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Q9VSA3

- ACADM_DROME

UniProt

Q9VSA3 - ACADM_DROME

Protein

Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

CG12262

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    This enzyme is specific for acyl chain lengths of 4 to 16.By similarity

    Catalytic activityi

    A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.

    Cofactori

    FAD.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei163 – 1631Substrate; via carbonyl oxygenBy similarity
    Active sitei397 – 3971Proton acceptorBy similarity
    Binding sitei398 – 3981Substrate; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi154 – 16310FADBy similarity
    Nucleotide bindingi187 – 1893FADBy similarity
    Nucleotide bindingi302 – 3043FADBy similarity
    Nucleotide bindingi312 – 3132FADBy similarity
    Nucleotide bindingi370 – 3745FADBy similarity
    Nucleotide bindingi399 – 4013FADBy similarity

    GO - Molecular functioni

    1. acyl-CoA dehydrogenase activity Source: UniProtKB
    2. flavin adenine dinucleotide binding Source: InterPro

    GO - Biological processi

    1. fatty acid beta-oxidation Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    ReactomeiREACT_180846. PPARA activates gene expression.
    REACT_202493. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
    REACT_204741. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
    REACT_206217. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
    UniPathwayiUPA00660.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.7)
    Short name:
    MCAD
    Gene namesi
    ORF Names:CG12262
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0035811. CG12262.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. lipid particle Source: FlyBase
    2. microtubule associated complex Source: FlyBase
    3. mitochondrial matrix Source: UniProtKB-SubCell
    4. mitochondrion Source: FlyBase

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1717MitochondrionBy similarityAdd
    BLAST
    Chaini18 – 419402Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000508Add
    BLAST

    Proteomic databases

    PaxDbiQ9VSA3.
    PRIDEiQ9VSA3.

    Expressioni

    Gene expression databases

    BgeeiQ9VSA3.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    mbtQ9VXE51EBI-87748,EBI-75994

    Protein-protein interaction databases

    BioGridi64295. 83 interactions.
    DIPiDIP-20518N.
    IntActiQ9VSA3. 1 interaction.
    MINTiMINT-814595.
    STRINGi7227.FBpp0076520.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VSA3.
    SMRiQ9VSA3. Positions 32-409.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni274 – 2774Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1960.
    GeneTreeiENSGT00750000117417.
    InParanoidiQ9VSA3.
    KOiK00249.
    OMAiHIPENCD.
    OrthoDBiEOG74FF0S.
    PhylomeDBiQ9VSA3.

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProiIPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
    PS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9VSA3-1 [UniParc]FASTAAdd to Basket

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    MAFLNKLAAP ALRQLVSQSR AYAAVSHVSP NGTSFALTED QLQLQELARK    50
    FTREEIIPVA AQYDKSGEYP WPIIKKAWEL GLMNNHIPAD IGGLDLDVFT 100
    TCLSAEELAY GCTGIMTALE ASGLGQTPVI LSGNKEQKKK YLGRLLEEPL 150
    VAAYCVTEPG AGSDVSGIKT RAEKKGDEWV INGQKMWITN GGVANWYFVL 200
    ARTNPDPKCP PSKAFTGFIV ERDSPGLTPG RKELNMGQRA SDTRGITFED 250
    VRVPKENVLI GEGAGFKIAM GTFDKTRPPV AAGAVGLAQR CLDEALKYAL 300
    ERKTFGVPIA YHQAVQFMLA DMAIGVETSR LAWRLSAWEI DQGRRNSYYA 350
    SIAKCHAADM ANKIASDAVQ IFGGNGFNSE YPVEKLMRDA KIYQIYEGTS 400
    QIQRLIISRN MYEAAKGQA 419
    Length:419
    Mass (Da):45,871
    Last modified:May 1, 2000 - v1
    Checksum:i0B1970302243C394
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014296 Genomic DNA. Translation: AAF50524.1.
    AY089546 mRNA. Translation: AAL90284.1.
    RefSeqiNP_648149.1. NM_139892.3.
    UniGeneiDm.879.

    Genome annotation databases

    EnsemblMetazoaiFBtr0076808; FBpp0076520; FBgn0035811.
    GeneIDi38864.
    KEGGidme:Dmel_CG12262.
    UCSCiCG12262-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014296 Genomic DNA. Translation: AAF50524.1 .
    AY089546 mRNA. Translation: AAL90284.1 .
    RefSeqi NP_648149.1. NM_139892.3.
    UniGenei Dm.879.

    3D structure databases

    ProteinModelPortali Q9VSA3.
    SMRi Q9VSA3. Positions 32-409.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 64295. 83 interactions.
    DIPi DIP-20518N.
    IntActi Q9VSA3. 1 interaction.
    MINTi MINT-814595.
    STRINGi 7227.FBpp0076520.

    Proteomic databases

    PaxDbi Q9VSA3.
    PRIDEi Q9VSA3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0076808 ; FBpp0076520 ; FBgn0035811 .
    GeneIDi 38864.
    KEGGi dme:Dmel_CG12262.
    UCSCi CG12262-RA. d. melanogaster.

    Organism-specific databases

    FlyBasei FBgn0035811. CG12262.

    Phylogenomic databases

    eggNOGi COG1960.
    GeneTreei ENSGT00750000117417.
    InParanoidi Q9VSA3.
    KOi K00249.
    OMAi HIPENCD.
    OrthoDBi EOG74FF0S.
    PhylomeDBi Q9VSA3.

    Enzyme and pathway databases

    UniPathwayi UPA00660 .
    Reactomei REACT_180846. PPARA activates gene expression.
    REACT_202493. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
    REACT_204741. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
    REACT_206217. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.

    Miscellaneous databases

    GenomeRNAii 38864.
    NextBioi 810749.
    PROi Q9VSA3.

    Gene expression databases

    Bgeei Q9VSA3.

    Family and domain databases

    Gene3Di 1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProi IPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view ]
    Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
    PS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view ]
    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.

    Entry informationi

    Entry nameiACADM_DROME
    AccessioniPrimary (citable) accession number: Q9VSA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 12, 2003
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3