ID   GYAR_AERPE              Reviewed;         335 AA.
AC   Q9YAW4;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   03-AUG-2022, entry version 113.
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=APE_1831.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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; BA000002; BAA80834.2; -; Genomic_DNA.
DR   PIR; E72568; E72568.
DR   AlphaFoldDB; Q9YAW4; -.
DR   SMR; Q9YAW4; -.
DR   STRING; 272557.APE_1831.1; -.
DR   EnsemblBacteria; BAA80834; BAA80834; APE_1831.1.
DR   KEGG; ape:APE_1831.1; -.
DR   PATRIC; fig|272557.25.peg.1228; -.
DR   eggNOG; arCOG01755; Archaea.
DR   OMA; KMKPNCI; -.
DR   Proteomes; UP000002518; 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   3: Inferred from homology;
KW   Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..335
FT                   /note="Glyoxylate reductase"
FT                   /id="PRO_0000075946"
FT   ACT_SITE        242
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT   ACT_SITE        290
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT   BINDING         159..162
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT   BINDING         181..183
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT   BINDING         240..242
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT   BINDING         290..292
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
SQ   SEQUENCE   335 AA;  37757 MW;  0CD5EE38E1AA6163 CRC64;
     MKRPRVFVTR EVFPEALELL SKYYDVEVWD KYQPPPYETL LSKAREADAL YTLLTDRIDC
     DLLSQAPRLR IVAQMAVGFD NIDVECATRL GIYVTNTPGV LTEATAEFTW ALILAAARRV
     VEADHFVRWG EWWRLRTGWH PMMMLGVELR GKTLGILGMG RIGSRVAEIG KAFGMRIIYH
     SRSRKREIEK ELGAEYRSLE DLLRESDILS IHLPLTDETR HLIGESELKL MKKTAILVNT
     GRGAIVDTGA LVKALREGWI AAAALDVFEE EPLNPNHPLT AFKNVVLAPH AASATRETRL
     RMAMMAAENL VAFAQGKVPP NLVNREVVKV RQPGF