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P41367

- ACADM_PIG

UniProt

P41367 - ACADM_PIG

Protein

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

ACADM

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 3 (29 May 2007)
      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 oxygen
    Binding sitei216 – 2161Substrate
    Binding sitei278 – 2781Substrate
    Active sitei401 – 4011Proton acceptor
    Binding sitei402 – 4021Substrate; via amide nitrogen
    Binding sitei413 – 4131Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi158 – 16710FAD
    Nucleotide bindingi191 – 1933FAD
    Nucleotide bindingi306 – 3083FAD; shared with dimeric partner
    Nucleotide bindingi316 – 3172FAD
    Nucleotide bindingi374 – 3785FAD; shared with dimeric partner
    Nucleotide bindingi403 – 4053FAD

    GO - Molecular functioni

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

    GO - Biological processi

    1. cardiac muscle cell differentiation Source: Ensembl
    2. carnitine biosynthetic process Source: Ensembl
    3. carnitine metabolic process, CoA-linked Source: Ensembl
    4. fatty acid beta-oxidation Source: UniProtKB
    5. fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: Ensembl
    6. glycogen biosynthetic process Source: Ensembl
    7. liver development Source: Ensembl
    8. medium-chain fatty acid catabolic process Source: Ensembl
    9. post-embryonic development Source: Ensembl
    10. regulation of gluconeogenesis Source: Ensembl
    11. response to cold Source: Ensembl
    12. response to starvation Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    ReactomeiREACT_226431. PPARA activates gene expression.
    SABIO-RKP41367.
    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
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Chromosome 6

    Subcellular locationi

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. mitochondrial matrix Source: UniProtKB-SubCell

    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_0000000505Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    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 residuei279 – 2791N6-acetyllysineBy 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

    PaxDbiP41367.
    PRIDEiP41367.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    IntActiP41367. 2 interactions.
    STRINGi9823.ENSSSCP00000004085.

    Structurei

    Secondary structure

    1
    421
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi43 – 5816
    Helixi61 – 7010
    Helixi75 – 839
    Helixi93 – 953
    Helixi102 – 11514
    Helixi117 – 13620
    Helixi139 – 15113
    Beta strandi156 – 1594
    Beta strandi165 – 1673
    Helixi169 – 1713
    Beta strandi175 – 1784
    Beta strandi180 – 19314
    Turni194 – 1974
    Beta strandi199 – 2068
    Helixi215 – 2184
    Beta strandi219 – 2257
    Beta strandi231 – 2366
    Beta strandi239 – 2424
    Beta strandi247 – 25812
    Helixi259 – 2613
    Beta strandi262 – 2654
    Helixi269 – 30335
    Helixi313 – 3153
    Helixi317 – 34529
    Helixi351 – 37626
    Helixi378 – 3814
    Helixi387 – 3948
    Helixi395 – 3984
    Beta strandi400 – 4023
    Helixi404 – 41714

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UDYX-ray2.40A/B/C/D26-421[»]
    3MDDX-ray2.40A/B36-420[»]
    3MDEX-ray2.40A/B36-420[»]
    ProteinModelPortaliP41367.
    SMRiP41367. Positions 36-420.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP41367.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1960.
    GeneTreeiENSGT00750000117417.
    HOGENOMiHOG000131659.
    HOVERGENiHBG000224.
    KOiK00249.
    OMAiSAWEVDQ.
    OrthoDBiEOG74FF0S.
    TreeFamiTF105020.

    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.

    P41367-1 [UniParc]FASTAAdd to Basket

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    MAAMFRRSCR VLRSLSHFGW RSQHTKAVPQ CEPGSGFSFE LTEQQKEFQA    50
    TARKFAREEI IPVAAEYDRT GEYPVPLLKR AWELGLMNTH IPESFGGLGL 100
    GIIDSCLITE ELAYGCTGVQ TAIEANTLGQ VPLIIGGNYQ QQKKYLGRMT 150
    EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG DEYIINGQKM WITNGGKANW 200
    YFLLARSDPD PKAPASKAFT GFIVEADTPG VQIGRKEINM GQRCSDTRGI 250
    VFEDVRVPKE NVLTGEGAGF KIAMGTFDKT RPPVAAGAVG LAQRALDEAT 300
    KYALERKTFG KLLAEHQGIS FLLADMAMKV ELARLSYQRA AWEIDSGRRN 350
    TYYASIAKAY AADIANQLAT DAVQVFGGNG FNTEYPVEKL MRDAKIYQIY 400
    EGTAQIQRII IAREHIGRYK N 421
    Length:421
    Mass (Da):46,485
    Last modified:May 29, 2007 - v3
    Checksum:i73BC66092D5E02CB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81S → G in AAA83759. 1 PublicationCurated
    Sequence conflicti40 – 401E → K in AAA83759. 1 PublicationCurated
    Sequence conflicti283 – 2831P → S in AAA83759. 1 PublicationCurated
    Sequence conflicti305 – 3051E → G in AAA83759. 1 PublicationCurated
    Sequence conflicti331 – 3311E → D in AAA83759. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40845 mRNA. Translation: AAA83759.1.
    AY705916 mRNA. Translation: AAW30430.1.
    RefSeqiNP_999204.1. NM_214039.1.
    UniGeneiSsc.142.

    Genome annotation databases

    EnsembliENSSSCT00000004179; ENSSSCP00000004085; ENSSSCG00000003776.
    GeneIDi397104.
    KEGGissc:397104.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40845 mRNA. Translation: AAA83759.1 .
    AY705916 mRNA. Translation: AAW30430.1 .
    RefSeqi NP_999204.1. NM_214039.1.
    UniGenei Ssc.142.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UDY X-ray 2.40 A/B/C/D 26-421 [» ]
    3MDD X-ray 2.40 A/B 36-420 [» ]
    3MDE X-ray 2.40 A/B 36-420 [» ]
    ProteinModelPortali P41367.
    SMRi P41367. Positions 36-420.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P41367. 2 interactions.
    STRINGi 9823.ENSSSCP00000004085.

    Proteomic databases

    PaxDbi P41367.
    PRIDEi P41367.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSSSCT00000004179 ; ENSSSCP00000004085 ; ENSSSCG00000003776 .
    GeneIDi 397104.
    KEGGi ssc:397104.

    Organism-specific databases

    CTDi 34.

    Phylogenomic databases

    eggNOGi COG1960.
    GeneTreei ENSGT00750000117417.
    HOGENOMi HOG000131659.
    HOVERGENi HBG000224.
    KOi K00249.
    OMAi SAWEVDQ.
    OrthoDBi EOG74FF0S.
    TreeFami TF105020.

    Enzyme and pathway databases

    UniPathwayi UPA00660 .
    Reactomei REACT_226431. PPARA activates gene expression.
    SABIO-RK P41367.

    Miscellaneous databases

    EvolutionaryTracei P41367.

    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. Suzuki H., Kimura M., Ito T., Murakami Y., Hamasima N., Yasue H.
      Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Mutation detection in the porcine ACADM gene."
      Jeon J.-T., Park J.-J., Kim J.-H., Lim H.-T., Seo B.-Y., Cho I.-C.
      Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Skeletal muscle.
    3. "Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate."
      Kim J.-J.P., Wang M., Paschke R.
      Proc. Natl. Acad. Sci. U.S.A. 90:7523-7527(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEXES WITH FAD AND SUBSTRATE.
      Tissue: Liver.

    Entry informationi

    Entry nameiACADM_PIG
    AccessioniPrimary (citable) accession number: P41367
    Secondary accession number(s): Q58XQ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 114 of the entry and version 3 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3