ID   DHE3_PYREN              Reviewed;         420 AA.
AC   Q47951;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 44.
DE   RecName: Full=Glutamate dehydrogenase;
DE            Short=GDH;
DE            EC=1.4.1.3;
GN   Name=gdhA;
OS   Pyrococcus endeavori.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=39456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP   CHARACTERIZATION.
RC   STRAIN=ES4;
RX   MEDLINE=93352584; PubMed=8349661;
RA   Diruggiero J., Robb F.T., Jagus R., Klump H.H., Borges K.M.,
RA   Kessel M., Mai X., Adams M.W.W.A.;
RT   "Characterization, cloning, and in vitro expression of the extremely
RT   thermostable glutamate dehydrogenase from the hyperthermophilic
RT   Archaeon, ES4.";
RL   J. Biol. Chem. 268:17767-17774(1993).
CC   -!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NAD(P)(+) = 2-
CC       oxoglutarate + NH(3) + NAD(P)H.
CC   -!- SUBUNIT: Homohexamer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L12408; AAA64795.1; -; Genomic_DNA.
DR   PIR; A47410; A47410.
DR   HSSP; P80319; 1GTM.
DR   SMR; Q47951; 5-420.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; NAD; NADP; Oxidoreductase.
FT   CHAIN         1    420       Glutamate dehydrogenase.
FT                                /FTId=PRO_0000182756.
FT   NP_BIND     220    226       NAD (Potential).
FT   ACT_SITE    105    105       By similarity.
SQ   SEQUENCE   420 AA;  47141 MW;  26C571CC5DEF85CB CRC64;
     MVEQDPFEIA VKQLERAAQY MKISEEALEF LKRPQRIVEV TIPVEMDDGT VKVFTGFRVQ
     YNWARGPTKG GIRWHPEETL STVKALAAWM TWKTAVMDLP YGGGKGGIIV DPKKLSDREK
     ERLARGYIRA IYDVISPYED IPAPDVYTNP QIMAWMMDEY EAISRRKTPA FGIITGKPLS
     IGGSLGRNEA TARGASYTIR EARKVLGWGD LKGKTIAIQG YGNAGYYLAK IMSEDYGMKV
     VAVSDSKGGI YNPDGLNADE VLKWKQEHGS VKDFPGATNI TNEELLELEV DVLAPAAIEE
     VITKKNADNI KAKIVAEVAN GPVTPEADEI LFEKGILQIP DFLCNAGGVT VSYFEWVQNI
     TGYYWTLEEV REKLDKKMTK AFYDVYNTAK EKNIHMRDAD YVVAVQRVYQ AMLDRGWVKH
//