ID   GYAR_THEON              Reviewed;         334 AA.
AC   B6YWH0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=TON_0945;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(2008).
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; CP000855; ACJ16433.1; -; Genomic_DNA.
DR   RefSeq; WP_012571905.1; NC_011529.1.
DR   AlphaFoldDB; B6YWH0; -.
DR   SMR; B6YWH0; -.
DR   STRING; 523850.TON_0945; -.
DR   PRIDE; B6YWH0; -.
DR   EnsemblBacteria; ACJ16433; ACJ16433; TON_0945.
DR   GeneID; 7017248; -.
DR   KEGG; ton:TON_0945; -.
DR   PATRIC; fig|523850.10.peg.953; -.
DR   eggNOG; arCOG01755; Archaea.
DR   HOGENOM; CLU_019796_1_2_2; -.
DR   OMA; KMKPNCI; -.
DR   OrthoDB; 36410at2157; -.
DR   Proteomes; UP000002727; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047964; F:glyoxylate reductase (NAD+) activity; IEA:UniProtKB-UniRule.
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; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN           1..334
FT                   /note="Glyoxylate reductase"
FT                   /id="PRO_1000201582"
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   334 AA;  37780 MW;  19FB2B93FD933EBF CRC64;
     MKPKVLITRK IPENGIKMLR EHFEVEVWED EHEISREVLL EKVRDVDALV TMLSERIDAE
     VFDAAPRLKI VANYAVGYDN IDIEEATKMG VYITNTPDVL TNATADMAWV LLLATARRLI
     EADKFVRSGE WKKRGVAWHP LMFLGYDVYG RTIGIVGFGR IGQAIARRAK GFGMRILYNS
     RTRKPEVEKE LGAEFMPLDE LLKESDFVVL VVPLTKETYH MINEERLKLM KPTAILVNIA
     RGKVVDTEAL VKALREGWIA GAGLDVFEEE PYYHEELFSL DNVVLAPHIG SATYGAREGM
     AELVARNLIA FKNGEVPPTL VNREVLNVRK PGFE