GHRB_SALPC
ID GHRB_SALPC Reviewed; 324 AA.
AC C0Q1A7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=SPC_3725;
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594;
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
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; CP000857; ACN47803.1; -; Genomic_DNA.
DR RefSeq; WP_000804686.1; NC_012125.1.
DR AlphaFoldDB; C0Q1A7; -.
DR SMR; C0Q1A7; -.
DR PRIDE; C0Q1A7; -.
DR EnsemblBacteria; ACN47803; ACN47803; SPC_3725.
DR KEGG; sei:SPC_3725; -.
DR HOGENOM; CLU_019796_1_2_6; -.
DR OMA; KMKPNCI; -.
DR Proteomes; UP000001599; 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; PS00670; D_2_HYDROXYACID_DH_2; 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_1000187300"
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; 35313 MW; D0E0B79E9A49E0D9 CRC64;
MKPSIILYKT LPDDLLHRLE AHFTVTQVPN LHPETVARHA QAFASAQGLL GASETVNRAL
LEKMPALRAA STISVGYDNV EVDALTARKI VLMHTPTVLT ETVADTVMAL MLATARRVVD
VAERVKAGEW TESIGPAWFG VDVHHKTLGI VGMGRIGMAL AQRAHFGFTM PVLYHARRRH
QEAEDRFNAR YCDLDTLLQE ADFVCVILPL TAETRHLFGA TQFARMKSSA IFINAGRGPV
VDENALIAAL QNGEIYAAGL DVFEQEPLSV DSPLLNMSNV VAVPHIGSAT HETRYNMMAC
AVDNLIDALQ GKIEKNCVNP QAAG