DHE3_THELN
ID DHE3_THELN Reviewed; 419 AA.
AC Q56304; H3ZRF0; Q9UWK7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 4.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Glutamate dehydrogenase;
DE Short=GDH;
DE EC=1.4.1.3;
GN Name=gdhA; ORFNames=OCC_00135;
OS Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523849;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=22493191; DOI=10.1128/jb.00123-12;
RA Gardner A.F., Kumar S., Perler F.B.;
RT "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT litoralis NS-C.";
RL J. Bacteriol. 194:2375-2376(2012).
RN [3]
RP PROTEIN SEQUENCE OF 2-21, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=8135516; DOI=10.1128/aem.60.2.562-568.1994;
RA Ma K., Robb F.T., Adams M.W.W.;
RT "Purification and characterization of NADP-specific alcohol dehydrogenase
RT and glutamate dehydrogenase from the hyperthermophilic archaeon
RT Thermococcus litoralis.";
RL Appl. Environ. Microbiol. 60:562-568(1994).
RN [4]
RP SUBUNIT, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=10547290; DOI=10.1006/jmbi.1999.3205;
RA Britton K.L., Yip K.S.P., Sedelnikova S.E., Stillman T.J., Adams M.W.W.,
RA Ma K., Maeder D.L., Robb F.T., Tolliday N., Vetriani C., Rice D.W.,
RA Baker P.J.;
RT "Structure determination of the glutamate dehydrogenase from the
RT hyperthermophile Thermococcus litoralis and its comparison with that from
RT Pyrococcus furiosus.";
RL J. Mol. Biol. 293:1121-1132(1999).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0.;
CC Temperature dependence:
CC Optimum temperature is above 95 degrees Celsius.;
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:10547290}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8135516}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; L19995; AAA72393.1; -; Genomic_DNA.
DR EMBL; CP006670; EHR77478.1; -; Genomic_DNA.
DR RefSeq; WP_004070133.1; NC_022084.1.
DR PDB; 1BVU; X-ray; 2.50 A; A/B/C/D/E/F=2-419.
DR PDBsum; 1BVU; -.
DR AlphaFoldDB; Q56304; -.
DR SMR; Q56304; -.
DR STRING; 523849.OCC_00135; -.
DR EnsemblBacteria; EHR77478; EHR77478; OCC_00135.
DR GeneID; 16550867; -.
DR KEGG; tlt:OCC_00135; -.
DR HOGENOM; CLU_025763_1_2_2; -.
DR OMA; PCFAAFP; -.
DR OrthoDB; 40988at2157; -.
DR BRENDA; 1.4.1.3; 6302.
DR BRENDA; 1.4.1.4; 6302.
DR EvolutionaryTrace; Q56304; -.
DR Proteomes; UP000015502; 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: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; Cytoplasm; Direct protein sequencing; NAD; NADP;
KW Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8135516"
FT CHAIN 2..419
FT /note="Glutamate dehydrogenase"
FT /id="PRO_0000182762"
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 CONFLICT 245
FT /note="S -> T (in Ref. 1; AAA72393)"
FT /evidence="ECO:0000305"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 25..30
FT /evidence="ECO:0007829|PDB:1BVU"
FT STRAND 35..45
FT /evidence="ECO:0007829|PDB:1BVU"
FT STRAND 51..62
FT /evidence="ECO:0007829|PDB:1BVU"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1BVU"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 80..97
FT /evidence="ECO:0007829|PDB:1BVU"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 117..131
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1BVU"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1BVU"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 190..205
FT /evidence="ECO:0007829|PDB:1BVU"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:1BVU"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:1BVU"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:1BVU"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:1BVU"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:1BVU"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:1BVU"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:1BVU"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 324..333
FT /evidence="ECO:0007829|PDB:1BVU"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 346..360
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 366..391
FT /evidence="ECO:0007829|PDB:1BVU"
FT HELIX 395..414
FT /evidence="ECO:0007829|PDB:1BVU"
SQ SEQUENCE 419 AA; 46726 MW; F53A237F0C5B7215 CRC64;
MVEQDPFEIA VKQLERAAQY MDISEEALEF LKRPQRIVEV SIPVEMDDGS VKVFTGFRVQ
YNWARGPTKG GIRWHPEETL STVKALAAWM TWKTAVMDLP YGGGKGGVIC NPKEMSDREK
ERLARGYVRA IYDVISPYTD IPAPDVYTNP QIMAWMMDEY ETISRRKDPS FGVITGKPPS
VGGIVARMDA TARGASYTVR EAAKALGMDL KGKTIAIQGY GNAGYYMAKI MSEEYGMKVV
AVSDSKGGIY NPDGLNADEV LAWKKKTGSV KDFPGATNIT NEELLELEVD VLAPSAIEEV
ITKKNADNIK AKIVAELANG PTTPEADEIL YEKGILIIPD FLCNAGGVTV SYFEWVQNIT
GDYWTVEETR AKLDKKMTKA FWDVYNTHKE KNINMRDAAY VVAVSRVYQA MKDRGWIKK
