ID   GYAR_THEPD              Reviewed;         339 AA.
AC   A1RYE4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=Tpen_0823;
OS   Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC   Thermofilum.
OX   NCBI_TaxID=368408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2475 / Hrk 5;
RX   PubMed=18263724; DOI=10.1128/jb.01949-07;
RA   Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA   Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA   Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA   Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT   "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT   biosynthetic pathways without genome reduction.";
RL   J. Bacteriol. 190:2957-2965(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; CP000505; ABL78224.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1RYE4; -.
DR   SMR; A1RYE4; -.
DR   STRING; 368408.Tpen_0823; -.
DR   EnsemblBacteria; ABL78224; ABL78224; Tpen_0823.
DR   KEGG; tpe:Tpen_0823; -.
DR   eggNOG; arCOG01755; Archaea.
DR   HOGENOM; CLU_019796_1_3_2; -.
DR   OMA; KMKPNCI; -.
DR   Proteomes; UP000000641; 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..339
FT                   /note="Glyoxylate reductase"
FT                   /id="PRO_0000348416"
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        289
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT   BINDING         157..160
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         289..291
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
SQ   SEQUENCE   339 AA;  37993 MW;  83C1C68D2F9A7E5C CRC64;
     MARPKVYVTR IIPEPGLSML KECCDVVVHE SKDWPPSREE LLRNIRDKDA LLCLLTDKID
     AEVMDAAPNL KVISTYSVGF DHIDIPEATK RGIYVTHTPG VLTDAVAEFT VGLILAVTRR
     IVEADKIIRT GQWDKPWNPY FLTGPELKGK TIGLVGLGRI GVATAKRLSS FDVKILYYDI
     ERRWDVETVI PNMEFTDLDT LLEKSDIVSI HVPLTKETYH LINEERLRKM KKTAYLINTA
     RGPVVDTEAL VKALKEGWIA GAALDVFEQE PLPPNHPLTK FDNVVLAPHI ASATIEARQR
     MAELAARNLI AVLKGEMPPA LVNKEVLKVR PLEKVKMIP