GHRB_YERPY
ID GHRB_YERPY Reviewed; 326 AA.
AC B1JH01;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=YPK_0017;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000950; ACA66331.1; -; Genomic_DNA.
DR RefSeq; WP_012303319.1; NZ_CP009792.1.
DR AlphaFoldDB; B1JH01; -.
DR SMR; B1JH01; -.
DR EnsemblBacteria; ACA66331; ACA66331; YPK_0017.
DR KEGG; ypy:YPK_0017; -.
DR PATRIC; fig|502800.11.peg.619; -.
DR OMA; KMKPNCI; -.
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; IPR029752; D-isomer_DH_CS1.
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; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; NADP; Oxidoreductase.
FT CHAIN 1..326
FT /note="Glyoxylate/hydroxypyruvate reductase B"
FT /id="PRO_0000348414"
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 326 AA; 35447 MW; C70A000E4E8FCC4E CRC64;
MKPSIVLYKS IPTDLHQRLA QHFTVNSFDG LTPDNQPELL AALQQAEGLI GSGGKIDQDF
LQLAPNLRAA STISVGYDNF DVEALSQRGI ALMHTPTVLT ETVADTMMAL MLSTARRVVE
LAERVKAGEW QESIGDDWFG VDVHHKTIGI LGMGRIGMAL AQRAHFGFSM PVLYTSRRPH
EAAEQRFGAR HCSLDTLLAE ADFLCITLPM TEQTYHMIGR EQLAKIKSSA ILINAGRGPV
VDEQALIAAL QDGTIHAAGL DVFEQEPLPV DSPLLTLRNV VAVPHIGSAT HETRYNMAAC
AVDNLINALT GTVKENCVNP QVLITH