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Q56304

- DHE3_THELN

UniProt

Q56304 - DHE3_THELN

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Protein
Glutamate dehydrogenase
Gene
gdhA, OCC_00135
Organism
Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
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.

pH dependencei

Optimum pH is 8.0.

Temperature dependencei

Optimum temperature is above 95 degrees Celsius.

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi219 – 2257NAD Reviewed prediction

GO - Molecular functioni

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

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
ORF Names:OCC_00135
OrganismiThermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
Taxonomic identifieri523849 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
ProteomesiUP000015502: Chromosome

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 419418Glutamate dehydrogenase
PRO_0000182762Add
BLAST

Interactioni

Subunit structurei

Homohexamer.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1814
Helixi25 – 306
Beta strandi35 – 4511
Beta strandi51 – 6212
Beta strandi66 – 694
Beta strandi72 – 754
Helixi80 – 9718
Beta strandi102 – 1109
Helixi112 – 1143
Helixi117 – 13115
Helixi132 – 1343
Turni137 – 1393
Helixi150 – 16415
Helixi170 – 1734
Beta strandi174 – 1763
Helixi179 – 1813
Helixi190 – 20516
Beta strandi214 – 2185
Helixi222 – 23514
Beta strandi238 – 2436
Beta strandi248 – 2503
Helixi257 – 26711
Beta strandi268 – 2703
Beta strandi277 – 2793
Helixi281 – 2866
Beta strandi290 – 2945
Helixi303 – 3064
Beta strandi312 – 3154
Beta strandi318 – 3203
Helixi324 – 33310
Beta strandi336 – 3383
Helixi340 – 3434
Helixi346 – 36015
Helixi366 – 39126
Helixi395 – 41420

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BVUX-ray2.50A/B/C/D/E/F2-419[»]
ProteinModelPortaliQ56304.

Miscellaneous databases

EvolutionaryTraceiQ56304.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q56304-1 [UniParc]FASTAAdd to Basket

« Hide

MVEQDPFEIA VKQLERAAQY MDISEEALEF LKRPQRIVEV SIPVEMDDGS    50
VKVFTGFRVQ YNWARGPTKG GIRWHPEETL STVKALAAWM TWKTAVMDLP 100
YGGGKGGVIC NPKEMSDREK ERLARGYVRA IYDVISPYTD IPAPDVYTNP 150
QIMAWMMDEY ETISRRKDPS FGVITGKPPS VGGIVARMDA TARGASYTVR 200
EAAKALGMDL KGKTIAIQGY GNAGYYMAKI MSEEYGMKVV AVSDSKGGIY 250
NPDGLNADEV LAWKKKTGSV KDFPGATNIT NEELLELEVD VLAPSAIEEV 300
ITKKNADNIK AKIVAELANG PTTPEADEIL YEKGILIIPD FLCNAGGVTV 350
SYFEWVQNIT GDYWTVEETR AKLDKKMTKA FWDVYNTHKE KNINMRDAAY 400
VVAVSRVYQA MKDRGWIKK 419
Length:419
Mass (Da):46,726
Last modified:May 14, 2014 - v4
Checksum:iF53A237F0C5B7215
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti245 – 2451S → T in AAA72393. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L19995 Genomic DNA. Translation: AAA72393.1.
CP006670 Genomic DNA. Translation: EHR77478.1.
RefSeqiWP_004070133.1. NC_022084.1.
YP_008430491.1. NC_022084.1.

Genome annotation databases

GeneIDi16550867.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L19995 Genomic DNA. Translation: AAA72393.1 .
CP006670 Genomic DNA. Translation: EHR77478.1 .
RefSeqi WP_004070133.1. NC_022084.1.
YP_008430491.1. NC_022084.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BVU X-ray 2.50 A/B/C/D/E/F 2-419 [» ]
ProteinModelPortali Q56304.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 16550867.

Miscellaneous databases

EvolutionaryTracei Q56304.

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. "Cloning and sequencing of glutamate dehydrogenases from hyperthermophilic archaea."
    Borges K.M., Diruggiero J., Robb F.T.
    Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Genome sequence of the model hyperthermophilic archaeon Thermococcus litoralis NS-C."
    Gardner A.F., Kumar S., Perler F.B.
    J. Bacteriol. 194:2375-2376(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51850 / DSM 5473 / JCM 8560 / NS-C.
  3. "Purification and characterization of NADP-specific alcohol dehydrogenase and glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis."
    Ma K., Robb F.T., Adams M.W.W.
    Appl. Environ. Microbiol. 60:562-568(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21, SUBCELLULAR LOCATION.
    Strain: ATCC 51850 / DSM 5473 / JCM 8560 / NS-C.
  4. "Structure determination of the glutamate dehydrogenase from the hyperthermophile Thermococcus litoralis and its comparison with that from Pyrococcus furiosus."
    Britton K.L., Yip K.S.P., Sedelnikova S.E., Stillman T.J., Adams M.W.W., Ma K., Maeder D.L., Robb F.T., Tolliday N., Vetriani C., Rice D.W., Baker P.J.
    J. Mol. Biol. 293:1121-1132(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Entry informationi

Entry nameiDHE3_THELN
AccessioniPrimary (citable) accession number: Q56304
Secondary accession number(s): H3ZRF0, Q9UWK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 14, 2014
Last modified: September 3, 2014
This is version 81 of the entry and version 4 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

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

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