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P11310

- ACADM_HUMAN

UniProt

P11310 - ACADM_HUMAN

Protein

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

ACADM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 176 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      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.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei167 – 1671Substrate; via carbonyl oxygen
    Binding sitei216 – 2161Substrate
    Active sitei401 – 4011Proton acceptor
    Binding sitei402 – 4021Substrate; via amide nitrogen
    Binding sitei413 – 4131Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi158 – 16710FAD1 Publication
    Nucleotide bindingi191 – 1933FAD1 Publication
    Nucleotide bindingi306 – 3083FAD1 Publication
    Nucleotide bindingi316 – 3172FAD1 Publication
    Nucleotide bindingi374 – 3785FAD1 Publication
    Nucleotide bindingi403 – 4053FAD1 Publication

    GO - Molecular functioni

    1. acyl-CoA dehydrogenase activity Source: UniProtKB
    2. flavin adenine dinucleotide binding Source: InterPro
    3. identical protein binding Source: BHF-UCL
    4. medium-chain-acyl-CoA dehydrogenase activity Source: BHF-UCL

    GO - Biological processi

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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04089-MONOMER.
    ReactomeiREACT_116145. PPARA activates gene expression.
    REACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
    REACT_1697. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
    REACT_1708. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
    SABIO-RKP11310.
    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:89. ACADM.

    Subcellular locationi

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrial matrix Source: Reactome
    4. mitochondrion Source: LIFEdb
    5. nucleus Source: UniProt

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:201450]: An inborn error of mitochondrial fatty acid beta-oxidation which causes fasting hypoglycemia, hepatic dysfunction and encephalopathy, often resulting in death in infancy.14 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti53 – 531R → C in ACADMD.
    VAR_000317
    Natural varianti67 – 671Y → H in ACADMD; mild. 1 Publication
    VAR_013698
    Natural varianti78 – 781I → T in ACADMD. 1 Publication
    VAR_015954
    Natural varianti115 – 1162Missing in ACADMD. 1 Publication
    VAR_000318
    Natural varianti116 – 1161C → Y in ACADMD. 1 Publication
    VAR_015955
    Natural varianti121 – 1211T → I in ACADMD. 1 Publication
    VAR_015956
    Natural varianti149 – 1491M → I in ACADMD. 1 Publication
    VAR_000319
    Natural varianti193 – 1931T → A in ACADMD; the thermostability is markedly decreased. 1 Publication
    VAR_000320
    Natural varianti195 – 1951G → R in ACADMD. 1 Publication
    VAR_000321
    Natural varianti206 – 2061R → L in ACADMD. 1 Publication
    VAR_015957
    Natural varianti244 – 2441C → R in ACADMD. 1 Publication
    VAR_000322
    Natural varianti245 – 2451S → L in ACADMD. 1 Publication
    VAR_013699
    Natural varianti267 – 2671G → R in ACADMD. 1 Publication
    VAR_000323
    Natural varianti281 – 2811R → T in ACADMD; mild or benign clinical phenotype. 1 Publication
    VAR_013700
    Natural varianti310 – 3101G → R in ACADMD. 1 Publication
    VAR_015958
    Natural varianti326 – 3261M → T in ACADMD. 1 Publication
    VAR_000324
    Natural varianti329 – 3291K → E in ACADMD; most common variant. 6 Publications
    Corresponds to variant rs77931234 [ dbSNP | Ensembl ].
    VAR_000325
    Natural varianti336 – 3361S → R in ACADMD. 1 Publication
    VAR_000326
    Natural varianti352 – 3521Y → C in ACADMD. 1 Publication
    VAR_015959
    Natural varianti375 – 3751I → T in ACADMD. 1 Publication
    VAR_000327

