIGLAL AQRAHFGFNM PILYNARRHH
SEAEERFEAR YCELETLLQE ADYVCLILPL TDETHHLIGK AEFEKMKKSA IFINAGRGPV
VDEKALIEAL QKGEIHAAGL DVFEQEPLPV DSPLLTMSNV VSLPHIGSAT HETRYNMAAT
AVDNLINALN GNVEKNCVNP HVNA