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Database: UniProt
Entry: Q5JEZ2
LinkDB: Q5JEZ2
Original site: Q5JEZ2 
ID   GYAR_THEKO              Reviewed;         333 AA.
AC   Q5JEZ2;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   16-JAN-2019, entry version 95.
DE   RecName: Full=Glyoxylate reductase {ECO:0000255|HAMAP-Rule:MF_00776};
DE            EC=1.1.1.26 {ECO:0000255|HAMAP-Rule:MF_00776};
GN   Name=gyaR {ECO:0000255|HAMAP-Rule:MF_00776}; OrderedLocusNames=TK0683;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon
RT   Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus
RT   genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycolate + NAD(+) = glyoxylate + H(+) + NADH;
CC         Xref=Rhea:RHEA:18229, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC         ChEBI:CHEBI:36655, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.26; Evidence={ECO:0000255|HAMAP-Rule:MF_00776};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00776}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00776}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. GyaR subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00776}.
DR   EMBL; AP006878; BAD84872.1; -; Genomic_DNA.
DR   RefSeq; WP_011249634.1; NC_006624.1.
DR   ProteinModelPortal; Q5JEZ2; -.
DR   SMR; Q5JEZ2; -.
DR   STRING; 69014.TK0683; -.
DR   PRIDE; Q5JEZ2; -.
DR   EnsemblBacteria; BAD84872; BAD84872; TK0683.
DR   GeneID; 3234458; -.
DR   KEGG; tko:TK0683; -.
DR   PATRIC; fig|69014.16.peg.664; -.
DR   eggNOG; arCOG01755; Archaea.
DR   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136700; -.
DR   InParanoid; Q5JEZ2; -.
DR   KO; K00015; -.
DR   OMA; KWIAHNG; -.
DR   OrthoDB; 36410at2157; -.
DR   BioCyc; TKOD69014:G1G2A-679-MONOMER; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0030267; F:glyoxylate reductase (NADP) activity; IBA:GO_Central.
DR   GO; GO:0047964; F:glyoxylate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   HAMAP; MF_00776; GyaR; 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; IPR023519; Glyoxylate_reductase_GyaR.
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   Complete proteome; Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1    333       Glyoxylate reductase.
FT                                /FTId=PRO_0000075950.
FT   NP_BIND     158    161       NADP. {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   NP_BIND     180    182       NADP. {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   NP_BIND     239    241       NADP. {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   NP_BIND     288    290       NADP. {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   ACT_SITE    241    241       {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   ACT_SITE    270    270       {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   ACT_SITE    288    288       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00776}.
SQ   SEQUENCE   333 AA;  37931 MW;  5D836274189CC8D2 CRC64;
     MRPKVFITRA IPENGIEMLK EHFEVEVWPE EREIPREVLL KKVRDVDALV TMLSERIDSE
     VFDAAPRLRI VANYAVGYDN IDVEEATRRG IYVTNTPDVL TDATADFAWT LLLATARRLI
     EADHFTRSGE WKRRGIAWHP RWFLGYDVYG KTIGIVGFGR IGQAVARRAR GFGMRILYYS
     RSRKPEAEKE LGAEFRSLED LLRESDFVVL AVPLTKETQY MINEERLRLM KKTAILVNIA
     RGKVVDTKAL MKALKEGWIA GAGLDVYEEE PYYNEELFSL KNVVLAPHIG SATYGAREGM
     AELVARNLIA FKNGEVPPTL VNKEVVKVRK PGF
//
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