ID   DHE3_PYRKO              Reviewed;         421 AA.
AC   O59650; Q5JDK3;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=Glutamate dehydrogenase;
DE            Short=GDH;
DE            EC=1.4.1.3;
GN   Name=gdhA; OrderedLocusNames=TK1431;
OS   Pyrococcus kodakaraensis (Thermococcus kodakaraensis).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RC   STRAIN=KOD1;
RX   MEDLINE=98179090; PubMed=9520268; DOI=10.1007/s004380050655;
RA   Rahman R.N.Z.A., Fujiwara S., Takagi M., Imanaka T.;
RT   "Sequence analysis of glutamate dehydrogenase (GDH) from the
RT   hyperthermophilic archaeon Pyrococcus sp. KOD1 and comparison of the
RT   enzymatic characteristics of native and recombinant GDHs.";
RL   Mol. Gen. Genet. 257:338-347(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon
RT   Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus
RT   genomes.";
RL   Genome Res. 15:352-363(2005).
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.
CC   -!- MISCELLANEOUS: Uses both NAD and NADP.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
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DR   EMBL; D89911; BAA25261.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD85620.1; -; Genomic_DNA.
DR   PIR; T44789; T44789.
DR   RefSeq; YP_183844.1; -.
DR   HSSP; O74024; 1EUZ.
DR   SMR; O59650; 5-420.
DR   GeneID; 3234478; -.
DR   GenomeReviews; AP006878_GR; TK1431.
DR   KEGG; tko:TK1431; -.
DR   NMPDR; fig|69014.3.peg.1302; -.
DR   HOGENOM; O59650; -.
DR   OMA; O59650; ANNKMGE.
DR   BioCyc; TKOD69014:TK1431-MON; -.
DR   BRENDA; 1.4.1.3; 192130.
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   Complete proteome; Cytoplasm; Direct protein sequencing; NAD; NADP;
KW   Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    421       Glutamate dehydrogenase.
FT                                /FTId=PRO_0000182759.
FT   NP_BIND     220    226       NAD (Potential).
FT   ACT_SITE    105    105       By similarity.
FT   CONFLICT    138    138       W -> C (in Ref. 1; BAA25261).
FT   CONFLICT    347    347       A -> T (in Ref. 1; BAA25261).
SQ   SEQUENCE   421 AA;  47056 MW;  13EF3F1DD1602E51 CRC64;
     MVEIDPFEMA VQQLERAAQF MDISEEALEW LKRPMRIVEV SVPVEMDDGS VKVFTGFRVQ
     HNWARGPTKG GIRWHPAETL STVKALATWM TWKVAVVDLP YGGGKGGIIV DPKKLSEREQ
     ERLARSYIRA VYDVIGPWTD IPAPDVYTNP KIMAWMMDEY ETIMRRKGPA FGVITGKPPG
     VGGIVARMDA TARGAAFTIR EAAKALGWDD LKGKTIAIQG YGNAGYYLHK IMSEEFGMKV
     VAVSDSKGGI YNPDGLPPAD EVLKWKKEHG SVKDMPGTQN ITNEELLELE VDILAPSAIE
     GVITKENADN VKAKIVAEVA NGPVTPEADE ILHEKGILQI PDFLCNAGGV TVSYFEWVQN
     INGFYWTVEE TRKRLDDKMT KAFWDVFNTH KEKNIHMRDA AYVVAVSRVY EAMKHRGWVK
     K
//