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