GYAR_THEGJ
ID GYAR_THEGJ Reviewed; 334 AA.
AC C5A1V0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=TGAM_1867;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
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; CP001398; ACS34369.1; -; Genomic_DNA.
DR RefSeq; WP_015859478.1; NC_012804.1.
DR AlphaFoldDB; C5A1V0; -.
DR SMR; C5A1V0; -.
DR STRING; 593117.TGAM_1867; -.
DR PaxDb; C5A1V0; -.
DR EnsemblBacteria; ACS34369; ACS34369; TGAM_1867.
DR GeneID; 7988271; -.
DR KEGG; tga:TGAM_1867; -.
DR PATRIC; fig|593117.10.peg.1876; -.
DR eggNOG; arCOG01755; Archaea.
DR HOGENOM; CLU_019796_1_2_2; -.
DR OMA; KMKPNCI; -.
DR OrthoDB; 36410at2157; -.
DR Proteomes; UP000001488; 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; IPR015878; Ado_hCys_hydrolase_NAD-bd.
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 SMART; SM00997; AdoHcyase_NAD; 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.
FT CHAIN 1..334
FT /note="Glyoxylate reductase"
FT /id="PRO_1000212917"
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; 37740 MW; 7D9C41EE6405DFCB CRC64;
MKPKVFITRA IPENGIDMLR EHFEVEVWPE EREIPREVLL EKVRDVDALV TMLSERIDGE
VFDNAPRLRI VANYAVGYDN VDVEEATRRG IYVTNTPDVL TNATADFAWT LLLATARRLI
EADSFTRSGE WKRKGIAWHP LMFLGHDVYG KTIGIIGFGR IGQAVARRAK GFGMRILYYS
RTRKPEAEEE LKAEFKPLEE LLKESDFVVL AVPLTKETYH MIGERELKLM KPTAILVNIA
RGKVVDTEAL IKALKEGWIA GAGLDVFEEE PYYNEELFSL KNVILAPHIG SATFGAREGM
AELVARNLIA FKNGEVPPTL VNKEVVKVKK PGFR