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Q56304

- DHE3_THELN

UniProt

Q56304 - DHE3_THELN

Protein

Glutamate dehydrogenase

Gene

gdhA

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
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 4 (14 May 2014)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    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 – 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

    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

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 419418Glutamate dehydrogenasePRO_0000182762Add
    BLAST

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Structurei

    Secondary structure

    1
    419
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    Experimental Info

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

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 82 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, 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