GenomeNet

Database: UniProt
Entry: A8G7S7
LinkDB: A8G7S7
Original site: A8G7S7 
ID   GHRB_SERP5              Reviewed;         325 AA.
AC   A8G7S7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   16-JAN-2019, 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};
GN   OrderedLocusNames=Spro_0057;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Taghavi S., Newman L., Vangronsveld J., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000826; ABV39167.1; -; Genomic_DNA.
DR   RefSeq; WP_012004530.1; NC_009832.1.
DR   ProteinModelPortal; A8G7S7; -.
DR   SMR; A8G7S7; -.
DR   STRING; 399741.Spro_0057; -.
DR   EnsemblBacteria; ABV39167; ABV39167; Spro_0057.
DR   KEGG; spe:Spro_0057; -.
DR   eggNOG; ENOG4105C5I; Bacteria.
DR   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136700; -.
DR   KO; K00090; -.
DR   OMA; WDVHGKT; -.
DR   OrthoDB; 1638924at2; -.
DR   Proteomes; UP000007074; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase.
FT   CHAIN         1    325       Glyoxylate/hydroxypyruvate reductase B.
FT                                /FTId=PRO_0000348398.
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   325 AA;  35463 MW;  65AC6FF0BC3502DC CRC64;
     MKPSIVLYKN IPADLRERLE QHFTVHAFDG LTPDNHDELR QALQQAEGII GSGGKIDEAF
     LQQTPKLRAA STISVGYDNF DVDALNAHNV LLMHTPTVLT ETVADTIMSL VLATARRVVE
     VAERVKAGEW QGSIGADWFG VDVHHKTIGI LGMGRIGLAL AQRAHFGFGM PVLYNARRTH
     EEAEQRFNAR RCDLDTLLAE SDFICITLPL TDETFHMISR DQLAKMKKSG ILINAGRGPV
     VDEAALIEAL QNGTIHAAGL DVFEKEPLPV SSPLLTLPNV VALPHIGSAT HETRYGMAEC
     AVDNLIAALT GTVKENCVNP QLLKK
//
DBGET integrated database retrieval system