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Q9VA02

- DHTK1_DROME

UniProt

Q9VA02 - DHTK1_DROME

Protein

Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1 homolog, mitochondrial

Gene

CG1544

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.By similarity

    Catalytic activityi

    2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.

    Cofactori

    Thiamine pyrophosphate.By similarity

    GO - Molecular functioni

    1. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB
    2. thiamine pyrophosphate binding Source: InterPro

    GO - Biological processi

    1. generation of precursor metabolites and energy Source: UniProtKB
    2. glycolytic process Source: UniProtKB-KW
    3. tricarboxylic acid cycle Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Thiamine pyrophosphate

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1 homolog, mitochondrial (EC:1.2.4.2)
    Gene namesi
    ORF Names:CG1544
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0039827. CG1544.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial membrane Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 919Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1 homolog, mitochondrialPRO_0000307943
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Proteomic databases

    PaxDbiQ9VA02.

    Expressioni

    Gene expression databases

    BgeeiQ9VA02.

    Interactioni

    Protein-protein interaction databases

    BioGridi68534. 4 interactions.
    IntActiQ9VA02. 1 interaction.
    MINTiMINT-940711.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VA02.
    SMRiQ9VA02. Positions 54-917.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0567.
    GeneTreeiENSGT00530000063092.
    InParanoidiQ9VA02.
    KOiK15791.
    OMAiLCSGKHY.
    OrthoDBiEOG7CZK4Z.
    PhylomeDBiQ9VA02.

    Family and domain databases

    Gene3Di3.40.50.970. 2 hits.
    InterProiIPR011603. 2oxoglutarate_DH_E1.
    IPR001017. DH_E1.
    IPR029061. THDP-binding.
    IPR005475. Transketolase-like_Pyr-bd.
    [Graphical view]
    PANTHERiPTHR23152. PTHR23152. 1 hit.
    PfamiPF00676. E1_dh. 1 hit.
    PF02779. Transket_pyr. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
    SMARTiSM00861. Transket_pyr. 1 hit.
    [Graphical view]
    SUPFAMiSSF52518. SSF52518. 2 hits.
    TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9VA02-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRYLALSEA GIAKLPRPQS RCYHSEKGVW GYKPIAQREF QVAEDVRASR    50
    NSQANVYRFV EAFRQHGHKL AAVNPISIRT SQQELQELSP AFYGLQTQEP 100
    VRTDGLLSGP QVAHNVAQLE QLLKDIYCGR STSAEFSYVE DIEEREWLAR 150
    NFETLDQQQL GKSERCEIAE LLIKSQAWDN FMALKFPTVK RYGGEGAESM 200
    LAFFWQLLRD SVQANIEHVV LAMPHRGRTP LQAALLNMRP AKVFRKLSGA 250
    SEFSEDIEAM SDVISHFHVS EQLKILGKKL SFSMVRNPSH LEAANPVAMG 300
    KTRSKQQARG EGAFGDGSQP FGEHVLNVIL HGDAAFAGQG INQECLNMAY 350
    VPHFEVGGSL HLIVNNQVGF TTPGDRGRST AYTSDLAKSI QAPVFHVNGD 400
    DPEALARVTS LAFRYQREFR KDIFIDLNCF RRWGHNELDD PTFTNPLVYK 450
    IVHQRESVPD LYAQQLAKEQ VLSESKAKEM RDEYMKYLGE ELALAPAYQP 500
    PPSYFEKQWT NFQLAPSKEL TYWDTGLDYS LLHYIGQQSV TFPEDFNIHP 550
    HLLKTHVNAR LKKLENGVKI DWSTAEALAI GSLMYQGHNV RISGEDVGRG 600
    TFSHRHAMLV DQQTNEMFIP LNSMEGGNGG KLELAHSILS EEAVLGFEYG 650
    MAIDNPNNLI IWEAQFGDFA NGAQIIIDTF IVSGETKWME SNALVMLLPH 700
    GYDGAASEHS SCRIERFLQL CDSKETSADG DSVNVHIVNP TTPAQYYHVL 750
    RRQLARNFRK PLVVVAPKTL LRLPAATSTH EDFQPGTLFH NVLGDTIAKP 800
    EQVRKVILCS GKHYYTLAEE REKRQAYDTA ILRLESLCPF PIQELQAQLA 850
    QYGNVQSFVW SQEEHRNMGA WTFVRPRFEN LIGQQLHYCG RCEAPTPATG 900
    IGKVHKREVD EIVAAPFEL 919
    Length:919
    Mass (Da):103,635
    Last modified:March 1, 2003 - v2
    Checksum:i064A1E1034DE5E0E
    GO

    Sequence cautioni

    The sequence AAM48330.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti248 – 2481S → G in AAN71328. (PubMed:12537569)Curated
    Sequence conflicti913 – 9131V → D in AAN71328. (PubMed:12537569)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014297 Genomic DNA. Translation: AAF57126.2.
    AY118301 mRNA. Translation: AAM48330.1. Different initiation.
    BT001573 mRNA. Translation: AAN71328.1.
    RefSeqiNP_651849.1. NM_143592.2.
    UniGeneiDm.10912.

    Genome annotation databases

    EnsemblMetazoaiFBtr0085755; FBpp0085117; FBgn0039827.
    GeneIDi43689.
    KEGGidme:Dmel_CG1544.
    UCSCiCG1544-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014297 Genomic DNA. Translation: AAF57126.2 .
    AY118301 mRNA. Translation: AAM48330.1 . Different initiation.
    BT001573 mRNA. Translation: AAN71328.1 .
    RefSeqi NP_651849.1. NM_143592.2.
    UniGenei Dm.10912.

    3D structure databases

    ProteinModelPortali Q9VA02.
    SMRi Q9VA02. Positions 54-917.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 68534. 4 interactions.
    IntActi Q9VA02. 1 interaction.
    MINTi MINT-940711.

    Proteomic databases

    PaxDbi Q9VA02.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0085755 ; FBpp0085117 ; FBgn0039827 .
    GeneIDi 43689.
    KEGGi dme:Dmel_CG1544.
    UCSCi CG1544-RA. d. melanogaster.

    Organism-specific databases

    FlyBasei FBgn0039827. CG1544.

    Phylogenomic databases

    eggNOGi COG0567.
    GeneTreei ENSGT00530000063092.
    InParanoidi Q9VA02.
    KOi K15791.
    OMAi LCSGKHY.
    OrthoDBi EOG7CZK4Z.
    PhylomeDBi Q9VA02.

    Miscellaneous databases

    GenomeRNAii 43689.
    NextBioi 835260.
    PROi Q9VA02.

    Gene expression databases

    Bgeei Q9VA02.

    Family and domain databases

    Gene3Di 3.40.50.970. 2 hits.
    InterProi IPR011603. 2oxoglutarate_DH_E1.
    IPR001017. DH_E1.
    IPR029061. THDP-binding.
    IPR005475. Transketolase-like_Pyr-bd.
    [Graphical view ]
    PANTHERi PTHR23152. PTHR23152. 1 hit.
    Pfami PF00676. E1_dh. 1 hit.
    PF02779. Transket_pyr. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000157. Oxoglu_dh_E1. 1 hit.
    SMARTi SM00861. Transket_pyr. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52518. SSF52518. 2 hits.
    TIGRFAMsi TIGR00239. 2oxo_dh_E1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo and Head.

    Entry informationi

    Entry nameiDHTK1_DROME
    AccessioniPrimary (citable) accession number: Q9VA02
    Secondary accession number(s): Q8IGV6, Q8MT95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 2007
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 93 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    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