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi86 – 861L → M: Strongly reduced rate of electron transfer to ETF. 1 Publication
    Mutagenesisi98 – 981L → W: Strongly reduced rate of electron transfer to ETF. 1 Publication
    Mutagenesisi100 – 1001L → Y: Strongly reduced rate of electron transfer to ETF. 1 Publication
    Mutagenesisi108 – 1081I → M: Strongly reduced rate of electron transfer to ETF. 1 Publication
    Mutagenesisi191 – 1911W → A: Loss of electron transfer to ETF. 1 Publication
    Mutagenesisi191 – 1911W → F: Reduces rate of electron transfer to ETF about six-fold. 1 Publication
    Mutagenesisi237 – 2371E → A: Strongly reduced rate of electron transfer to ETF. 2 Publications
    Mutagenesisi384 – 3841E → A: Reduces rate of electron transfer to ETF three-fold. 2 Publications
    Mutagenesisi384 – 3841E → Q: Reduces rate of electron transfer to ETF two-fold. 2 Publications

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi201450. phenotype.
    Orphaneti42. Medium chain acyl-CoA dehydrogenase deficiency.
    PharmGKBiPA24425.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2525MitochondrionAdd
    BLAST
    Chaini26 – 421396Medium-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000502Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei69 – 691N6-acetyllysine; alternateBy similarity
    Modified residuei69 – 691N6-succinyllysine; alternateBy 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-acetyllysine1 Publication
    Modified residuei301 – 3011N6-acetyllysine1 Publication

    Post-translational modificationi

    Acetylation at Lys-307 and Lys-311 in proximity of the cofactor-binding sites reduces catalytic activity By similarity. These sites are deacetylated by SIRT3.By similarity1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP11310.
    PaxDbiP11310.
    PRIDEiP11310.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00005040.
    UCD-2DPAGEP11310.

    PTM databases

    PhosphoSiteiP11310.

    Expressioni

    Gene expression databases

    ArrayExpressiP11310.
    BgeeiP11310.
    CleanExiHS_ACADM.
    GenevestigatoriP11310.

    Organism-specific databases

    HPAiHPA006198.
    HPA026542.

    Interactioni

    Subunit structurei

    Homotetramer. Interacts with the heterodimeric electron transfer flavoprotein ETF.3 Publications

    Protein-protein interaction databases

    BioGridi106552. 11 interactions.
    DIPiDIP-34281N.
    IntActiP11310. 7 interactions.
    MINTiMINT-3007693.
    STRINGi9606.ENSP00000409612.

    Structurei

    Secondary structure

    1
    421
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 383
    Helixi43 – 5917
    Helixi61 – 7010
    Helixi75 – 8410
    Helixi93 – 953
    Helixi102 – 11514
    Helixi117 – 12913
    Helixi131 – 1366
    Helixi139 – 15113
    Beta strandi156 – 1594
    Beta strandi165 – 1684
    Helixi169 – 1713
    Beta strandi175 – 1784
    Beta strandi180 – 19314
    Turni194 – 1974
    Beta strandi199 – 2068
    Helixi215 – 2173
    Beta strandi219 – 2257
    Beta strandi231 – 2333
    Beta strandi239 – 2413
    Beta strandi247 – 25812
    Helixi259 – 2613
    Beta strandi262 – 2654
    Turni266 – 2683
    Helixi269 – 30335
    Beta strandi309 – 3124
    Helixi313 – 3153
    Helixi317 – 34529
    Helixi351 – 37626
    Helixi377 – 3793
    Helixi387 – 3948
    Helixi395 – 3984
    Turni399 – 4013
    Helixi404 – 41714

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EGCX-ray2.60A/B/C/D26-421[»]
    1EGDX-ray2.40A/B/C/D26-421[»]
    1EGEX-ray2.75A/B/C/D26-421[»]
    1T9GX-ray2.90A/B/C/D26-421[»]
    2A1TX-ray2.80A/B/C/D1-421[»]
    ProteinModelPortaliP11310.
    SMRiP11310. Positions 35-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11310.

