ID   DHE3_THEKO              Reviewed;         421 AA.
AC   O59650; Q5JDK3;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Glutamate dehydrogenase;
DE            Short=GDH;
DE            EC=1.4.1.3;
GN   Name=gdhA; OrderedLocusNames=TK1431;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
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=ATCC BAA-918 / JCM 12380 / KOD1;
RX   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=ATCC BAA-918 / JCM 12380 / 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 Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC         NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.3;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10011};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH +
CC         NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.3;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10011};
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.
CC       {ECO:0000305}.
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DR   EMBL; D89911; BAA25261.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD85620.1; -; Genomic_DNA.
DR   PIR; T44789; T44789.
DR   RefSeq; WP_011250382.1; NC_006624.1.
DR   AlphaFoldDB; O59650; -.
DR   SMR; O59650; -.
DR   STRING; 69014.TK1431; -.
DR   EnsemblBacteria; BAD85620; BAD85620; TK1431.
DR   GeneID; 78447955; -.
DR   KEGG; tko:TK1431; -.
DR   PATRIC; fig|69014.16.peg.1392; -.
DR   eggNOG; arCOG01352; Archaea.
DR   HOGENOM; CLU_025763_1_2_2; -.
DR   InParanoid; O59650; -.
DR   OrthoDB; 6425at2157; -.
DR   PhylomeDB; O59650; -.
DR   BRENDA; 1.4.1.3; 5246.
DR   SABIO-RK; O59650; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR   CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR014362; Glu_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
DR   NCBIfam; NF040817; GdhA_Arch; 1.
DR   PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 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   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; NAD; NADP; Oxidoreductase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9520268"
FT   CHAIN           2..421
FT                   /note="Glutamate dehydrogenase"
FT                   /id="PRO_0000182759"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   BINDING         220..226
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        138
FT                   /note="W -> C (in Ref. 1; BAA25261)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        347
FT                   /note="A -> T (in Ref. 1; BAA25261)"
FT                   /evidence="ECO:0000305"
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
//