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P54385

- DHE3_DROME

UniProt

P54385 - DHE3_DROME

Protein

Glutamate dehydrogenase, mitochondrial

Gene

Gdh

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      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 ADP. Inhibited by GTP and ATP By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei138 – 1381SubstrateBy similarity
    Binding sitei162 – 1621SubstrateBy similarity
    Binding sitei167 – 1671NADBy similarity
    Active sitei174 – 1741PROSITE-ProRule annotation
    Binding sitei243 – 2431NADBy similarity
    Binding sitei257 – 2571GTPBy similarity
    Binding sitei261 – 2611GTPBy similarity
    Binding sitei310 – 3101GTPBy similarity
    Binding sitei313 – 3131GTPBy similarity
    Binding sitei430 – 4301SubstrateBy similarity
    Binding sitei436 – 4361NADBy similarity
    Binding sitei442 – 4421ADPBy similarity
    Binding sitei521 – 5211ADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi132 – 1343NADBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. glutamate metabolic process Source: FlyBase
    2. NADH oxidation Source: FlyBase

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_216833. Amino acid synthesis and interconversion (transamination).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate dehydrogenase, mitochondrial (EC:1.4.1.3)
    Short name:
    GDH
    Gene namesi
    Name:Gdh
    Synonyms:Glud
    ORF Names:CG5320
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0001098. Gdh.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: FlyBase

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5353MitochondrionSequence AnalysisAdd
    BLAST
    Chaini54 – 562509Glutamate dehydrogenase, mitochondrialPRO_0000007214Add
    BLAST

    Proteomic databases

    PaxDbiP54385.
    PRIDEiP54385.

    Expressioni

    Tissue specificityi

    Expressed throughout the embryo during early stages before becoming localized in mesodermal tissue by stage 8. At stage 12 expression is concentrated in the posterior midgut. After stage 13 expression it is found in the anterior and posterior midgut, the hindgut, fat body, muscle, and central nervous system. In 3rd instar larvae expression is found in the leg disks, the wing pouch of the wing disk, the eye-antenna disk, and the developing brain medulla.1 Publication

    Developmental stagei

    Expressed at all stages.1 Publication

    Gene expression databases

    BgeeiP54385.

    Interactioni

    Subunit structurei

    Homohexamer.

    Protein-protein interaction databases

    BioGridi67768. 22 interactions.
    IntActiP54385. 1 interaction.
    MINTiMINT-747345.

    Structurei

    3D structure databases

    ProteinModelPortaliP54385.
    SMRiP54385. Positions 54-562.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0334.
    GeneTreeiENSGT00390000000854.
    InParanoidiP54385.
    KOiK00261.
    OMAiTCIGVIE.
    OrthoDBiEOG73NG50.
    PhylomeDBiP54385.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: P54385-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MYHLKSLARQ GARRQQELAT LAKALPTAVM QSSRGYATEH QIPDRLKDVP    50
    TAKDPRFFDM VEYFFHRGCQ IAEESLVDDM KGKLTRDEKK QKVKGILMLM 100
    QPCDHIIEIA FPLRRDAGNY EMITGYRAQH STHKTPTKGG IRFSLDVSRD 150
    EVKALSALMT FKCACVDVPF GGAKAGLKIN PKEYSEHELE KITRRFTLEL 200
    AKKGFIGPGV DVPAPDMGTG EREMSWIADT YAKTIGHLDI NAHACVTGKP 250
    INQGGIHGRV SATGRGVFHG LENFINEANY MSQIGTTPGW GGKTFIVQGF 300
    GNVGLHTTRY LTRAGATCIG VIEHDGTLYN PEGIDPKLLE DYKNEHGTIV 350
    GYQNAKPYEG ENLMFEKCDI FIPAAVEKVI TSENANRIQA KIIAEAANGP 400
    TTPAADKILI DRNILVIPDL YINAGGVTVS FFEWLKNLNH VSYGRLTFKY 450
    ERESNYHLLA SVQQSIERII NDESVQESLE RRFGRVGGRI PVTPSESFQK 500
    RISGASEKDI VHSGLDYTME RSARAIMKTA MKYNLGLDLR TAAYVNSIEK 550
    IFTTYRDAGL AF 562
    Length:562
    Mass (Da):62,536
    Last modified:December 1, 2000 - v2
    Checksum:i687A183D3BC0211F
    GO
    Isoform C (identifier: P54385-2) [UniParc]FASTAAdd to Basket

    Also known as: Short, F

    The sequence of this isoform differs from the canonical sequence as follows:
         460-472: Missing.

