GYAR_PYRAB
ID GYAR_PYRAB Reviewed; 335 AA.
AC Q9UYR1; G8ZIK9;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=PYRAB14460;
GN ORFNames=PAB2374;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ248287; CAB50351.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70892.1; -; Genomic_DNA.
DR PIR; B75057; B75057.
DR RefSeq; WP_010868561.1; NC_000868.1.
DR AlphaFoldDB; Q9UYR1; -.
DR SMR; Q9UYR1; -.
DR STRING; 272844.PAB2374; -.
DR EnsemblBacteria; CAB50351; CAB50351; PAB2374.
DR GeneID; 1495721; -.
DR KEGG; pab:PAB2374; -.
DR PATRIC; fig|272844.11.peg.1537; -.
DR eggNOG; arCOG01755; Archaea.
DR HOGENOM; CLU_019796_1_2_2; -.
DR OMA; KMKPNCI; -.
DR OrthoDB; 36410at2157; -.
DR PhylomeDB; Q9UYR1; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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 3: Inferred from homology;
KW Cytoplasm; NAD; Oxidoreductase.
FT CHAIN 1..335
FT /note="Glyoxylate reductase"
FT /id="PRO_0000075947"
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 289
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 289..291
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00776"
SQ SEQUENCE 335 AA; 38270 MW; 32CEA1CB7126A0B4 CRC64;
MSKPRVFITR EIPEVGIEML EKEFEVEVWE DEREIPREIL LEKVKDVDAL VTMLSERIDR
EVFERAPRLR IVANYAVGYD NIDVEEATKR GIYVTNTPGV LTDATADLAF ALLLATARHL
VKGDKFTRSG EWKKRGVAWH PKWFLGYDVY GKTIGIIGFG RIGQAIAKRA RGFDMRILYY
SRTRKPEVEK ELNAEFKPLD ELLRESDFVV LAVPLNKETY HMINEERLKM MKRTAILINV
ARGKVIDTKA LIKALKEGWI AGAGLDVYEE EPYYNEELFS LDNVVLTPHI GSATFGAREG
MAKLVAENLI AFKRGEVPPT LVNREVLKVR KPGFQ
