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Database: UniProt
Entry: Q8U3Y2
LinkDB: Q8U3Y2
Original site: Q8U3Y2 
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   16-JAN-2019, entry version 97.
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;
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
RT   P. 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;
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; AE009950; AAL80443.1; -; Genomic_DNA.
DR   RefSeq; WP_011011434.1; NC_003413.1.
DR   PDB; 5AOV; X-ray; 1.40 A; A=1-336.
DR   PDBsum; 5AOV; -.
DR   ProteinModelPortal; Q8U3Y2; -.
DR   SMR; Q8U3Y2; -.
DR   STRING; 186497.PF0319; -.
DR   PRIDE; Q8U3Y2; -.
DR   EnsemblBacteria; AAL80443; AAL80443; PF0319.
DR   GeneID; 1468154; -.
DR   KEGG; pfu:PF0319; -.
DR   PATRIC; fig|186497.12.peg.334; -.
DR   eggNOG; arCOG01755; Archaea.
DR   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136700; -.
DR   KO; K00015; -.
DR   OMA; KWIAHNG; -.
DR   OrthoDB; 36410at2157; -.
DR   BioCyc; MetaCyc:MONOMER-17245; -.
DR   BioCyc; PFUR186497:G1FZR-332-MONOMER; -.
DR   Proteomes; UP000001013; 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   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    336       Glyoxylate reductase.
FT                                /FTId=PRO_0000075948.
FT   NP_BIND     158    161       NADP. {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   NP_BIND     180    182       NADP. {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   NP_BIND     239    241       NADP. {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   NP_BIND     288    290       NADP. {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   ACT_SITE    241    241       {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   ACT_SITE    270    270       {ECO:0000255|HAMAP-Rule:MF_00776}.
FT   ACT_SITE    288    288       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00776}.
FT   STRAND        4      7       {ECO:0000244|PDB:5AOV}.
FT   HELIX        13     20       {ECO:0000244|PDB:5AOV}.
FT   STRAND       23     27       {ECO:0000244|PDB:5AOV}.
FT   HELIX        36     42       {ECO:0000244|PDB:5AOV}.
FT   HELIX        43     45       {ECO:0000244|PDB:5AOV}.
FT   STRAND       47     51       {ECO:0000244|PDB:5AOV}.
FT   HELIX        59     63       {ECO:0000244|PDB:5AOV}.
FT   STRAND       70     76       {ECO:0000244|PDB:5AOV}.
FT   HELIX        83     88       {ECO:0000244|PDB:5AOV}.
FT   STRAND       92     94       {ECO:0000244|PDB:5AOV}.
FT   HELIX       101    117       {ECO:0000244|PDB:5AOV}.
FT   HELIX       119    127       {ECO:0000244|PDB:5AOV}.
FT   HELIX       130    134       {ECO:0000244|PDB:5AOV}.
FT   TURN        140    143       {ECO:0000244|PDB:5AOV}.
FT   STRAND      152    157       {ECO:0000244|PDB:5AOV}.
FT   HELIX       160    170       {ECO:0000244|PDB:5AOV}.
FT   TURN        171    173       {ECO:0000244|PDB:5AOV}.
FT   STRAND      175    179       {ECO:0000244|PDB:5AOV}.
FT   HELIX       185    191       {ECO:0000244|PDB:5AOV}.
FT   HELIX       198    204       {ECO:0000244|PDB:5AOV}.
FT   STRAND      206    210       {ECO:0000244|PDB:5AOV}.
FT   TURN        216    220       {ECO:0000244|PDB:5AOV}.
FT   HELIX       224    229       {ECO:0000244|PDB:5AOV}.
FT   STRAND      235    238       {ECO:0000244|PDB:5AOV}.
FT   HELIX       242    244       {ECO:0000244|PDB:5AOV}.
FT   HELIX       247    255       {ECO:0000244|PDB:5AOV}.
FT   STRAND      258    265       {ECO:0000244|PDB:5AOV}.
FT   STRAND      268    271       {ECO:0000244|PDB:5AOV}.
FT   HELIX       275    278       {ECO:0000244|PDB:5AOV}.
FT   STRAND      283    285       {ECO:0000244|PDB:5AOV}.
FT   HELIX       294    312       {ECO:0000244|PDB:5AOV}.
FT   HELIX       325    328       {ECO:0000244|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
//
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