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Q54KB7

- DHE3_DICDI

UniProt

Q54KB7 - DHE3_DICDI

Protein

Glutamate dehydrogenase, mitochondrial

Gene

gluD

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Enzyme regulationi

    Subject to allosteric regulation. Activated by AMP and ADP.2 Publications

    Kineticsi

    1. KM=0.36 mM for alpha-ketoglutarate1 Publication
    2. KM=16 µM for NADH1 Publication
    3. KM=34.5 mM for NH31 Publication

    pH dependencei

    Optimum pH is 7.25 to 7.5.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei102 – 1021SubstrateBy similarity
    Binding sitei126 – 1261SubstrateBy similarity
    Binding sitei131 – 1311NADBy similarity
    Active sitei138 – 1381PROSITE-ProRule annotation
    Binding sitei394 – 3941SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi96 – 983NADBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. glutamate catabolic process Source: dictyBase

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    ATP-binding, NAD, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKQ54KB7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate dehydrogenase, mitochondrial (EC:1.4.1.3)
    Short name:
    GDH
    Gene namesi
    Name:gluD
    ORF Names:DDB_G0287469
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 5, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0287469. glud1.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: dictyBase
    3. phagocytic vesicle Source: dictyBase

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 502Glutamate dehydrogenase, mitochondrialPRO_0000327666
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Proteomic databases

    PRIDEiQ54KB7.

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Protein-protein interaction databases

    STRINGi44689.DDB_0231438.

    Structurei

    3D structure databases

    ProteinModelPortaliQ54KB7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0334.
    KOiK00261.
    OMAiTMELCQK.
    PhylomeDBiQ54KB7.

    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.

    Q54KB7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQSLARLSRT SLVQKGLVPQ TIKNYSSVSQ AEIDNEPRFL ECFKTFFDKA    50
    AGLTNLKPGV LNNMKECNVA LRVEFPIKNE HGDVDIIAGY RAQHSHHRLP 100
    CKGGIRFSEE VDLQEVMALA SLMTYKCAVV DVPFGGAKGG VRIDPKKYTV 150
    AQREKITRAY TLLLCQKNFI GPGVDVPAPD MGTGEQEMAW IRDTYQAFNT 200
    NDVDSMACVT GKPISSGGIR GRTEATGLGV FYGIREFLSY EEVLKKTGLT 250
    PGIKGKSIVI QGFGNVGYFA AKFFEQAGAK VIAVAEHNGA VYNADGLNID 300
    ALNKYKLQHG TFIDFPGATN IVDSVKALEI PCDILIPAAL EKQIHIGNVA 350
    DIQAKLIGEA ANGPMTPRAD QILLNRGHVI IPDLLLNAGG VTVSYFEWLK 400
    NLSHVRFGRL NKKWEESSKK LLLEFVESTV NKKLSEAERS LIIHGADEID 450
    IVRSGLEDTM QNACAETRKT ANEKNTDYRS AALYNAIMKI KAVYESSGNV 500
    FS 502
    Length:502
    Mass (Da):55,042
    Last modified:May 24, 2005 - v1
    Checksum:iD6BB324A859C0528
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000101 Genomic DNA. Translation: EAL63700.1.
    RefSeqiXP_637204.1. XM_632112.1.

    Genome annotation databases

    EnsemblProtistsiDDB0231438; DDB0231438; DDB_G0287469.
    GeneIDi8626141.
    KEGGiddi:DDB_G0287469.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000101 Genomic DNA. Translation: EAL63700.1 .
    RefSeqi XP_637204.1. XM_632112.1.

    3D structure databases

    ProteinModelPortali Q54KB7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDB_0231438.

    Proteomic databases

    PRIDEi Q54KB7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0231438 ; DDB0231438 ; DDB_G0287469 .
    GeneIDi 8626141.
    KEGGi ddi:DDB_G0287469.

    Organism-specific databases

    dictyBasei DDB_G0287469. glud1.

    Phylogenomic databases

    eggNOGi COG0334.
    KOi K00261.
    OMAi TMELCQK.
    PhylomeDBi Q54KB7.

    Enzyme and pathway databases

    SABIO-RK Q54KB7.

    Miscellaneous databases

    PROi Q54KB7.

    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. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    2. "The NAD-dependent glutamate dehydrogenase from Dictyostelium discoideum: purification and properties."
      Pamula F., Wheldrake J.F.
      Arch. Biochem. Biophys. 291:225-230(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    3. "The effect of AMP on the NAD-dependent glutamate dehydrogenase during activation and morphogenesis in the cellular slime moulds."
      Pamula F., Wheldrake J.F.
      J. Gen. Microbiol. 138:1935-1940(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.

    Entry informationi

    Entry nameiDHE3_DICDI
    AccessioniPrimary (citable) accession number: Q54KB7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3