ID   GYAR_THELN              Reviewed;         331 AA.
AC   Q9C4M5; H3ZJV9;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 98.
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}; Synonyms=gr;
GN   ORFNames=OCC_02245;
OS   Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19,
RP   CHARACTERIZATION, AND SUBUNIT.
RC   STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX   PubMed=11532010; DOI=10.1046/j.1432-1327.2001.02394.x;
RA   Ohshima T., Nunoura-Kominato N., Kudome T., Sakuraba H.;
RT   "A novel hyperthermophilic archaeal glyoxylate reductase from Thermococcus
RT   litoralis. Characterization, gene cloning, nucleotide sequence and
RT   expression in Escherichia coli.";
RL   Eur. J. Biochem. 268:4740-4747(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX   PubMed=22493191; DOI=10.1128/jb.00123-12;
RA   Gardner A.F., Kumar S., Perler F.B.;
RT   "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT   litoralis NS-C.";
RL   J. Bacteriol. 194:2375-2376(2012).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.73 mM for glyoxylate;
CC         KM=1.3 mM for hydroxypyruvate;
CC         KM=0.067 mM for NADH;
CC       pH dependence:
CC         Optimum pH is 6.5.;
CC       Temperature dependence:
CC         Optimum temperature is 90 degrees Celsius. Extremely thermostable.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00776,
CC       ECO:0000269|PubMed:11532010}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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; AB033995; BAB40320.1; -; Genomic_DNA.
DR   EMBL; CP006670; EHR79758.1; -; Genomic_DNA.
DR   RefSeq; WP_004066272.1; NC_022084.1.
DR   AlphaFoldDB; Q9C4M5; -.
DR   SMR; Q9C4M5; -.
DR   STRING; 523849.OCC_02245; -.
DR   EnsemblBacteria; EHR79758; EHR79758; OCC_02245.
DR   GeneID; 16548498; -.
DR   KEGG; tlt:OCC_02245; -.
DR   HOGENOM; CLU_019796_1_2_2; -.
DR   OMA; KMKPNCI; -.
DR   OrthoDB; 36410at2157; -.
DR   BRENDA; 1.1.1.26; 6302.
DR   SABIO-RK; Q9C4M5; -.
DR   Proteomes; UP000015502; 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; 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase.
FT   CHAIN           1..331
FT                   /note="Glyoxylate reductase"
FT                   /id="PRO_0000075951"
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   331 AA;  36808 MW;  E277D769D82B9763 CRC64;
     MKPKVFITRQ IPENGIKMIE KFYEIELWKD PKAPPRGVLL EKVREVDALV TLVTDKVDKE
     LLENAPKLKI IAQYAVGYDN IDIEEATKRG IYVTNTPGVL TDATADLAFA LLLAVARRIV
     EADAFVRSGE WKKSEVGWHP LMFLGYGLKG KTLGIVGFGR IGQALAKRAK GFGMKIIYYS
     RTRKPEAEEE IGAEYVDFET LLKESDFISL HVPLTKETYH MIGEKELKLM KPNAILINTS
     RGAVVDTNAL IKALKEGWIA GAGLDVFEEE PYYNEELFKL KNVVLAPHIG SATHEAREGM
     AELVAKNLIA FAKGEIPPNL VNKDVLTSSP P