    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.
    HOGENOMiHOG000131659.
    HOVERGENiHBG000224.
    KOiK00249.
    OrthoDBiEOG74FF0S.
    PhylomeDBiP11310.
    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]

    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 1 (identifier: P11310-1) [UniParc]FASTAAdd to Basket

    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

    MAAGFGRCCR VLRSISRFHW RSQHTKANRQ REPGLGFSFE FTEQQKEFQA    50
    TARKFAREEI IPVAAEYDKT GEYPVPLIRR AWELGLMNTH IPENCGGLGL 100
    GTFDACLISE ELAYGCTGVQ TAIEGNSLGQ MPIIIAGNDQ QKKKYLGRMT 150
    EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG DEYIINGQKM WITNGGKANW 200
    YFLLARSDPD PKAPANKAFT GFIVEADTPG IQIGRKELNM GQRCSDTRGI 250
    VFEDVKVPKE NVLIGDGAGF KVAMGAFDKT RPVVAAGAVG LAQRALDEAT 300
    KYALERKTFG KLLVEHQAIS FMLAEMAMKV ELARMSYQRA AWEVDSGRRN 350
    TYYASIAKAF AGDIANQLAT DAVQILGGNG FNTEYPVEKL MRDAKIYQIY 400
    EGTSQIQRLI VAREHIDKYK N 421
    Length:421
    Mass (Da):46,588
    Last modified:July 1, 1989 - v1
    Checksum:i7CD0B5832410581B
    GO
    Isoform 2 (identifier: P11310-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         10-10: R → RCSLQ

    Show »
    Length:425
    Mass (Da):47,020
    Checksum:iC6A133404E1B6E70
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti356 – 3561I → T in AAF63626. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti53 – 531R → C in ACADMD.
    VAR_000317
    Natural varianti67 – 671Y → H in ACADMD; mild. 1 Publication
    VAR_013698
    Natural varianti78 – 781I → T in ACADMD. 1 Publication
    VAR_015954
    Natural varianti115 – 1162Missing in ACADMD. 1 Publication
    VAR_000318
    Natural varianti116 – 1161C → Y in ACADMD. 1 Publication
    VAR_015955
    Natural varianti121 – 1211T → I in ACADMD. 1 Publication
    VAR_015956
    Natural varianti132 – 1321P → R in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035716
    Natural varianti149 – 1491M → I in ACADMD. 1 Publication
    VAR_000319
    Natural varianti193 – 1931T → A in ACADMD; the thermostability is markedly decreased. 1 Publication
    VAR_000320
    Natural varianti195 – 1951G → R in ACADMD. 1 Publication
    VAR_000321
    Natural varianti206 – 2061R → L in ACADMD. 1 Publication
    VAR_015957
    Natural varianti244 – 2441C → R in ACADMD. 1 Publication
    VAR_000322
    Natural varianti245 – 2451S → L in ACADMD. 1 Publication
    VAR_013699
    Natural varianti267 – 2671G → R in ACADMD. 1 Publication
    VAR_000323
    Natural varianti281 – 2811R → T in ACADMD; mild or benign clinical phenotype. 1 Publication
    VAR_013700
    Natural varianti310 – 3101G → R in ACADMD. 1 Publication
    VAR_015958
    Natural varianti326 – 3261M → T in ACADMD. 1 Publication
    VAR_000324
    Natural varianti329 – 3291K → E in ACADMD; most common variant. 6 Publications
    Corresponds to variant rs77931234 [ dbSNP | Ensembl ].
    VAR_000325
    Natural varianti336 – 3361S → R in ACADMD. 1 Publication
    VAR_000326
    Natural varianti352 – 3521Y → C in ACADMD. 1 Publication
    VAR_015959
    Natural varianti375 – 3751I → T in ACADMD. 1 Publication
    VAR_000327

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei10 – 101R → RCSLQ in isoform 2. 1 PublicationVSP_038420

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16827 mRNA. Translation: AAA51566.1.
    M91432
    , M91421, M91422, M91423, M91425, M91426, M91427, M91428, M91429, M91430, M91431 Genomic DNA. Translation: AAA59567.1.
    AF251043 mRNA. Translation: AAF63626.1.
    AK312629 mRNA. Translation: BAG35514.1.
    AL357314 Genomic DNA. Translation: CAI22390.1.
    CH471059 Genomic DNA. Translation: EAX06401.1.
    BC005377 mRNA. Translation: AAH05377.1.
    M60505 Genomic DNA. Translation: AAB59625.1.
    CCDSiCCDS44165.1. [P11310-2]
    CCDS668.1. [P11310-1]
    PIRiA29031. DEHUCM.
    RefSeqiNP_000007.1. NM_000016.5. [P11310-1]
    NP_001120800.1. NM_001127328.2. [P11310-2]
    UniGeneiHs.445040.

