DHE3_THEPR
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 03-AUG-2022, entry version 92.
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 coli
RT of hyperthermophilic glutamate dehydrogenase gene from Thermococcus
RT profundus.";
RL J. Ferment. Bioeng. 83:405-411(1997).
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 -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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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 PDB; 6JN9; EM; 3.80 A; A=1-419.
DR PDB; 6JNA; EM; 3.80 A; A=1-419.
DR PDB; 6JNC; EM; 3.70 A; A=1-419.
DR PDB; 6JND; EM; 3.90 A; A=1-419.
DR PDBsum; 1EUZ; -.
DR PDBsum; 6JN9; -.
DR PDBsum; 6JNA; -.
DR PDBsum; 6JNC; -.
DR PDBsum; 6JND; -.
DR AlphaFoldDB; O74024; -.
DR SMR; O74024; -.
DR BRENDA; 1.4.1.3; 6303.
DR EvolutionaryTrace; O74024; -.
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:cellular amino acid metabolic process; IEA:InterPro.
DR CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR InterPro; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; NADP; Oxidoreductase.
FT CHAIN 1..419
FT /note="Glutamate dehydrogenase"
FT /id="PRO_0000182763"
FT ACT_SITE 105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT BINDING 219..225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:1EUZ"
FT STRAND 35..45
FT /evidence="ECO:0007829|PDB:1EUZ"
FT STRAND 51..62
FT /evidence="ECO:0007829|PDB:1EUZ"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 80..96
FT /evidence="ECO:0007829|PDB:1EUZ"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 117..131
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1EUZ"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1EUZ"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 190..206
FT /evidence="ECO:0007829|PDB:1EUZ"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:1EUZ"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:1EUZ"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:1EUZ"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:1EUZ"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:1EUZ"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:1EUZ"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:1EUZ"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:1EUZ"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:1EUZ"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 324..332
FT /evidence="ECO:0007829|PDB:1EUZ"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 346..359
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 366..391
FT /evidence="ECO:0007829|PDB:1EUZ"
FT HELIX 395..413
FT /evidence="ECO:0007829|PDB:1EUZ"
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
