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P42174

- DHE3_PIG

UniProt

P42174 - DHE3_PIG

Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

GLUD1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Mitochondrial glutamate dehydrogenase that converts L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate By similarity.By similarity

    Catalytic activityi

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

    GO - Molecular functioni

    1. glutamate dehydrogenase [NAD(P)+] activity Source: UniProtKB

    GO - Biological processi

    1. glutamine metabolic process Source: UniProtKB
    2. tricarboxylic acid metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate dehydrogenase 1, mitochondrial (EC:1.4.1.3)
    Short name:
    GDH 1
    Alternative name(s):
    Membrane protein 50
    Short name:
    MP50
    Gene namesi
    Name:GLUD1
    Synonyms:GLUD
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›33›33Glutamate dehydrogenase 1, mitochondrialPRO_0000182741Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei15 – 151N6-succinyllysineBy similarity

    Post-translational modificationi

    ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity. Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer By similarity.By similarity

    Keywords - PTMi

    ADP-ribosylation

    Proteomic databases

    PaxDbiP42174.

    Expressioni

    Tissue specificityi

    Liver, brain and thyroid.

    Interactioni

    Subunit structurei

    Homohexamer.By similarity

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000011056.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0334.

    Sequencei

    Sequence statusi: Fragments.

    P42174-1 [UniParc]FASTAAdd to Basket

    « Hide

    SEAAADREDD PNFFKMVEGF GSILEADXDI LIP                     33
    Length:33
    Mass (Da):3,624
    Last modified:November 1, 1995 - v1
    Checksum:i63B6C5C3C479F4DD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-adjacent residuesi20 – 212Curated
    Non-terminal residuei33 – 331

    Sequence databases

    PIRiS39010.

    Cross-referencesi

    Sequence databases

    PIRi S39010.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000011056.

    Proteomic databases

    PaxDbi P42174.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0334.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "A membrane-bound form of glutamate dehydrogenase possesses an ATP-dependent high-affinity microtubule-binding activity."
      Rajas F., Rousset B.
      Biochem. J. 295:447-455(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.

    Entry informationi

    Entry nameiDHE3_PIG
    AccessioniPrimary (citable) accession number: P42174
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 63 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3