ID   DHE3_PYRWO              Reviewed;          24 AA.
AC   Q09115;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   16-JUN-2009, entry version 37.
DE   RecName: Full=Glutamate dehydrogenase;
DE            Short=GDH;
DE            EC=1.4.1.3;
DE   Flags: Fragment;
GN   Name=gdhA; Synonyms=gdh;
OS   Pyrococcus woesei.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=2262;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=94010338; PubMed=8406037; DOI=10.1016/0378-1119(93)90527-A;
RA   Eggen R.I.L., Geerling A.C.M., Waldkoetter K., Antranikian G.,
RA   de Vos W.M.;
RT   "The glutamate dehydrogenase-encoding gene of the hyperthermophilic
RT   archaeon Pyrococcus furiosus: sequence, transcription and analysis of
RT   the deduced amino acid sequence.";
RL   Gene 132:143-148(1993).
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.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
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DR   HSSP; P80319; 1GTM.
DR   BRENDA; 1.4.1.3; 7355.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; PARTIAL.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; NAD; NADP; Oxidoreductase.
FT   CHAIN         1    >24       Glutamate dehydrogenase.
FT                                /FTId=PRO_0000182760.
FT   NON_TER      24     24
SQ   SEQUENCE   24 AA;  2882 MW;  67FD81A4C45DBBC7 CRC64;
     VEQDPYEIVI KQLERAAQYM EISE
//