P41367 · ACADM_PIG

  • Protein
    Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
  • Gene
    ACADM
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Medium-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (PubMed:3233192).
The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (PubMed:3233192).
Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).
Among the different mitochondrial acyl-CoA dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 6 to 12 carbons long primary chains (By similarity).

Catalytic activity

  • a medium-chain 2,3-saturated fatty acyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.
    EC:1.3.8.7 (UniProtKB | ENZYME | Rhea)
  • H+ + oxidized [electron-transfer flavoprotein] + pentanoyl-CoA = (2E)-pentenoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.
  • H+ + hexanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.
  • H+ + octanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-octenoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.
  • decanoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = (2E)-decenoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.
  • dodecanoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = (2E)-dodecenoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.
  • H+ + oxidized [electron-transfer flavoprotein] + tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.
  • H+ + hexadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Pathway

Lipid metabolism; mitochondrial fatty acid beta-oxidation.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site158-167FAD (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site167octanoyl-CoA (UniProtKB | ChEBI)
Binding site191-193FAD (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site216octanoyl-CoA (UniProtKB | ChEBI)
Binding site278octanoyl-CoA (UniProtKB | ChEBI)
Binding site281octanoyl-CoA (UniProtKB | ChEBI)
Binding site306-308FAD (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site316-317FAD (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site349octanoyl-CoA (UniProtKB | ChEBI)
Binding site351octanoyl-CoA (UniProtKB | ChEBI)
Binding site374-378FAD (UniProtKB | ChEBI); ligand shared between dimeric partners
Active site401Proton acceptor
Binding site401octanoyl-CoA (UniProtKB | ChEBI)
Binding site402-405FAD (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Componentaxon
Cellular Componentcytoplasm
Cellular Componentmitochondrial matrix
Cellular Componentmitochondrial membrane
Cellular Componentmitochondrion
Molecular Functionacyl-CoA dehydrogenase activity
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionidentical protein binding
Molecular Functionmedium-chain fatty acyl-CoA dehydrogenase activity
Biological Processcardiac muscle cell differentiation
Biological Processcarnitine biosynthetic process
Biological Processcarnitine metabolic process, CoA-linked
Biological Processfatty acid beta-oxidation
Biological Processfatty acid beta-oxidation using acyl-CoA dehydrogenase
Biological Processglycogen biosynthetic process
Biological Processliver development
Biological Processmedium-chain fatty acid catabolic process
Biological Processpost-embryonic development
Biological Processregulation of gluconeogenesis
Biological Processresponse to cold
Biological Processresponse to starvation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
  • EC number
  • Short names
    MCAD

Gene names

    • Name
      ACADM

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus

Accessions

  • Primary accession
    P41367
  • Secondary accessions
    • Q58XQ3

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for transit peptide, chain, modified residue.

TypeIDPosition(s)Description
Transit peptide1-25Mitochondrion
ChainPRO_000000050526-421Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Modified residue79N6-acetyllysine
Modified residue179N6-succinyllysine
Modified residue212N6-acetyllysine; alternate
Modified residue212N6-succinyllysine; alternate
Modified residue217N6-acetyllysine; alternate
Modified residue217N6-succinyllysine; alternate
Modified residue259N6-acetyllysine; alternate
Modified residue259N6-succinyllysine; alternate
Modified residue271N6-acetyllysine; alternate
Modified residue271N6-succinyllysine; alternate
Modified residue279N6-acetyllysine
Modified residue301N6-acetyllysine
Modified residue351Phosphothreonine

Post-translational modification

Acetylated. Could occur at proximity of the cofactor-binding sites and reduce the catalytic activity. Could be deacetylated by SIRT3.

Keywords

Proteomic databases

Interaction

Subunit

Homotetramer (PubMed:12966080).
Interacts with the heterodimeric electron transfer flavoprotein ETF (By similarity).

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    421
  • Mass (Da)
    46,485
  • Last updated
    2007-05-29 v3
  • Checksum
    73BC66092D5E02CB
MAAMFRRSCRVLRSLSHFGWRSQHTKAVPQCEPGSGFSFELTEQQKEFQATARKFAREEIIPVAAEYDRTGEYPVPLLKRAWELGLMNTHIPESFGGLGLGIIDSCLITEELAYGCTGVQTAIEANTLGQVPLIIGGNYQQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPASKAFTGFIVEADTPGVQIGRKEINMGQRCSDTRGIVFEDVRVPKENVLTGEGAGFKIAMGTFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLLAEHQGISFLLADMAMKVELARLSYQRAAWEIDSGRRNTYYASIAKAYAADIANQLATDAVQVFGGNGFNTEYPVEKLMRDAKIYQIYEGTAQIQRIIIAREHIGRYKN

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A4X1UK62A0A4X1UK62_PIGACADM394
A0A2C9F350A0A2C9F350_PIGACADM416
A0A5G2R006A0A5G2R006_PIGACADM384

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict8in Ref. 1; AAA83759
Sequence conflict40in Ref. 1; AAA83759
Sequence conflict283in Ref. 1; AAA83759
Sequence conflict305in Ref. 1; AAA83759
Sequence conflict331in Ref. 1; AAA83759

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U40845
EMBL· GenBank· DDBJ
AAA83759.1
EMBL· GenBank· DDBJ
mRNA
AY705916
EMBL· GenBank· DDBJ
AAW30430.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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