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O74024

- DHE3_THEPR

UniProt

O74024 - DHE3_THEPR

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Protein

Glutamate dehydrogenase

Gene

gdhA

Organism
Thermococcus profundus
Status
Reviewed - Annotation score: 2 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 – 1051PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi219 – 2257NADSequence 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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase (EC:1.4.1.3)
Short name:
GDH
Gene namesi
Name:gdhA
Synonyms:gdh
OrganismiThermococcus profundus
Taxonomic identifieri49899 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 419419Glutamate dehydrogenasePRO_0000182763Add
BLAST

Interactioni

Subunit structurei

Homohexamer.By similarity

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1713Combined sources
Helixi25 – 328Combined sources
Beta strandi35 – 4511Combined sources
Beta strandi51 – 6212Combined sources
Beta strandi66 – 749Combined sources
Helixi80 – 9617Combined sources
Beta strandi102 – 1109Combined sources
Helixi117 – 13115Combined sources
Helixi132 – 1343Combined sources
Turni137 – 1393Combined sources
Beta strandi140 – 1434Combined sources
Helixi150 – 16415Combined sources
Helixi170 – 1734Combined sources
Helixi179 – 1813Combined sources
Helixi190 – 20617Combined sources
Beta strandi214 – 2185Combined sources
Helixi222 – 23312Combined sources
Beta strandi238 – 2436Combined sources
Beta strandi248 – 2503Combined sources
Helixi257 – 26711Combined sources
Beta strandi268 – 2703Combined sources
Beta strandi277 – 2793Combined sources
Helixi281 – 2844Combined sources
Beta strandi290 – 2945Combined sources
Beta strandi296 – 2994Combined sources
Turni303 – 3053Combined sources
Helixi306 – 3083Combined sources
Beta strandi312 – 3154Combined sources
Beta strandi318 – 3203Combined sources
Helixi324 – 3329Combined sources
Beta strandi336 – 3383Combined sources
Helixi340 – 3434Combined sources
Helixi346 – 35914Combined sources
Helixi366 – 39126Combined sources
Helixi395 – 41319Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EUZX-ray2.25A/B/C/D/E/F1-419[»]
ProteinModelPortaliO74024.
SMRiO74024. Positions 3-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO74024.

Family & Domainsi

Sequence similaritiesi

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.

O74024-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVEIDPFEMA VKQLERAAQY MDISEEALEW LKKPMRIVEV SVPIEMDDGS
60 70 80 90 100
VKVFTGFRVQ HNWARGPTKG GIRWHPAETL STVKALATWM TWKVAVVDLP
110 120 130 140 150
YGGGKGGIIV NPKELSEREQ ERLARAYIRA VYDVIGPWTD IPAPDVYTNP
160 170 180 190 200
KIMGWMMDEY ETIMRRKGPA FGVITGKPLS IGGSLGRGTA TAQGAIFTIR
210 220 230 240 250
EAAKALGIDL KGKKIAVQGY GNAGYYTAKL AKEQLGMTVV AVSDSRGGIY
260 270 280 290 300
NPDGLDPDEV LKWKREHGSV KDFPGATNIT NEELLELEVD VLAPAAIEEV
310 320 330 340 350
ITEKNADNIK AKIVAEVANG PVTPEADDIL REKGILQIPD FLCNAGGVTV
360 370 380 390 400
SYFEWVQNIN GYYWTEEEVR EKLDKKMTKA FWEVYNTHKD KNIHMRDAAY
410
VVAVSRVYQA MKDRGWVKK
Length:419
Mass (Da):46,700
Last modified:November 1, 1998 - v1
Checksum:i1DF3C1122E562706
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87814 Genomic DNA. Translation: BAA28943.1.
PIRiT44308.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87814 Genomic DNA. Translation: BAA28943.1 .
PIRi T44308.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EUZ X-ray 2.25 A/B/C/D/E/F 1-419 [» ]
ProteinModelPortali O74024.
SMRi O74024. Positions 3-419.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei O74024.

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

  1. "Molecular cloning, nucleotide sequence and expression in Escherichia coli of hyperthermophilic glutamate dehydrogenase gene from Thermococcus profundus."
    Higuchi S., Kobayashi T., Kimura K., Horikoshi K., Kudo T.
    J. Ferment. Bioeng. 83:405-411(1997)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiDHE3_THEPR
AccessioniPrimary (citable) accession number: O74024
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: November 26, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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