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Q64HZ9

- DHE4_HYLLA

UniProt

Q64HZ9 - DHE4_HYLLA

Protein

Glutamate dehydrogenase 2, mitochondrial

Gene

GLUD2

Organism
Hylobates lar (Common gibbon) (White-handed gibbon)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (25 Oct 2004)
      Previous versions | rss
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    Functioni

    Important for recycling the chief excitatory neurotransmitter, glutamate, during neurotransmission.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei81 – 811SubstrateBy similarity
    Active sitei180 – 1801PROSITE-ProRule annotation

    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

    NADP

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate dehydrogenase 2, mitochondrial (EC:1.4.1.3)
    Short name:
    GDH 2
    Gene namesi
    Name:GLUD2
    OrganismiHylobates lar (Common gibbon) (White-handed gibbon)
    Taxonomic identifieri9580 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHylobatidaeHylobates

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5050MitochondrionBy similarityAdd
    BLAST
    Chaini51 – 555505Glutamate dehydrogenase 2, mitochondrialPRO_0000007209Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei65 – 651N6-succinyllysineBy similarity
    Modified residuei76 – 761PhosphoserineBy similarity
    Modified residuei81 – 811N6-acetyllysine; alternateBy similarity
    Modified residuei81 – 811N6-succinyllysine; alternateBy similarity
    Modified residuei107 – 1071N6-acetyllysine; alternateBy similarity
    Modified residuei107 – 1071N6-succinyllysine; alternateBy similarity
    Modified residuei125 – 1251PhosphoserineBy similarity
    Modified residuei132 – 1321PhosphotyrosineBy similarity
    Modified residuei159 – 1591N6-acetyllysine; alternateBy similarity
    Modified residuei159 – 1591N6-succinyllysine; alternateBy similarity
    Modified residuei168 – 1681N6-acetyllysineBy similarity
    Modified residuei169 – 1691ADP-ribosylcysteineBy similarity
    Modified residuei180 – 1801N6-acetyllysine; alternateBy similarity
    Modified residuei180 – 1801N6-succinyllysine; alternateBy similarity
    Modified residuei184 – 1841N6-acetyllysineBy similarity
    Modified residuei188 – 1881N6-acetyllysine; alternateBy similarity
    Modified residuei188 – 1881N6-succinyllysine; alternateBy similarity
    Modified residuei197 – 1971N6-succinyllysineBy similarity
    Modified residuei208 – 2081N6-acetyllysineBy similarity
    Modified residuei323 – 3231N6-acetyllysineBy similarity
    Modified residuei343 – 3431N6-acetyllysine; alternateBy similarity
    Modified residuei343 – 3431N6-succinyllysine; alternateBy similarity
    Modified residuei349 – 3491N6-acetyllysine; alternateBy similarity
    Modified residuei349 – 3491N6-succinyllysine; alternateBy similarity
    Modified residuei360 – 3601N6-acetyllysine; alternateBy similarity
    Modified residuei360 – 3601N6-succinyllysine; alternateBy similarity
    Modified residuei362 – 3621N6-acetyllysine; alternateBy similarity
    Modified residuei362 – 3621N6-succinyllysine; alternateBy similarity
    Modified residuei383 – 3831N6-acetyllysineBy similarity
    Modified residuei387 – 3871N6-acetyllysine; alternateBy similarity
    Modified residuei387 – 3871N6-succinyllysine; alternateBy similarity
    Modified residuei396 – 3961N6-acetyllysineBy similarity
    Modified residuei412 – 4121N6-acetyllysine; alternateBy similarity
    Modified residuei412 – 4121N6-succinyllysine; alternateBy similarity
    Modified residuei454 – 4541N6-acetyllysine; alternateBy similarity
    Modified residuei454 – 4541N6-succinyllysine; alternateBy similarity
    Modified residuei474 – 4741N6-acetyllysine; alternateBy similarity
    Modified residuei474 – 4741N6-succinyllysine; alternateBy similarity
    Modified residuei477 – 4771N6-acetyllysine; alternateBy similarity
    Modified residuei477 – 4771N6-succinyllysine; alternateBy similarity
    Modified residuei500 – 5001N6-acetyllysine; alternateBy similarity
    Modified residuei500 – 5001N6-succinyllysine; alternateBy similarity
    Modified residuei524 – 5241N6-acetyllysine; alternateBy similarity
    Modified residuei524 – 5241N6-succinyllysine; alternateBy similarity
    Modified residuei542 – 5421N6-acetyllysine; alternateBy similarity
    Modified residuei542 – 5421N6-succinyllysine; alternateBy similarity
    Modified residuei545 – 5451N6-acetyllysineBy similarity

    Post-translational modificationi

    Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer.By similarity

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Phosphoprotein

    Proteomic databases

    PRIDEiQ64HZ9.

    Interactioni

    Subunit structurei

    Homohexamer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ64HZ9.
    SMRiQ64HZ9. Positions 60-555.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    HOVERGENiHBG005479.

    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.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00208. ELFV_dehydrog. 1 hit.
    PF02812. ELFV_dehydrog_N. 1 hit.
    [Graphical view]
    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.

    Q64HZ9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYCYLGKALL PSGAGPAALG SAGAALLGRA RGQPAAAPQP GLALAAWRHY    50
    SEVVADRKDD PNFFKMVEGF FDRGASIVED KLVKDLRTRE SEEQKRNRVR 100
    GILRIIKPCN HVLSLSFPIR RDDGSWEVIE GYRAQHSQHR TPCKGGIRYS 150
    ADVSVDEVKA LASLMTYKCA VVDVPFGGAK AGVKINPKNY TENELEKITR 200
    RFTMELAKKG FIGPGIDVPA PDMNTGEREM SWIADTYAST IGHYDINAHA 250
    CVTGKPISQG GIHGRISATG RGVFHGIENF INEASYMSIL GMTPGFGDKT 300
    FVVQGFGNVG LHSMRYLHRF GAKCIAVGES DGSIWNPDGI DPKELEDFKL 350
    QHGSILGFPK AKPYEGSILE ADCDILIPAA SEKQLTKSNA PRVKAKIIAE 400
    GANGPTTPEA DKIFLERNIM VIPDLYVNAG GVTVSYFEWL KNLNHVSYGR 450
    LTFKYERDSN YHLLMSVQES LERKFGKHGG TIPIVPTAEF QDSISGASEK 500
    DIVHSALAYT MERSARQIMR TAMKYNLGLD LRTAAYVNAI EKVFKVYSEA 550
    GVTFT 555
    Length:555
    Mass (Da):60,866
    Last modified:October 25, 2004 - v1
    Checksum:i36BF0E321F993A53
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY588269 Genomic DNA. Translation: AAU03135.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY588269 Genomic DNA. Translation: AAU03135.1 .

    3D structure databases

    ProteinModelPortali Q64HZ9.
    SMRi Q64HZ9. Positions 60-555.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q64HZ9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG005479.

    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.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00208. ELFV_dehydrog. 1 hit.
    PF02812. ELFV_dehydrog_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00082. GLFDHDRGNASE.
    SMARTi SM00839. ELFV_dehydrog. 1 hit.
    [Graphical view ]
    PROSITEi PS00074. GLFV_DEHYDROGENASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Birth and adaptive evolution of a hominoid gene that supports high neurotransmitter flux."
      Burki F., Kaessmann H.
      Nat. Genet. 36:1061-1063(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiDHE4_HYLLA
    AccessioniPrimary (citable) accession number: Q64HZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: October 25, 2004
    Last modified: October 1, 2014
    This is version 55 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3