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P96110

- DHE3_THEMA

UniProt

P96110 - DHE3_THEMA

Protein

Glutamate dehydrogenase

Gene

gdhA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (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

    Temperature dependencei

    Optimum temperature is 75 degrees Celsius. Thermostable.

    Sites

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

    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

    BioCyciRETL1328306-WGS:GSTH-4406-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate dehydrogenase (EC:1.4.1.3)
    Short name:
    GDH
    Gene namesi
    Name:gdhA
    Synonyms:gdh
    Ordered Locus Names:TM_1015
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000008183: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 416415Glutamate dehydrogenasePRO_0000182764Add
    BLAST

    Interactioni

    Subunit structurei

    Homohexamer.

    Protein-protein interaction databases

    STRINGi243274.TM1015.

    Structurei

    Secondary structure

    1
    416
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 2015
    Helixi25 – 328
    Beta strandi35 – 4511
    Beta strandi51 – 6212
    Beta strandi66 – 694
    Beta strandi72 – 776
    Helixi80 – 9718
    Beta strandi103 – 1097
    Helixi112 – 1143
    Helixi117 – 13014
    Helixi132 – 1343
    Turni137 – 1393
    Beta strandi140 – 1434
    Helixi150 – 16415
    Beta strandi171 – 1744
    Helixi177 – 1793
    Turni183 – 1875
    Helixi188 – 20316
    Turni208 – 2103
    Beta strandi212 – 2165
    Helixi220 – 23112
    Beta strandi236 – 2416
    Beta strandi246 – 2483
    Helixi255 – 26410
    Beta strandi265 – 2684
    Beta strandi272 – 2776
    Helixi279 – 2824
    Beta strandi288 – 2925
    Helixi301 – 3044
    Beta strandi310 – 3134
    Beta strandi316 – 3183
    Helixi322 – 3309
    Beta strandi334 – 3363
    Helixi338 – 3414
    Helixi344 – 35714
    Helixi364 – 38926
    Helixi393 – 41119

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B26X-ray3.00A/B/C/D/E/F1-416[»]
    1B3BX-ray3.10A/B/C/D/E/F2-416[»]
    2TMGX-ray2.90A/B/C/D/E/F2-416[»]
    ProteinModelPortaliP96110.
    SMRiP96110. Positions 5-413.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP96110.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0334.
    KOiK00261.
    OMAiTMELCQK.
    OrthoDBiEOG65XN4D.

    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.

    P96110-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPEKSLYEMA VEQFNRAASL MDLESDLAEV LRRPKRVLIV EFPVRMDDGH    50
    VEVFTGYRVQ HNVARGPAKG GIRYHPDVTL DEVKALAFWM TWKTAVMNLP 100
    FGGGKGGVRV DPKKLSRNEL ERLSRRFFSE IQVIIGPYND IPAPDVNTNA 150
    DVMAWYMDTY SMNVGHTVLG IVTGKPVELG GSKGREEATG RGVKVCAGLA 200
    MDVLGIDPKK ATVAVQGFGN VGQFAALLIS QELGSKVVAV SDSRGGIYNP 250
    EGFDVEELIR YKKEHGTVVT YPKGERITNE ELLELDVDIL VPAALEGAIH 300
    AGNAERIKAK AVVEGANGPT TPEADEILSR RGILVVPDIL ANAGGVTVSY 350
    FEWVQDLQSF FWDLDQVRNA LEKMMKGAFN DVMKVKEKYN VDMRTAAYIL 400
    AIDRVAYATK KRGIYP 416
    Length:416
    Mass (Da):45,821
    Last modified:January 23, 2007 - v4
    Checksum:iD7294929879CB4F2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531M → I in CAA71058. (PubMed:9680336)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09925 Genomic DNA. Translation: CAA71058.1.
    AE000512 Genomic DNA. Translation: AAD36092.1.
    PIRiG72305.
    T45284.
    RefSeqiNP_228821.1. NC_000853.1.
    YP_007977367.1. NC_021214.1.
    YP_008991888.1. NC_023151.1.

    Genome annotation databases

    EnsemblBacteriaiAAD36092; AAD36092; TM_1015.
    GeneIDi896847.
    KEGGitma:TM1015.
    tmi:THEMA_09280.
    tmm:Tmari_1018.
    PATRICi23936959. VBITheMar51294_1028.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09925 Genomic DNA. Translation: CAA71058.1 .
    AE000512 Genomic DNA. Translation: AAD36092.1 .
    PIRi G72305.
    T45284.
    RefSeqi NP_228821.1. NC_000853.1.
    YP_007977367.1. NC_021214.1.
    YP_008991888.1. NC_023151.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B26 X-ray 3.00 A/B/C/D/E/F 1-416 [» ]
    1B3B X-ray 3.10 A/B/C/D/E/F 2-416 [» ]
    2TMG X-ray 2.90 A/B/C/D/E/F 2-416 [» ]
    ProteinModelPortali P96110.
    SMRi P96110. Positions 5-413.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243274.TM1015.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD36092 ; AAD36092 ; TM_1015 .
    GeneIDi 896847.
    KEGGi tma:TM1015.
    tmi:THEMA_09280.
    tmm:Tmari_1018.
    PATRICi 23936959. VBITheMar51294_1028.

    Phylogenomic databases

    eggNOGi COG0334.
    KOi K00261.
    OMAi TMELCQK.
    OrthoDBi EOG65XN4D.

    Enzyme and pathway databases

    BioCyci RETL1328306-WGS:GSTH-4406-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P96110.

    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. "Glutamate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: molecular characterization and phylogenetic implications."
      Kort R., Liebl W., Labedan B., Forterre P., Eggen R.I.L., de Vos W.M.
      Extremophiles 1:52-60(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13, CHARACTERIZATION.
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    3. "Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0-A resolution."
      Knapp S., de Vos W.M., Rice D., Ladenstein R.
      J. Mol. Biol. 267:916-932(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    4. "Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. I. Introduction of a six-residue ion-pair network in the hinge region."
      Lebbink J.H., Knapp S., van der Oost J., Rice D., Ladenstein R., de Vos W.M.
      J. Mol. Biol. 280:287-296(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
    5. "Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: construction of a 16-residue ion-pair network at the subunit interface."
      Lebbink J.H., Knapp S., van der Oost J., Rice D., Ladenstein R., de Vos W.M.
      J. Mol. Biol. 289:357-369(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).

    Entry informationi

    Entry nameiDHE3_THEMA
    AccessioniPrimary (citable) accession number: P96110
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 105 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