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GHRB_YERPE
ID   GHRB_YERPE              Reviewed;         326 AA.
AC   Q0W9V5; Q74PC9; Q8CZG7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 109.
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=YPO4078, y4096, YP_3988;
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM87639.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAS64128.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL590842; CAL22649.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM87639.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE017042; AAS64128.1; ALT_INIT; Genomic_DNA.
DR   PIR; AF0495; AF0495.
DR   RefSeq; WP_002209630.1; NZ_VWRZ01000093.1.
DR   RefSeq; YP_002348933.1; NC_003143.1.
DR   AlphaFoldDB; Q0W9V5; -.
DR   SMR; Q0W9V5; -.
DR   STRING; 214092.YPO4078; -.
DR   PaxDb; Q0W9V5; -.
DR   EnsemblBacteria; AAM87639; AAM87639; y4096.
DR   EnsemblBacteria; AAS64128; AAS64128; YP_3988.
DR   GeneID; 66843671; -.
DR   KEGG; ype:YPO4078; -.
DR   KEGG; ypk:y4096; -.
DR   KEGG; ypm:YP_3988; -.
DR   PATRIC; fig|214092.21.peg.4620; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_2_6; -.
DR   OMA; KMKPNCI; -.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central.
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; 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.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..326
FT                   /note="Glyoxylate/hydroxypyruvate reductase B"
FT                   /id="PRO_0000348406"
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;  35465 MW;  935B405A48250AE2 CRC64;
     MKPSIVLYKS IPTDLHQRLA QHFTVNSFDG LTPDNQPELL AALQQAEGLI GSGGKIDQDF
     LQLAPNLRAA STISVGYDNF DVEALSQRGI ALMHTPTVLT ETVADTMMAL MLSTARRVVE
     LAERVKAGEW QESIGDDWFG VDVHHKTIGI LGMGRIGMAL AQRAHFGFSM PVLYTSRRPH
     EAAEQRFGAR HCSLDTLLAE ADFLCITLPM TEQTYHMIGR EQLAKMKSSA ILINAGRGPV
     VDEQALIAAL QDGTIHAAGL DVFEQEPLPV DSPLLTLRNV VAVPHIGSAT HETRYNMAAC
     AVDNLINALT GTVKENCVNP QVLITH
 
 
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