ID   DHE3_PYRAB              Reviewed;         420 AA.
AC   Q47950; G8ZJ34;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Glutamate dehydrogenase;
DE            Short=GDH;
DE            EC=1.4.1.3;
GN   Name=gdhA; Synonyms=gdh; OrderedLocusNames=PYRAB05690;
GN   ORFNames=PAB0391;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-255.
RC   STRAIN=GE5 / Orsay;
RA   Borges K.M., Diruggiero J., Robb F.T.;
RT   "Cloning and sequencing of glutamate dehydrogenases from hyperthermophilic
RT   archaea.";
RL   Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ248284; CAB49491.1; -; Genomic_DNA.
DR   EMBL; L19116; AAA64796.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69961.1; -; Genomic_DNA.
DR   PIR; D75176; D75176.
DR   RefSeq; WP_010867693.1; NC_000868.1.
DR   AlphaFoldDB; Q47950; -.
DR   SMR; Q47950; -.
DR   STRING; 272844.PAB0391; -.
DR   GeneID; 1495474; -.
DR   KEGG; pab:PAB0391; -.
DR   PATRIC; fig|272844.11.peg.607; -.
DR   eggNOG; arCOG01352; Archaea.
DR   HOGENOM; CLU_025763_1_2_2; -.
DR   OrthoDB; 6425at2157; -.
DR   PhylomeDB; Q47950; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:RHEA.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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   3: Inferred from homology;
KW   Cytoplasm; NAD; NADP; Oxidoreductase.
FT   CHAIN           1..420
FT                   /note="Glutamate dehydrogenase"
FT                   /id="PRO_0000182755"
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"
SQ   SEQUENCE   420 AA;  47098 MW;  82F8B343572DFE2B CRC64;
     MVEQDPFEIA VKQLERAAQY MKISEEALEF LKRPQRIVEV TIPVEMDDGS VKVFTGFRVQ
     YNWARGPTKG GIRWHPEETL STVKALAAWM TWKTAVMDLP YGGGKGGIIV DPKKLSDREK
     ERLARGYIRA IYDVISPYED IPAPDVYTNP QIMAWMMDEY ETIARRKTPA FGIITGKPLS
     IGGSLGRNEA TARGASYTIR EAAKVLGWDD LKGKTIAIQG YGNAGYYLAK IMSEDYGMKV
     VAVSDSKGGI YNPDGLNADE VLKWKREHGS VKDFPGATNI TNEELLELEV DVLAPAAIEE
     VITKKNADNI KAKIVAEVAN GPVTPEADEI LFEKGILQIP DFLCNAGGVT VSYFEWVQNI
     TGYYWTLEEV REKLDKKMTK AFYDVYNTAK EKNIHMRDAA YVVAVQRVYQ AMLDRGWVKH
//