    Genome annotation databases

    EnsembliENST00000370841; ENSP00000359878; ENSG00000117054. [P11310-1]
    ENST00000420607; ENSP00000409612; ENSG00000117054. [P11310-2]
    GeneIDi34.
    KEGGihsa:34.
    UCSCiuc001dgw.4. human. [P11310-1]
    uc009wbp.3. human. [P11310-2]

    Polymorphism databases

    DMDMi113017.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16827 mRNA. Translation: AAA51566.1 .
    M91432
    , M91421 , M91422 , M91423 , M91425 , M91426 , M91427 , M91428 , M91429 , M91430 , M91431 Genomic DNA. Translation: AAA59567.1 .
    AF251043 mRNA. Translation: AAF63626.1 .
    AK312629 mRNA. Translation: BAG35514.1 .
    AL357314 Genomic DNA. Translation: CAI22390.1 .
    CH471059 Genomic DNA. Translation: EAX06401.1 .
    BC005377 mRNA. Translation: AAH05377.1 .
    M60505 Genomic DNA. Translation: AAB59625.1 .
    CCDSi CCDS44165.1. [P11310-2 ]
    CCDS668.1. [P11310-1 ]
    PIRi A29031. DEHUCM.
    RefSeqi NP_000007.1. NM_000016.5. [P11310-1 ]
    NP_001120800.1. NM_001127328.2. [P11310-2 ]
    UniGenei Hs.445040.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EGC X-ray 2.60 A/B/C/D 26-421 [» ]
    1EGD X-ray 2.40 A/B/C/D 26-421 [» ]
    1EGE X-ray 2.75 A/B/C/D 26-421 [» ]
    1T9G X-ray 2.90 A/B/C/D 26-421 [» ]
    2A1T X-ray 2.80 A/B/C/D 1-421 [» ]
    ProteinModelPortali P11310.
    SMRi P11310. Positions 35-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106552. 11 interactions.
    DIPi DIP-34281N.
    IntActi P11310. 7 interactions.
    MINTi MINT-3007693.
    STRINGi 9606.ENSP00000409612.

    Chemistry

    DrugBanki DB03147. Flavin adenine dinucleotide.

    PTM databases

    PhosphoSitei P11310.

    Polymorphism databases

    DMDMi 113017.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00005040.
    UCD-2DPAGE P11310.

    Proteomic databases

    MaxQBi P11310.
    PaxDbi P11310.
    PRIDEi P11310.

    Protocols and materials databases

    DNASUi 34.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370841 ; ENSP00000359878 ; ENSG00000117054 . [P11310-1 ]
    ENST00000420607 ; ENSP00000409612 ; ENSG00000117054 . [P11310-2 ]
    GeneIDi 34.
    KEGGi hsa:34.
    UCSCi uc001dgw.4. human. [P11310-1 ]
    uc009wbp.3. human. [P11310-2 ]

    Organism-specific databases

    CTDi 34.
    GeneCardsi GC01P076190.
    GeneReviewsi ACADM.
    HGNCi HGNC:89. ACADM.
    HPAi HPA006198.
    HPA026542.
    MIMi 201450. phenotype.
    607008. gene.
    neXtProti NX_P11310.
    Orphaneti 42. Medium chain acyl-CoA dehydrogenase deficiency.
    PharmGKBi PA24425.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1960.
    HOGENOMi HOG000131659.
    HOVERGENi HBG000224.
    KOi K00249.
    OrthoDBi EOG74FF0S.
    PhylomeDBi P11310.
    TreeFami TF105020.

    Enzyme and pathway databases

    UniPathwayi UPA00660 .
    BioCyci MetaCyc:HS04089-MONOMER.
    Reactomei REACT_116145. PPARA activates gene expression.
    REACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
    REACT_1697. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
    REACT_1708. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
    SABIO-RK P11310.

