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Database: UniProt
Entry: Q9C4M5
LinkDB: Q9C4M5
Original site: Q9C4M5 
ID   GYAR_THELN              Reviewed;         331 AA.
AC   Q9C4M5; H3ZJV9;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-JAN-2019, entry version 87.
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}; Synonyms=gr;
GN   ORFNames=OCC_02245;
OS   Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 /
OS   NS-C).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19,
RP   CHARACTERIZATION, AND SUBUNIT.
RC   STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX   PubMed=11532010; DOI=10.1046/j.1432-1327.2001.02394.x;
RA   Ohshima T., Nunoura-Kominato N., Kudome T., Sakuraba H.;
RT   "A novel hyperthermophilic archaeal glyoxylate reductase from
RT   Thermococcus litoralis. Characterization, gene cloning, nucleotide
RT   sequence and expression in Escherichia coli.";
RL   Eur. J. Biochem. 268:4740-4747(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX   PubMed=22493191; DOI=10.1128/JB.00123-12;
RA   Gardner A.F., Kumar S., Perler F.B.;
RT   "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT   litoralis NS-C.";
RL   J. Bacteriol. 194:2375-2376(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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.73 mM for glyoxylate;
CC         KM=1.3 mM for hydroxypyruvate;
CC         KM=0.067 mM for NADH;
CC       pH dependence:
CC         Optimum pH is 6.5.;
CC       Temperature dependence:
CC         Optimum temperature is 90 degrees Celsius. Extremely
CC         thermostable.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00776,
CC       ECO:0000269|PubMed:11532010}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. GyaR subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00776}.
DR   EMBL; AB033995; BAB40320.1; -; Genomic_DNA.
DR   EMBL; CP006670; EHR79758.1; -; Genomic_DNA.
DR   RefSeq; WP_004066272.1; NC_022084.1.
DR   ProteinModelPortal; Q9C4M5; -.
DR   SMR; Q9C4M5; -.
DR   EnsemblBacteria; EHR79758; EHR79758; OCC_02245.
DR   GeneID; 16548498; -.
DR   KEGG; tlt:OCC_02245; -.
DR   KO; K00015; -.
DR   OMA; KWIAHNG; -.
DR   OrthoDB; 36410at2157; -.
DR   BRENDA; 1.1.1.26; 6302.
DR   SABIO-RK; Q9C4M5; -.
DR   Proteomes; UP000015502; 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Direct protein sequencing; NAD;
KW   Oxidoreductase.
FT   CHAIN         1    331       Glyoxylate reductase.
FT                                /FTId=PRO_0000075951.
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}.
SQ   SEQUENCE   331 AA;  36808 MW;  E277D769D82B9763 CRC64;
     MKPKVFITRQ IPENGIKMIE KFYEIELWKD PKAPPRGVLL EKVREVDALV TLVTDKVDKE
     LLENAPKLKI IAQYAVGYDN IDIEEATKRG IYVTNTPGVL TDATADLAFA LLLAVARRIV
     EADAFVRSGE WKKSEVGWHP LMFLGYGLKG KTLGIVGFGR IGQALAKRAK GFGMKIIYYS
     RTRKPEAEEE IGAEYVDFET LLKESDFISL HVPLTKETYH MIGEKELKLM KPNAILINTS
     RGAVVDTNAL IKALKEGWIA GAGLDVFEEE PYYNEELFKL KNVVLAPHIG SATHEAREGM
     AELVAKNLIA FAKGEIPPNL VNKDVLTSSP P
//
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