GYAR_PYRFU
ID GYAR_PYRFU Reviewed; 336 AA.
AC Q8U3Y2;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=PF0319;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(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; AE009950; AAL80443.1; -; Genomic_DNA.
DR RefSeq; WP_011011434.1; NZ_CP023154.1.
DR PDB; 5AOV; X-ray; 1.40 A; A=1-336.
DR PDBsum; 5AOV; -.
DR AlphaFoldDB; Q8U3Y2; -.
DR SMR; Q8U3Y2; -.
DR STRING; 186497.PF0319; -.
DR PRIDE; Q8U3Y2; -.
DR EnsemblBacteria; AAL80443; AAL80443; PF0319.
DR GeneID; 41712111; -.
DR KEGG; pfu:PF0319; -.
DR PATRIC; fig|186497.12.peg.334; -.
DR eggNOG; arCOG01755; Archaea.
DR HOGENOM; CLU_019796_1_2_2; -.
DR OMA; KMKPNCI; -.
DR OrthoDB; 36410at2157; -.
DR PhylomeDB; Q8U3Y2; -.
DR BioCyc; MetaCyc:MON-17245; -.
DR BRENDA; 1.1.1.79; 5243.
DR BRENDA; 1.1.1.81; 5243.
DR Proteomes; UP000001013; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..336
FT /note="Glyoxylate reductase"
FT /id="PRO_0000075948"
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"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:5AOV"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:5AOV"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:5AOV"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:5AOV"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 101..117
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:5AOV"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:5AOV"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:5AOV"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:5AOV"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 185..191
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:5AOV"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:5AOV"
FT TURN 216..220
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:5AOV"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:5AOV"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:5AOV"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:5AOV"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 294..312
FT /evidence="ECO:0007829|PDB:5AOV"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:5AOV"
SQ SEQUENCE 336 AA; 38342 MW; CFC48402FD2073B5 CRC64;
MKPKVFITRA IPENGINMLE EEFEVEVWEE EREIPREKLL EKVKDVDALV TMLSERIDQE
VFENAPRLRI VANYAVGYDN IDVEEATRRG IYVTNTPDVL TNATADHAFA LLLATARHVV
KGDKFVRSGE WKRKGIAWHP KWFLGYELYG KTIGIVGFGR IGQAIARRAK GFNMRILYYS
RTRKSQAEKE LGAEYRPLEE VLKESDFVIL AVPLTKETMY MINEERLKLM KPTAILVNIA
RGKVVDTKAL IKALKEGWIA GAGLDVFEEE PYYNEELFSL DNVVLTPHIG SATFEAREAM
AELVARNLIA FKRGEIPPTL VNKEVIKIRK PGFNEQ
