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GYAR_KORCO
ID   GYAR_KORCO              Reviewed;         332 AA.
AC   B1L765;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Kcr_1548;
OS   Korarchaeum cryptofilum (strain OPF8).
OC   Archaea; Candidatus Korarchaeota; Candidatus Korarchaeum.
OX   NCBI_TaxID=374847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OPF8;
RX   PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA   Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA   Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA   Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA   Richardson P., Keller M., Stetter K.O.;
RT   "A korarchaeal genome reveals new insights into the evolution of the
RT   Archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(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; CP000968; ACB08294.1; -; Genomic_DNA.
DR   RefSeq; WP_012310191.1; NC_010482.1.
DR   AlphaFoldDB; B1L765; -.
DR   SMR; B1L765; -.
DR   STRING; 374847.Kcr_1548; -.
DR   EnsemblBacteria; ACB08294; ACB08294; Kcr_1548.
DR   GeneID; 6094825; -.
DR   KEGG; kcr:Kcr_1548; -.
DR   eggNOG; arCOG01755; Archaea.
DR   HOGENOM; CLU_019796_1_3_2; -.
DR   InParanoid; B1L765; -.
DR   OMA; KMKPNCI; -.
DR   OrthoDB; 36410at2157; -.
DR   PhylomeDB; B1L765; -.
DR   Proteomes; UP000001686; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0047964; F:glyoxylate reductase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IBA:GO_Central.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central.
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..332
FT                   /note="Glyoxylate reductase"
FT                   /id="PRO_0000348415"
FT   ACT_SITE        238
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT   ACT_SITE        286
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT   BINDING         155..158
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT   BINDING         236..238
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
FT   BINDING         286..288
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
SQ   SEQUENCE   332 AA;  37477 MW;  4A4A0FCA2D144207 CRC64;
     MKPRVFVTRE IPERGLSKIE EHFELDLWKD EAPPSKKVII ERVKDCDALV SLLTDPIDAE
     VFEAAPKLRI VAQYAVGYDN IDVKEATKRG IYVTNTPGVL TETTADFAFA LLMAAARRVV
     EADRYVREGK WKVAWHPMMM LGYDVYGRTL GIVGMGRIGA AVARRAKGFG MRILYYDSIR
     REDFEKELGV EYVPLEKLLE ESDFVSLHVP LTEETYHMIG EEQLRRMKRT AILVNTSRGK
     VVDQKALYKA LKEGWIAGAG LDVFEQEPIP PDDPLLKLEN VVLAPHAASA SHETRSRMAE
     MVAENLIAFK RGEIPPNLVN QEVVKVRPPG FQ
 
 
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