ID   DHE3_PYRAB              Reviewed;         420 AA.
AC   Q47950;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Glutamate dehydrogenase;
DE            Short=GDH;
DE            EC=1.4.1.3;
GN   Name=gdhA; Synonyms=gdh; OrderedLocusNames=PYRAB05690;
GN   ORFNames=PAB0391;
OS   Pyrococcus abyssi.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=29292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   MEDLINE=22511545; PubMed=12622808;
RX   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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-255.
RC   STRAIN=GE5 / Orsay;
RA   Borges K.M., Diruggiero J., Robb F.T.;
RT   "Cloning and sequencing of glutamate dehydrogenases from
RT   hyperthermophilic archaea.";
RL   Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NAD(P)(+) = 2-
CC       oxoglutarate + NH(3) + NAD(P)H.
CC   -!- SUBUNIT: Homohexamer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
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DR   EMBL; AJ248284; CAB49491.1; -; Genomic_DNA.
DR   EMBL; L19116; AAA64796.1; -; Genomic_DNA.
DR   PIR; D75176; D75176.
DR   RefSeq; NP_126260.1; -.
DR   HSSP; P80319; 1GTM.
DR   SMR; Q47950; 5-420.
DR   GeneID; 1495474; -.
DR   GenomeReviews; AL096836_GR; PYRAB05690.
DR   KEGG; pab:PAB0391; -.
DR   NMPDR; fig|272844.1.peg.598; -.
DR   HOGENOM; Q47950; -.
DR   OMA; Q47950; YLAKIMS.
DR   BioCyc; PABY272844:PAB0391-MON; -.
DR   BRENDA; 1.4.1.3; 262861.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer.
DR   InterPro; IPR014362; Glu_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11606:SF2; GLFV_DH; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000185; Glu_DH; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase.
FT   CHAIN         1    420       Glutamate dehydrogenase.
FT                                /FTId=PRO_0000182755.
FT   NP_BIND     220    226       NAD (Potential).
FT   ACT_SITE    105    105       By similarity.
SQ   SEQUENCE   420 AA;  47098 MW;  82F8B343572DFE2B CRC64;
     MVEQDPFEIA VKQLERAAQY MKISEEALEF LKRPQRIVEV TIPVEMDDGS VKVFTGFRVQ
     YNWARGPTKG GIRWHPEETL STVKALAAWM TWKTAVMDLP YGGGKGGIIV DPKKLSDREK
     ERLARGYIRA IYDVISPYED IPAPDVYTNP QIMAWMMDEY ETIARRKTPA FGIITGKPLS
     IGGSLGRNEA TARGASYTIR EAAKVLGWDD LKGKTIAIQG YGNAGYYLAK IMSEDYGMKV
     VAVSDSKGGI YNPDGLNADE VLKWKREHGS VKDFPGATNI TNEELLELEV DVLAPAAIEE
     VITKKNADNI KAKIVAEVAN GPVTPEADEI LFEKGILQIP DFLCNAGGVT VSYFEWVQNI
     TGYYWTLEEV REKLDKKMTK AFYDVYNTAK EKNIHMRDAA YVVAVQRVYQ AMLDRGWVKH
//