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Protein

Glutamate dehydrogenase

Gene

gdhA

Organism
Thermococcus profundus
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei105PROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi219 – 225NADSequence analysis7

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BRENDAi1.4.1.3. 6303.

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001827631 – 419Glutamate dehydrogenaseAdd BLAST419

Interactioni

Subunit structurei

Homohexamer.By similarity

Structurei

Secondary structure

1419
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 17Combined sources13
Helixi25 – 32Combined sources8
Beta strandi35 – 45Combined sources11
Beta strandi51 – 62Combined sources12
Beta strandi66 – 74Combined sources9
Helixi80 – 96Combined sources17
Beta strandi102 – 110Combined sources9
Helixi117 – 131Combined sources15
Helixi132 – 134Combined sources3
Turni137 – 139Combined sources3
Beta strandi140 – 143Combined sources4
Helixi150 – 164Combined sources15
Helixi170 – 173Combined sources4
Helixi179 – 181Combined sources3
Helixi190 – 206Combined sources17
Beta strandi214 – 218Combined sources5
Helixi222 – 233Combined sources12
Beta strandi238 – 243Combined sources6
Beta strandi248 – 250Combined sources3
Helixi257 – 267Combined sources11
Beta strandi268 – 270Combined sources3
Beta strandi277 – 279Combined sources3
Helixi281 – 284Combined sources4
Beta strandi290 – 294Combined sources5
Beta strandi296 – 299Combined sources4
Turni303 – 305Combined sources3
Helixi306 – 308Combined sources3
Beta strandi312 – 315Combined sources4
Beta strandi318 – 320Combined sources3
Helixi324 – 332Combined sources9
Beta strandi336 – 338Combined sources3
Helixi340 – 343Combined sources4
Helixi346 – 359Combined sources14
Helixi366 – 391Combined sources26
Helixi395 – 413Combined sources19

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO74024.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

CDDicd01076. NAD_bind_1_Glu_DH. 1 hit.
Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR033524. Glu/Leu/Phe/Val_DH_AS.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
IPR033922. NAD_bind_Glu_DH.
[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]
SUPFAMiSSF51735. SSF51735. 1 hit.
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.
PIRiT44308.

3D structure databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.4.1.3. 6303.

Miscellaneous databases

EvolutionaryTraceiO74024.

Family and domain databases

CDDicd01076. NAD_bind_1_Glu_DH. 1 hit.
Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR033524. Glu/Leu/Phe/Val_DH_AS.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
IPR033922. NAD_bind_Glu_DH.
[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]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 30, 2016
This is version 78 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.