    Miscellaneous databases

    EvolutionaryTracei P11310.
    GenomeRNAii 34.
    NextBioi 131.
    PROi P11310.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11310.
    Bgeei P11310.
    CleanExi HS_ACADM.
    Genevestigatori P11310.

    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. "Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and its expression in enzyme-deficient human tissue."
      Kelly D.P., Kim J.-J.P., Billadello J.J., Hainline B.E., Chu T.W., Strauss A.W.
      Proc. Natl. Acad. Sci. U.S.A. 84:4068-4072(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Structural organization and regulatory regions of the human medium-chain acyl-CoA dehydrogenase gene."
      Zhang Z.F., Kelly D.P., Kim J.-J.P., Zhou Y.Q., Ogden M.L., Whelan A.J., Strauss A.W.
      Biochemistry 31:81-89(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    3. "Medium-chain acyl-CoA dehydrogenase."
      Sun F., Wang Y., Block G.D.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Colon.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Heart.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Liver.
    8. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 218-235, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    9. "Identification of a common mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency."
      Matsubara Y., Narisawa K., Miyabayashi S., Tada K., Coates P.M., Bachmann C., Elsas L.J. II, Pollitt R.J., Rhead W.J., Roe C.R.
      Biochem. Biophys. Res. Commun. 171:498-505(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-342, VARIANT ACADMD GLU-329.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-279 AND LYS-301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "SIRT3 regulates long-chain acyl-coA dehydrogenase by deacetylating conserved lysines near the active site."
      Bharathi S.S., Zhang Y., Mohsen A.W., Uppala R., Balasubramani M., Schreiber E., Uechi G., Beck M.E., Rardin M.J., Vockley J., Verdin E., Gibson B.W., Hirschey M.D., Goetzman E.S.
      J. Biol. Chem. 288:33837-33847(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEACETYLATION BY SIRT3.
    13. "Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity."
      Lee H.J., Wang M., Paschke R., Nandy A., Ghisla S., Kim J.-J.P.
      Biochemistry 35:12412-12420(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD AND THE SUBSTRATE ANALOG OCTANOYL-COENZYME A, COFACTOR, SUBUNIT.
    14. "Extensive domain motion and electron transfer in the human electron transferring flavoprotein-medium chain acyl-CoA dehydrogenase complex."
      Toogood H.S., van Thiel A., Basran J., Sutcliffe M.J., Scrutton N.S., Leys D.
      J. Biol. Chem. 279:32904-32912(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-421 IN COMPLEXES WITH FAD AND THE ETFA-ETFB HETERODIMER, MUTAGENESIS OF LEU-86; LEU-98; LEU-100; ILE-108; GLU-237 AND GLU-384, SUBUNIT.
    15. "Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein."
      Toogood H.S., van Thiel A., Scrutton N.S., Leys D.
      J. Biol. Chem. 280:30361-30366(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEXES WITH FAD AND THE ETFA-ETFB HETERODIMER, MUTAGENESIS OF TRP-191; GLU-237 AND GLU-384, SUBUNIT.
    16. Cited for: REVIEW ON VARIANTS ACADMD.
    17. "Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation."
      Yokota I., Indo Y., Coates P.M., Tanaka K.
      J. Clin. Invest. 86:1000-1003(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ACADMD GLU-329.
    18. "Molecular characterization of inherited medium-chain acyl-CoA dehydrogenase deficiency."
      Kelly D.P., Whelan A.J., Ogden M.L., Alpers R., Zhang Z.F., Bellus G., Gregersen N., Dorland L., Strauss A.W.
      Proc. Natl. Acad. Sci. U.S.A. 87:9236-9240(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ACADMD GLU-329.
    19. "Molecular survey of a prevalent mutation, 985A-to-G transition, and identification of five infrequent mutations in the medium-chain Acyl-CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency."
      Yokota I., Coates P.M., Hale D.E., Rinaldo P., Tanaka K.
      Am. J. Hum. Genet. 49:1280-1291(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ACADMD ILE-149; ARG-244; ARG-267 AND THR-375.
