ID   DHE3_THEPR              Reviewed;         419 AA.
AC   O74024;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 50.
DE   RecName: Full=Glutamate dehydrogenase;
DE            Short=GDH;
DE            EC=1.4.1.3;
GN   Name=gdhA; Synonyms=gdh;
OS   Thermococcus profundus.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=49899;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Higuchi S., Kobayashi T., Kimura K., Horikoshi K., Kudo T.;
RT   "Molecular cloning, nucleotide sequence and expression in Escherichia
RT   coli of hyperthermophilic glutamate dehydrogenase gene from
RT   Thermococcus profundus.";
RL   J. Ferment. Bioeng. 83:405-411(1997).
CC   -!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NAD(P)(+) = 2-
CC       oxoglutarate + NH(3) + NAD(P)H.
CC   -!- SUBUNIT: Homohexamer (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; D87814; BAA28943.1; -; Genomic_DNA.
DR   PIR; T44308; T44308.
DR   PDB; 1EUZ; X-ray; 2.25 A; A/B/C/D/E/F=1-419.
DR   PDBsum; 1EUZ; -.
DR   BRENDA; 1.4.1.3; 256746.
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   3D-structure; NAD; NADP; Oxidoreductase.
FT   CHAIN         1    419       Glutamate dehydrogenase.
FT                                /FTId=PRO_0000182763.
FT   NP_BIND     219    225       NAD (Potential).
FT   ACT_SITE    105    105       By similarity.
FT   HELIX         5     17
FT   HELIX        25     32
FT   STRAND       35     45
FT   STRAND       51     62
FT   STRAND       66     74
FT   HELIX        80     96
FT   STRAND      102    110
FT   HELIX       117    131
FT   HELIX       132    134
FT   TURN        137    139
FT   STRAND      140    143
FT   HELIX       150    164
FT   HELIX       170    173
FT   HELIX       179    181
FT   HELIX       190    206
FT   STRAND      214    218
FT   HELIX       222    233
FT   STRAND      238    243
FT   STRAND      248    250
FT   HELIX       257    267
FT   STRAND      268    270
FT   STRAND      277    279
FT   HELIX       281    284
FT   STRAND      290    294
FT   STRAND      296    299
FT   TURN        303    305
FT   HELIX       306    308
FT   STRAND      312    315
FT   STRAND      318    320
FT   HELIX       324    332
FT   STRAND      336    338
FT   HELIX       340    343
FT   HELIX       346    359
FT   HELIX       366    391
FT   HELIX       395    413
SQ   SEQUENCE   419 AA;  46700 MW;  1DF3C1122E562706 CRC64;
     MVEIDPFEMA VKQLERAAQY MDISEEALEW LKKPMRIVEV SVPIEMDDGS VKVFTGFRVQ
     HNWARGPTKG GIRWHPAETL STVKALATWM TWKVAVVDLP YGGGKGGIIV NPKELSEREQ
     ERLARAYIRA VYDVIGPWTD IPAPDVYTNP KIMGWMMDEY ETIMRRKGPA FGVITGKPLS
     IGGSLGRGTA TAQGAIFTIR EAAKALGIDL KGKKIAVQGY GNAGYYTAKL AKEQLGMTVV
     AVSDSRGGIY NPDGLDPDEV LKWKREHGSV KDFPGATNIT NEELLELEVD VLAPAAIEEV
     ITEKNADNIK AKIVAEVANG PVTPEADDIL REKGILQIPD FLCNAGGVTV SYFEWVQNIN
     GYYWTEEEVR EKLDKKMTKA FWEVYNTHKD KNIHMRDAAY VVAVSRVYQA MKDRGWVKK
//