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O59650

- DHE3_THEKO

UniProt

O59650 - DHE3_THEKO

Protein

Glutamate dehydrogenase

Gene

gdhA

Organism
Thermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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 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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD, NADP

    Enzyme and pathway databases

    BioCyciTKOD69014:GH72-1456-MONOMER.
    SABIO-RKO59650.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate dehydrogenase (EC:1.4.1.3)
    Short name:
    GDH
    Gene namesi
    Name:gdhA
    Ordered Locus Names:TK1431
    OrganismiThermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
    Taxonomic identifieri69014 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
    ProteomesiUP000000536: Chromosome

    Subcellular locationi

    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 – 421420Glutamate dehydrogenasePRO_0000182759Add
    BLAST

    Interactioni

    Subunit structurei

    Homohexamer.

    Protein-protein interaction databases

    STRINGi69014.TK1431.

    Structurei

    3D structure databases

    ProteinModelPortaliO59650.
    SMRiO59650. Positions 3-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0334.
    HOGENOMiHOG000243801.
    KOiK00261.

    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.

    O59650-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVEIDPFEMA VQQLERAAQF MDISEEALEW LKRPMRIVEV SVPVEMDDGS    50
    VKVFTGFRVQ HNWARGPTKG GIRWHPAETL STVKALATWM TWKVAVVDLP 100
    YGGGKGGIIV DPKKLSEREQ ERLARSYIRA VYDVIGPWTD IPAPDVYTNP 150
    KIMAWMMDEY ETIMRRKGPA FGVITGKPPG VGGIVARMDA TARGAAFTIR 200
    EAAKALGWDD LKGKTIAIQG YGNAGYYLHK IMSEEFGMKV VAVSDSKGGI 250
    YNPDGLPPAD EVLKWKKEHG SVKDMPGTQN ITNEELLELE VDILAPSAIE 300
    GVITKENADN VKAKIVAEVA NGPVTPEADE ILHEKGILQI PDFLCNAGGV 350
    TVSYFEWVQN INGFYWTVEE TRKRLDDKMT KAFWDVFNTH KEKNIHMRDA 400
    AYVVAVSRVY EAMKHRGWVK K 421
    Length:421
    Mass (Da):47,056
    Last modified:January 23, 2007 - v4
    Checksum:i13EF3F1DD1602E51
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti138 – 1381W → C in BAA25261. (PubMed:9520268)Curated
    Sequence conflicti347 – 3471A → T in BAA25261. (PubMed:9520268)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89911 Genomic DNA. Translation: BAA25261.1.
    AP006878 Genomic DNA. Translation: BAD85620.1.
    PIRiT44789.
    RefSeqiYP_183844.1. NC_006624.1.

    Genome annotation databases

    EnsemblBacteriaiBAD85620; BAD85620; TK1431.
    GeneIDi3234478.
    KEGGitko:TK1431.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89911 Genomic DNA. Translation: BAA25261.1 .
    AP006878 Genomic DNA. Translation: BAD85620.1 .
    PIRi T44789.
    RefSeqi YP_183844.1. NC_006624.1.

    3D structure databases

    ProteinModelPortali O59650.
    SMRi O59650. Positions 3-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 69014.TK1431.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD85620 ; BAD85620 ; TK1431 .
    GeneIDi 3234478.
    KEGGi tko:TK1431.

    Phylogenomic databases

    eggNOGi COG0334.
    HOGENOMi HOG000243801.
    KOi K00261.

    Enzyme and pathway databases

    BioCyci TKOD69014:GH72-1456-MONOMER.
    SABIO-RK O59650.

    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. "Sequence analysis of glutamate dehydrogenase (GDH) from the hyperthermophilic archaeon Pyrococcus sp. KOD1 and comparison of the enzymatic characteristics of native and recombinant GDHs."
      Rahman R.N.Z.A., Fujiwara S., Takagi M., Imanaka T.
      Mol. Gen. Genet. 257:338-347(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11.
      Strain: ATCC BAA-918 / JCM 12380 / KOD1.
    2. "Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
      Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
      Genome Res. 15:352-363(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-918 / JCM 12380 / KOD1.

    Entry informationi

    Entry nameiDHE3_THEKO
    AccessioniPrimary (citable) accession number: O59650
    Secondary accession number(s): Q5JDK3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 93 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Uses both NAD and NADP.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3