GYAR_PYRHO
ID GYAR_PYRHO Reviewed; 334 AA.
AC O58320;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Glyoxylate reductase;
DE EC=1.1.1.26;
GN Name=gyaR; OrderedLocusNames=PH0597;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NADP.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of glyoxylate reductase (ph0597) from Pyrococcus
RT horikoshii OT3, complexed with nadp (i41).";
RL Submitted (JUN-2006) to the PDB data bank.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. GyaR subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA29686.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000001; BAA29686.1; ALT_INIT; Genomic_DNA.
DR PIR; A71175; A71175.
DR RefSeq; WP_010884698.1; NC_000961.1.
DR PDB; 2DBQ; X-ray; 1.70 A; A=1-334.
DR PDB; 2DBR; X-ray; 2.61 A; A/B/C/D/E/F=1-334.
DR PDB; 2DBZ; X-ray; 2.45 A; A/B=1-334.
DR PDBsum; 2DBQ; -.
DR PDBsum; 2DBR; -.
DR PDBsum; 2DBZ; -.
DR AlphaFoldDB; O58320; -.
DR SMR; O58320; -.
DR STRING; 70601.3257003; -.
DR EnsemblBacteria; BAA29686; BAA29686; BAA29686.
DR GeneID; 1442932; -.
DR KEGG; pho:PH0597; -.
DR eggNOG; arCOG01755; Archaea.
DR OMA; KMKPNCI; -.
DR OrthoDB; 36410at2157; -.
DR EvolutionaryTrace; O58320; -.
DR Proteomes; UP000000752; 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.
FT CHAIN 1..334
FT /note="Glyoxylate reductase"
FT /id="PRO_0000075949"
FT ACT_SITE 241
FT /evidence="ECO:0000250"
FT ACT_SITE 270
FT /evidence="ECO:0000250"
FT ACT_SITE 288
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 158..161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 180..182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 239..241
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 288..290
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:2DBQ"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:2DBQ"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:2DBQ"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2DBZ"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:2DBQ"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2DBZ"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:2DBQ"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:2DBQ"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:2DBQ"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:2DBQ"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2DBQ"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2DBZ"
FT HELIX 101..117
FT /evidence="ECO:0007829|PDB:2DBQ"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:2DBQ"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:2DBQ"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:2DBQ"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:2DBQ"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:2DBQ"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:2DBQ"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:2DBR"
FT HELIX 185..191
FT /evidence="ECO:0007829|PDB:2DBQ"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2DBZ"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:2DBQ"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:2DBQ"
FT TURN 216..220
FT /evidence="ECO:0007829|PDB:2DBQ"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:2DBQ"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:2DBQ"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:2DBQ"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:2DBQ"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:2DBQ"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:2DBQ"
FT HELIX 275..279
FT /evidence="ECO:0007829|PDB:2DBQ"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:2DBQ"
FT HELIX 294..312
FT /evidence="ECO:0007829|PDB:2DBQ"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:2DBQ"
SQ SEQUENCE 334 AA; 38000 MW; C0056A354ECBE202 CRC64;
MKPKVFITRE IPEVGIKMLE DEFEVEVWGD EKEIPREILL KKVKEVDALV TMLSERIDKE
VFENAPKLRI VANYAVGYDN IDIEEATKRG IYVTNTPDVL TDATADLAFA LLLATARHVV
KGDRFVRSGE WKKRGVAWHP KWFLGYDVYG KTIGIIGLGR IGQAIAKRAK GFNMRILYYS
RTRKEEVERE LNAEFKPLED LLRESDFVVL AVPLTRETYH LINEERLKLM KKTAILINIA
RGKVVDTNAL VKALKEGWIA GAGLDVFEEE PYYNEELFKL DNVVLTPHIG SASFGAREGM
AELVAKNLIA FKRGEIPPTL VNREVIKIRK PGFE
