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P80319

- DHE3_PYRFU

UniProt

P80319 - DHE3_PYRFU

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Protein

Glutamate dehydrogenase

Gene

gdhA

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei105 – 1051

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi220 – 2267NADSequence Analysis

GO - Molecular functioni

  1. glutamate dehydrogenase [NAD(P)+] activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular amino acid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

SABIO-RKP80319.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase (EC:1.4.1.3)
Short name:
GDH
Gene namesi
Name:gdhA
Synonyms:gdh
Ordered Locus Names:PF1602
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000001013: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 420420Glutamate dehydrogenasePRO_0000182757Add
BLAST

Proteomic databases

PRIDEiP80319.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

STRINGi186497.PF1602.

Structurei

Secondary structure

1
420
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1712
Helixi18 – 203
Helixi25 – 317
Beta strandi35 – 4511
Beta strandi51 – 6212
Beta strandi66 – 694
Beta strandi72 – 743
Helixi80 – 9617
Beta strandi102 – 1098
Helixi112 – 1143
Helixi117 – 13115
Helixi132 – 1343
Turni137 – 1393
Helixi150 – 16415
Helixi170 – 1734
Helixi179 – 1813
Turni185 – 1895
Helixi190 – 20516
Beta strandi215 – 2195
Helixi223 – 23412
Beta strandi239 – 2446
Beta strandi249 – 2568
Helixi258 – 26811
Beta strandi269 – 2713
Beta strandi277 – 2804
Helixi282 – 2876
Beta strandi291 – 2955
Helixi306 – 3094
Beta strandi313 – 3164
Beta strandi319 – 3213
Helixi325 – 3339
Beta strandi337 – 3393
Helixi341 – 3444
Helixi347 – 36115
Helixi367 – 39125
Helixi396 – 41419

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GTMX-ray2.20A/B/C2-420[»]
ProteinModelPortaliP80319.
SMRiP80319. Positions 5-420.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80319.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0334.
HOGENOMiHOG000243801.
KOiK00261.
OMAiFNFDRAK.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000185. Glu_DH. 1 hit.
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80319-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVEQDPYEIV IKQLERAAQY MEISEEALEF LKRPQRIVEV TIPVEMDDGS
60 70 80 90 100
VKVFTGFRVQ HNWARGPTKG GIRWHPEETL STVKALAAWM TWKTAVMDLP
110 120 130 140 150
YGGGKGGIIV DPKKLSDREK ERLARGYIRA IYDVISPYED IPAPDVYTNP
160 170 180 190 200
QIMAWMMDEY ETISRRKTPA FGIITGKPLS IGGSLGRIEA TARGASYTIR
210 220 230 240 250
EAAKVLGWDT LKGKTIAIQG YGNAGYYLAK IMSEDFGMKV VAVSDSKGGI
260 270 280 290 300
YNPDGLNADE VLKWKNEHGS VKDFPGATNI TNEELLELEV DVLAPAAIEE
310 320 330 340 350
VITKKNADNI KAKIVAEVAN GPVTPEADEI LFEKGILQIP DFLCNAGGVT
360 370 380 390 400
VSYFEWVQNI TGYYWTIEEV RERLDKKMTK AFYDVYNIAK EKNIHMRDAA
410 420
YVVAVQRVYQ AMLDRGWVKH
Length:420
Mass (Da):47,114
Last modified:February 1, 1996 - v2
Checksum:i673DB20F8764A93C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 892AW → WA AA sequence (PubMed:8060497)Curated
Sequence conflicti366 – 3661T → K AA sequence (PubMed:8060497)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M97860 Genomic DNA. Translation: AAA83390.1.
AE009950 Genomic DNA. Translation: AAL81726.1.
PIRiT46971. JN0854.
RefSeqiNP_579331.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL81726; AAL81726; PF1602.
GeneIDi1469478.
KEGGipfu:PF1602.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M97860 Genomic DNA. Translation: AAA83390.1 .
AE009950 Genomic DNA. Translation: AAL81726.1 .
PIRi T46971. JN0854.
RefSeqi NP_579331.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GTM X-ray 2.20 A/B/C 2-420 [» ]
ProteinModelPortali P80319.
SMRi P80319. Positions 5-420.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 186497.PF1602.

Proteomic databases

PRIDEi P80319.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL81726 ; AAL81726 ; PF1602 .
GeneIDi 1469478.
KEGGi pfu:PF1602.

Phylogenomic databases

eggNOGi COG0334.
HOGENOMi HOG000243801.
KOi K00261.
OMAi FNFDRAK.

Enzyme and pathway databases

SABIO-RK P80319.

Miscellaneous databases

EvolutionaryTracei P80319.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000185. Glu_DH. 1 hit.
PRINTSi PR00082. GLFDHDRGNASE.
SMARTi SM00839. ELFV_dehydrog. 1 hit.
[Graphical view ]
PROSITEi PS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The glutamate dehydrogenase-encoding gene of the hyperthermophilic archaeon Pyrococcus furiosus: sequence, transcription and analysis of the deduced amino acid sequence."
    Eggen R.I.L., Geerling A.C.M., Waldkoetter K., Antranikian G., de Vos W.M.
    Gene 132:143-148(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  2. "The amino acid sequence of glutamate dehydrogenase from Pyrococcus furiosus, a hyperthermophilic archaebacterium."
    Maras B., Valiante S., Chiaraluce R., Consalvi V., Politi L., de Rosa M., Bossa F., Scandurra R., Barra D.
    J. Protein Chem. 13:253-259(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  3. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
    Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
    Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  4. "The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures."
    Yip K.S.P., Stillman T.J., Britton K.L., Artymiuk P.J., Baker P.J., Sedelnikova S.E., Engel P.C., Pasquo A., Chiaraluce R., Consalvi V., Scandurra R., Rice D.W.
    Structure 3:1147-1158(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Entry informationi

Entry nameiDHE3_PYRFU
AccessioniPrimary (citable) accession number: P80319
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3