    Show »
    Length:549
    Mass (Da):61,082
    Checksum:iE4FA8AE7638654B1
    GO

    Sequence cautioni

    The sequence AAN71256.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 180175Missing in AAN71256. (PubMed:12537569)CuratedAdd
    BLAST
    Sequence conflicti11 – 155GARRQ → APAAR in CAA72173. (PubMed:10992165)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei460 – 47213Missing in isoform C. 1 PublicationVSP_001285Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11314 mRNA. Translation: CAA72173.1.
    Z29062 mRNA. Translation: CAA82304.1.
    AE014297 Genomic DNA. Translation: AAF56209.5.
    AE014297 Genomic DNA. Translation: AAS65200.1.
    AY061323 mRNA. Translation: AAL28871.1.
    BT001501 mRNA. Translation: AAN71256.1. Different initiation.
    PIRiS42919.
    RefSeqiNP_524470.4. NM_079746.6. [P54385-1]
    NP_996274.1. NM_206551.3. [P54385-2]
    UniGeneiDm.3641.

    Genome annotation databases

    EnsemblMetazoaiFBtr0089498; FBpp0088988; FBgn0001098. [P54385-1]
    GeneIDi42832.
    KEGGidme:Dmel_CG5320.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11314 mRNA. Translation: CAA72173.1 .
    Z29062 mRNA. Translation: CAA82304.1 .
    AE014297 Genomic DNA. Translation: AAF56209.5 .
    AE014297 Genomic DNA. Translation: AAS65200.1 .
    AY061323 mRNA. Translation: AAL28871.1 .
    BT001501 mRNA. Translation: AAN71256.1 . Different initiation.
    PIRi S42919.
    RefSeqi NP_524470.4. NM_079746.6. [P54385-1 ]
    NP_996274.1. NM_206551.3. [P54385-2 ]
    UniGenei Dm.3641.

    3D structure databases

    ProteinModelPortali P54385.
    SMRi P54385. Positions 54-562.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 67768. 22 interactions.
    IntActi P54385. 1 interaction.
    MINTi MINT-747345.

    Proteomic databases

    PaxDbi P54385.
    PRIDEi P54385.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0089498 ; FBpp0088988 ; FBgn0001098 . [P54385-1 ]
    GeneIDi 42832.
    KEGGi dme:Dmel_CG5320.

    Organism-specific databases

    CTDi 42832.
    FlyBasei FBgn0001098. Gdh.

    Phylogenomic databases

    eggNOGi COG0334.
    GeneTreei ENSGT00390000000854.
    InParanoidi P54385.
    KOi K00261.
    OMAi TCIGVIE.
    OrthoDBi EOG73NG50.
    PhylomeDBi P54385.

    Enzyme and pathway databases

    Reactomei REACT_216833. Amino acid synthesis and interconversion (transamination).

    Miscellaneous databases

    ChiTaRSi GDH. drosophila.
    GenomeRNAii 42832.
    NextBioi 830799.
    PROi P54385.

    Gene expression databases

    Bgeei P54385.

    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. "The glutamate dehydrogenase gene of Drosophila melanogaster: molecular analysis and expression."
      Papadopoulou D., Louis C.
      J. Neurogenet. 14:125-143(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS A AND C), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
      Strain: Berkeley.
      Tissue: Embryo.
    5. "Purification and genetic control of NAD-dependent glutamate dehydrogenase from Drosophila melanogaster."
      Caggese C., De Pinto V., Ferrandino A.
      Biochem. Genet. 20:449-460(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.

    Entry informationi

    Entry nameiDHE3_DROME
    AccessioniPrimary (citable) accession number: P54385
    Secondary accession number(s): P91624, Q8IH05, Q9VCF7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 121 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3