DHE3_PYRFU
ID DHE3_PYRFU Reviewed; 420 AA.
AC P80319;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Glutamate dehydrogenase;
DE Short=GDH;
DE EC=1.4.1.3;
GN Name=gdhA; Synonyms=gdh; OrderedLocusNames=PF1602;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=8406037; DOI=10.1016/0378-1119(93)90527-a;
RA Eggen R.I.L., Geerling A.C.M., Waldkoetter K., Antranikian G., de Vos W.M.;
RT "The glutamate dehydrogenase-encoding gene of the hyperthermophilic
RT archaeon Pyrococcus furiosus: sequence, transcription and analysis of the
RT deduced amino acid sequence.";
RL Gene 132:143-148(1993).
RN [2]
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=8060497; DOI=10.1007/bf01891983;
RA Maras B., Valiante S., Chiaraluce R., Consalvi V., Politi L., de Rosa M.,
RA Bossa F., Scandurra R., Barra D.;
RT "The amino acid sequence of glutamate dehydrogenase from Pyrococcus
RT furiosus, a hyperthermophilic archaebacterium.";
RL J. Protein Chem. 13:253-259(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=8591026; DOI=10.1016/s0969-2126(01)00251-9;
RA Yip K.S.P., Stillman T.J., Britton K.L., Artymiuk P.J., Baker P.J.,
RA Sedelnikova S.E., Engel P.C., Pasquo A., Chiaraluce R., Consalvi V.,
RA Scandurra R., Rice D.W.;
RT "The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key
RT role for ion-pair networks in maintaining enzyme stability at extreme
RT temperatures.";
RL Structure 3:1147-1158(1995).
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 -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; M97860; AAA83390.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81726.1; -; Genomic_DNA.
DR PIR; T46971; JN0854.
DR RefSeq; WP_011012748.1; NC_018092.1.
DR PDB; 1GTM; X-ray; 2.20 A; A/B/C=2-420.
DR PDBsum; 1GTM; -.
DR AlphaFoldDB; P80319; -.
DR SMR; P80319; -.
DR STRING; 186497.PF1602; -.
DR EnsemblBacteria; AAL81726; AAL81726; PF1602.
DR GeneID; 41713426; -.
DR KEGG; pfu:PF1602; -.
DR PATRIC; fig|186497.12.peg.1668; -.
DR eggNOG; arCOG01352; Archaea.
DR HOGENOM; CLU_025763_1_2_2; -.
DR OMA; WNPRGID; -.
DR OrthoDB; 40988at2157; -.
DR PhylomeDB; P80319; -.
DR BRENDA; 1.4.1.3; 5243.
DR SABIO-RK; P80319; -.
DR EvolutionaryTrace; P80319; -.
DR Proteomes; UP000001013; 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; Reference proteome.
FT CHAIN 1..420
FT /note="Glutamate dehydrogenase"
FT /id="PRO_0000182757"
FT ACT_SITE 105
FT BINDING 220..226
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT CONFLICT 88..89
FT /note="AW -> WA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="T -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:1GTM"
FT STRAND 35..45
FT /evidence="ECO:0007829|PDB:1GTM"
FT STRAND 51..62
FT /evidence="ECO:0007829|PDB:1GTM"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1GTM"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 80..96
FT /evidence="ECO:0007829|PDB:1GTM"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 117..131
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1GTM"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:1GTM"
FT TURN 185..189
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 190..205
FT /evidence="ECO:0007829|PDB:1GTM"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 223..234
FT /evidence="ECO:0007829|PDB:1GTM"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:1GTM"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 258..268
FT /evidence="ECO:0007829|PDB:1GTM"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:1GTM"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 282..287
FT /evidence="ECO:0007829|PDB:1GTM"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 306..309
FT /evidence="ECO:0007829|PDB:1GTM"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:1GTM"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:1GTM"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 347..361
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 367..391
FT /evidence="ECO:0007829|PDB:1GTM"
FT HELIX 396..414
FT /evidence="ECO:0007829|PDB:1GTM"
SQ SEQUENCE 420 AA; 47114 MW; 673DB20F8764A93C CRC64;
MVEQDPYEIV IKQLERAAQY MEISEEALEF LKRPQRIVEV TIPVEMDDGS VKVFTGFRVQ
HNWARGPTKG GIRWHPEETL STVKALAAWM TWKTAVMDLP YGGGKGGIIV DPKKLSDREK
ERLARGYIRA IYDVISPYED IPAPDVYTNP QIMAWMMDEY ETISRRKTPA FGIITGKPLS
IGGSLGRIEA TARGASYTIR EAAKVLGWDT LKGKTIAIQG YGNAGYYLAK IMSEDFGMKV
VAVSDSKGGI YNPDGLNADE VLKWKNEHGS VKDFPGATNI TNEELLELEV DVLAPAAIEE
VITKKNADNI KAKIVAEVAN GPVTPEADEI LFEKGILQIP DFLCNAGGVT VSYFEWVQNI
TGYYWTIEEV RERLDKKMTK AFYDVYNIAK EKNIHMRDAA YVVAVQRVYQ AMLDRGWVKH
