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P08503

- ACADM_RAT

UniProt

P08503 - ACADM_RAT

Protein

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acadm

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Cofactori

    FAD.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei167 – 1671Substrate; via carbonyl oxygenBy similarity
    Active sitei401 – 4011Proton acceptorBy similarity
    Binding sitei402 – 4021Substrate; via amide nitrogenBy similarity
    Binding sitei413 – 4131SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi158 – 16710FADBy similarity
    Nucleotide bindingi191 – 1933FADBy similarity
    Nucleotide bindingi306 – 3083FADBy similarity
    Nucleotide bindingi316 – 3172FADBy similarity
    Nucleotide bindingi374 – 3785FADBy similarity
    Nucleotide bindingi403 – 4053FADBy similarity

    GO - Molecular functioni

    1. acyl-CoA dehydrogenase activity Source: UniProtKB
    2. fatty-acyl-CoA binding Source: RGD
    3. flavin adenine dinucleotide binding Source: RGD
    4. identical protein binding Source: BHF-UCL
    5. isomerase activity Source: RGD

    GO - Biological processi

    1. fatty acid beta-oxidation Source: UniProtKB
    2. fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: RGD
    3. medium-chain fatty acid catabolic process Source: RGD
    4. protein homotetramerization Source: RGD
    5. response to copper ion Source: RGD
    6. response to drug Source: RGD
    7. response to glucocorticoid Source: RGD
    8. response to hormone Source: RGD
    9. response to nutrient Source: RGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    SABIO-RKP08503.
    UniPathwayiUPA00660.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.7)
    Short name:
    MCAD
    Gene namesi
    Name:Acadm
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2012. Acadm.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: BHF-UCL
    2. mitochondrial membrane Source: BHF-UCL
    3. mitochondrion Source: RGD

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2525MitochondrionAdd
    BLAST
    Chaini26 – 421396Medium-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000506Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei69 – 691N6-acetyllysine; alternateBy similarity
    Modified residuei69 – 691N6-succinyllysine; alternateBy similarity
    Modified residuei79 – 791N6-acetyllysineBy similarity
    Modified residuei179 – 1791N6-succinyllysineBy similarity
    Modified residuei212 – 2121N6-acetyllysine; alternateBy similarity
    Modified residuei212 – 2121N6-succinyllysine; alternateBy similarity
    Modified residuei217 – 2171N6-acetyllysine; alternateBy similarity
    Modified residuei217 – 2171N6-succinyllysine; alternateBy similarity
    Modified residuei259 – 2591N6-acetyllysine; alternateBy similarity
    Modified residuei259 – 2591N6-succinyllysine; alternateBy similarity
    Modified residuei271 – 2711N6-acetyllysine; alternateBy similarity
    Modified residuei271 – 2711N6-succinyllysine; alternateBy similarity
    Modified residuei301 – 3011N6-acetyllysineBy similarity

    Post-translational modificationi

    Acetylation at Lys-307 and Lys-311 in proximity of the cofactor-binding sites reduces catalytic activity. These sites are deacetylated by SIRT3 By similarity.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP08503.
    PRIDEiP08503.

    Expressioni

    Gene expression databases

    GenevestigatoriP08503.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    IntActiP08503. 1 interaction.
    STRINGi10116.ENSRNOP00000013238.

    Structurei

    3D structure databases

    ProteinModelPortaliP08503.
    SMRiP08503. Positions 34-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni278 – 2814Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1960.
    HOGENOMiHOG000131659.
    HOVERGENiHBG000224.
    InParanoidiP08503.
    KOiK00249.
    PhylomeDBiP08503.

    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.

    P08503-1 [UniParc]FASTAAdd to Basket

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    MAAALRRGYK VLRSVSHFEC RAQHTKPSLK QEPGLGFSFE LTEQQKEFQT    50
    IARKFAREEI IPVAPDYDKS GEYPFPLIKR AWELGLINTH IPESCGGLGL 100
    GTFDACLITE ELAYGCTGVQ TAIEANSLGQ MPVIIAGNDQ QKKKYLGRMT 150
    EQPMMCAYCV TEPSAGSDVA GIKTKAEKKG DEYVINGQKM WITNGGKANW 200
    YFVLTRSNPD PKVPASKAFT GFIVEADTPG IHIGKKELNM GQRCSDTRGI 250
    TFEDVRVPKE NVLIGEGAGF KIAMGAFDRT RPTVAAGAVG LAQRALDEAT 300
    KYALDRKTFG KLLVEHQGVS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN 350
    TYFASIAKAF AGDIANQLAT DAVQIFGGYG FNTEYPVEKL MRDAKIYQIY 400
    EGTAQIQRLI IAREHIEKYK N 421
    Length:421
    Mass (Da):46,555
    Last modified:August 1, 1988 - v1
    Checksum:i2CF076F8C919BDE8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02791 mRNA. Translation: AAA40670.1.
    PIRiA28436. DERTCM.
    RefSeqiNP_058682.2. NM_016986.2.
    UniGeneiRn.6302.

    Genome annotation databases

    GeneIDi24158.
    KEGGirno:24158.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02791 mRNA. Translation: AAA40670.1 .
    PIRi A28436. DERTCM.
    RefSeqi NP_058682.2. NM_016986.2.
    UniGenei Rn.6302.

    3D structure databases

    ProteinModelPortali P08503.
    SMRi P08503. Positions 34-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P08503. 1 interaction.
    STRINGi 10116.ENSRNOP00000013238.

    Chemistry

    ChEMBLi CHEMBL2176828.

    Proteomic databases

    PaxDbi P08503.
    PRIDEi P08503.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24158.
    KEGGi rno:24158.

    Organism-specific databases

    CTDi 34.
    RGDi 2012. Acadm.

    Phylogenomic databases

    eggNOGi COG1960.
    HOGENOMi HOG000131659.
    HOVERGENi HBG000224.
    InParanoidi P08503.
    KOi K00249.
    PhylomeDBi P08503.

    Enzyme and pathway databases

    UniPathwayi UPA00660 .
    SABIO-RK P08503.

    Miscellaneous databases

    NextBioi 602449.
    PROi P08503.

    Gene expression databases

    Genevestigatori P08503.

    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. "Molecular cloning and nucleotide sequence of cDNA encoding the entire precursor of rat liver medium chain acyl coenzyme A dehydrogenase."
      Matsubara Y., Kraus J.P., Ozasa H., Glassberg R., Finocchiaro G., Ikeda Y., Mole J., Rosenberg L.E., Tanaka K.
      J. Biol. Chem. 262:10104-10108(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.
    2. "Structurally different rat liver medium-chain acyl CoA dehydrogenases directed by complementary DNAs differing in their 5'-region."
      Inagaki T., Ohishi N., Tsukagoshi N., Udaka S., Ghisla S., Yagi K.
      Biochim. Biophys. Acta 1077:285-290(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 11-81.

    Entry informationi

    Entry nameiACADM_RAT
    AccessioniPrimary (citable) accession number: P08503
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 129 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3