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P82264

- DHE3_CHAAC

UniProt

P82264 - DHE3_CHAAC

Protein

Glutamate dehydrogenase, mitochondrial

Gene

glud1

Organism
Chaenocephalus aceratus (Blackfin icefish) (Chaenichthys aceratus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    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 By similarity.By similarity

    Catalytic activityi

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

    Enzyme regulationi

    Subject to allosteric regulation. Activated by ADP. Inhibited by GTP and ATP By similarity.By similarity

    pH dependencei

    Optimum pH is 8.0.

    Temperature dependencei

    Optimum temperature is 30 degrees Celsius.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei93 – 931SubstrateBy similarity
    Binding sitei117 – 1171SubstrateBy similarity
    Binding sitei122 – 1221NADBy similarity
    Active sitei129 – 1291By similarity
    Binding sitei198 – 1981NADBy similarity
    Binding sitei212 – 2121GTPBy similarity
    Binding sitei216 – 2161GTPBy similarity
    Binding sitei265 – 2651GTPBy similarity
    Binding sitei268 – 2681GTPBy similarity
    Binding sitei384 – 3841SubstrateBy similarity
    Binding sitei390 – 3901NADBy similarity
    Binding sitei396 – 3961ADPBy similarity
    Binding sitei462 – 4621ADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi87 – 893NADBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. glutamate dehydrogenase [NAD(P)+] activity Source: UniProtKB
    3. GTP binding Source: UniProtKB-KW

    GO - Biological processi

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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    ATP-binding, GTP-binding, NAD, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate dehydrogenase, mitochondrial (EC:1.4.1.3)
    Short name:
    GDH
    Gene namesi
    Name:glud1
    Synonyms:glud
    OrganismiChaenocephalus aceratus (Blackfin icefish) (Chaenichthys aceratus)
    Taxonomic identifieri36190 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataPercomorphariaPerciformesNotothenioideiChannichthyidaeChaenocephalus

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 504504Glutamate dehydrogenase, mitochondrialPRO_0000182743Add
    BLAST

    Proteomic databases

    PRIDEiP82264.

    Interactioni

    Subunit structurei

    Homohexamer.

    Structurei

    3D structure databases

    ProteinModelPortaliP82264.
    SMRiP82264. Positions 9-504.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    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.
    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]

    Sequencei

    Sequence statusi: Complete.

    P82264-1 [UniParc]FASTAAdd to Basket

    « Hide

    ADAADKPDDP NFFRMVEGFF DRGASIVEDK LVEDLRTKET PEQKKGRVAG    50
    ILRIIKPCNH VLSLSFPIKR DNGEWEVIEG YRAQHSQHRT PCKGGIRYSM 100
    DVSVDEVKAL ASLMTYKCAV VDVPFGGAKA GVRINTKNYS DNELEKITRR 150
    FTIELAKKGF IGPGIDVPAP DMSTGEREMS WIADTYANTI AHTDINAHAC 200
    VTGKPISQGG IHGRISATGR GVFHGIENFM NEASYMSMVG LTPGVQDKTF 250
    VIQGFGNVGL HSMRYLHRFG AKCVGIGEID GAIYNADGID PKALEEYKLQ 300
    NGTIVGFPGA KPYEGSILEA DCDILIPAAG EKQLTRNNAR RIKAKIIAEG 350
    ANGPTTPDAD KIFLENNVMV IPDMYLNAGG VTVSYFEWLK NLNHVSYGRL 400
    TFKYERDSNY HLLMSVQESL ERKFGKQGGP IPVVPTADFQ ARVAGASEKD 450
    IVHSGLAYTM ERSARQIMRT ASKHNLGLDI RTAAYVNAIE KVFKVYNEAG 500
    LTFT 504
    Length:504
    Mass (Da):55,394
    Last modified:March 1, 2001 - v1
    Checksum:iD8E20681642E3E89
    GO

    Cross-referencesi

    3D structure databases

    ProteinModelPortali P82264.
    SMRi P82264. Positions 9-504.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P82264.

    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.
    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 ]
    ProtoNeti Search...

    Publicationsi

    1. "L-glutamate dehydrogenase from the antarctic fish Chaenocephalus aceratus. Primary structure, function and thermodynamic characterisation: relationship with cold adaptation."
      Ciardiello M.A., Camardella L., Carratore V., di Prisco G.
      Biochim. Biophys. Acta 1543:11-23(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Tissue: Liver.

    Entry informationi

    Entry nameiDHE3_CHAAC
    AccessioniPrimary (citable) accession number: P82264
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 4, 2001
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 71 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    ADP can occupy the NADH binding site and activate the enzyme.By similarity

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3