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A0A7K6X951 · A0A7K6X951_9PASE

  • Protein
    Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
  • Gene
    Acadm_0
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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. 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. Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). 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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

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

Type
IDPosition(s)Description
Binding site161-170FAD (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site194-196FAD (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site309-311FAD (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site319-320FAD (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site377-381FAD (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Active site404Proton acceptor
Binding site406-408FAD (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Componentmitochondrial matrix
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionmedium-chain fatty acyl-CoA dehydrogenase activity
Biological Processfatty acid beta-oxidation
Biological Processmedium-chain fatty acid catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      Acadm_0
    • ORF names
      PROCAF_R10257

Organism names

  • Taxonomic identifier
  • Strain
    • B10K-UC-030-53
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Telluraves > Australaves > Passeriformes > Passeroidea > Nectariniidae > Promerops

Accessions

  • Primary accession
    A0A7K6X951

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain6-60Acyl-CoA dehydrogenase/oxidase N-terminal
Domain99-154Acyl-CoA dehydrogenase/oxidase N-terminal
Domain160-258Acyl-CoA oxidase/dehydrogenase middle
Domain270-417Acyl-CoA dehydrogenase/oxidase C-terminal

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    424
  • Mass (Da)
    46,877
  • Last updated
    2021-04-07 v1
  • MD5 Checksum
    52D2A73AF3E18517E31FFA164FFC3889
FSTELTDEQKEFQATARKFALEEIIPAAAQYDRTGEYPVPLIKRAWELGLMNSHIPESCGDRPCWVFLTDLVYLVSKPEFLQQSLRIMGRFESRVAFKGGLGLGTFEACLITEELAYGCTGVQTAIEANSLGQMPVIIAGNEQQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGLRTRAERKGDEYVINGQKMWITNGGKANWYFLLARTDPDPRAPASKAFTGFIVEANSPGIQIGRKELNMGQRCSDTRGIVFEEVRVPKENVLIAEGAGFKIAMGAFDRTRPPVAAGAVGLARRALDEATRYALERKTFGKPIVEHQAVAFLLAEMAMKVELARLGYQRAAWEVDAGHRNTFYASIAKAFAGDVANQVATDAVQIFGGNGFNTEYPVEKLMRDAKIYQIYEGTAQIQRVIIAREHLGRYKA

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue424

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VZSE01002773
EMBL· GenBank· DDBJ
NWX55777.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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