    20. "Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli."
      Gregersen N., Andresen B.S., Bross P., Winter V., Ruediger N., Engst S., Christensen E., Kelly D., Strauss A.W., Koelvraa S., Bolund L., Ghisla S.
      Hum. Genet. 86:545-551(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ACADMD GLU-329.
    21. "Frequency of the G985 MCAD mutation in the general population."
      Blakemore A.I., Singleton H., Pollitt R.J., Engel P.C., Kolvraa S., Gregersen N., Curtis D.
      Lancet 337:298-299(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ACADMD GLU-329 FREQUENCY.
    22. "Disease-causing mutations in exon 11 of the medium-chain acyl-CoA dehydrogenase gene."
      Andresen B.S., Jensen T.G., Bross P., Knudsen I., Winter V., Koelvraa S., Bolund L., Ding J.-H., Chen Y.-T., van Hove J.L.K., Curtis D., Yokota I., Tanaka K., Kim J.-J.P., Gregersen N.
      Am. J. Hum. Genet. 54:975-988(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ACADMD THR-326 AND ARG-336.
    23. "Medium chain acyl-CoA dehydrogenase deficiency in Pennsylvania: neonatal screening shows high incidence and unexpected mutation frequencies."
      Ziadeh R., Hoffman E.P., Finegold D.N., Hoop R.C., Brackett J.C., Strauss A.W., Naylor E.W.
      Pediatr. Res. 37:675-678(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ACADMD 115-GLY-CYS-116 DEL.
    24. "A novel mutation in medium chain acyl-CoA dehydrogenase causes sudden neonatal death."
      Brackett J.C., Sims H.F., Steiner R.D., Nunge M., Zimmerman E.M., Demartinville B., Rinaldo P., Slaugh R., Strauss A.W.
      J. Clin. Invest. 94:1477-1483(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ACADMD ARG-195.
    25. "The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: is there correlation between genotype and phenotype?"
      Andresen B.S., Bross P., Udvari S., Kirk J., Gray G., Kmoch S., Chamoles N., Knudsen I., Winter V., Wilcken B., Yokota I., Hart K., Packman S., Harpey J.P., Saudubray J.-M., Hale D.E., Bolund L., Koelvraa S., Gregersen N.
      Hum. Mol. Genet. 6:695-707(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ACADMD TYR-116; ALA-193 AND CYS-352.
    26. "Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site."
      Kuchler B., Abdel-Ghany A.G., Bross P., Nandy A., Rasched I., Ghisla S.
      Biochem. J. 337:225-230(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT ACADMD ALA-193.
    27. "Identification of a novel mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency."
      Yang B.-Z., Ding J.-H., Zhou C., Dimachkie M.M., Sweetman L., Dasouki M.J., Wilkinson J., Roe C.R.
      Mol. Genet. Metab. 69:259-262(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ACADMD LEU-206 AND GLU-329.
    28. "Medium-chain acyl-CoA dehydrogenase (MCAD) mutations identified by MS/MS-based prospective screening of newborns differ from those observed in patients with clinical symptoms: identification and characterization of a new, prevalent mutation that results in mild MCAD deficiency."
      Andresen B.S., Dobrowolski S.F., O'Reilly L., Muenzer J., McCandless S.E., Frazier D.M., Udvari S., Bross P., Knudsen I., Banas R., Chace D.H., Engel P.C., Naylor E.W., Gregersen N.
      Am. J. Hum. Genet. 68:1408-1418(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ACADMD HIS-67; THR-78; ILE-121 AND ARG-310.
    29. Cited for: VARIANT ACADMD LEU-245.
    30. "Compound heterozygosity in four asymptomatic siblings with medium-chain acyl-CoA dehydrogenase deficiency."
      Albers S., Levy H.L., Irons M., Strauss A.W., Marsden D.
      J. Inherit. Metab. Dis. 24:417-418(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ACADMD THR-281 AND GLU-329.
    31. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-132.

    Entry informationi

    Entry nameiACADM_HUMAN
    AccessioniPrimary (citable) accession number: P11310
    Secondary accession number(s): Q5T4U4, Q9NYF1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 176 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.
    Utilizes the electron transfer flavoprotein (ETF) as electron acceptor that transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3