GenomeNet

Database: UniProt
Entry: Q9UYR1
LinkDB: Q9UYR1
Original site: Q9UYR1 
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   16-JAN-2019, entry version 105.
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};
GN   OrderedLocusNames=PYRAB14460; 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.,
RA   Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic
RT   archaeon 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
RT   and 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;
CC         EC=1.1.1.26; 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}.
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   ProteinModelPortal; 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   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136700; -.
DR   KO; K00015; -.
DR   OMA; KWIAHNG; -.
DR   OrthoDB; 36410at2157; -.
DR   BioCyc; PABY272844:G1GT8-1590-MONOMER; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047964; F:glyoxylate reductase 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   Complete proteome; Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN         1    335       Glyoxylate reductase.
FT                                /FTId=PRO_0000075947.
FT   NP_BIND     159    162       NADP. {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   NP_BIND     181    183       NADP. {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   NP_BIND     240    242       NADP. {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   NP_BIND     289    291       NADP. {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   ACT_SITE    242    242       {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   ACT_SITE    271    271       {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   ACT_SITE    289    289       Proton donor. {ECO:0000255|HAMAP-
FT                                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
//
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