GYAR_THEKO
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 03-AUG-2022, entry version 108.
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 Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus 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; EC=1.1.1.26;
CC 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}.
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DR EMBL; AP006878; BAD84872.1; -; Genomic_DNA.
DR RefSeq; WP_011249634.1; NC_006624.1.
DR AlphaFoldDB; 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 HOGENOM; CLU_019796_1_2_2; -.
DR InParanoid; Q5JEZ2; -.
DR OMA; KMKPNCI; -.
DR OrthoDB; 36410at2157; -.
DR PhylomeDB; Q5JEZ2; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0047964; F:glyoxylate reductase (NAD+) activity; IEA:UniProtKB-UniRule.
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_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 Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..333
FT /note="Glyoxylate reductase"
FT /id="PRO_0000075950"
FT ACT_SITE 241
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT ACT_SITE 270
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT ACT_SITE 288
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT BINDING 158..161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT BINDING 180..182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT BINDING 239..241
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT BINDING 288..290
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-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