Q9VVU1 · Q9VVU1_DROME

  • Protein
    Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
  • Gene
    GH07925p
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

Catalytic activity

  • (2R)-2-methylbutanoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = ethylacryloyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.
  • (2S)-2-methylbutanoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.
  • 2-methylbutanoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.
    EC:1.3.8.5 (UniProtKB | ENZYME | Rhea)
  • 2-methylpropanoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = (2E)-2-methylpropenoyl-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+ + oxidized [electron-transfer flavoprotein] + valproyl-CoA = (2E)-2-propylpent-2-enoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.
  • butanoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = (2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein]
    This reaction proceeds in the forward direction.

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Pathway

Amino-acid degradation; L-isoleucine degradation.
Lipid metabolism; mitochondrial fatty acid beta-oxidation.

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmitochondrion
Molecular Function2-methylbutanoyl-CoA dehydrogenase activity
Molecular Functionacyl-CoA dehydrogenase activity
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionshort-chain fatty acyl-CoA dehydrogenase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
  • EC number
  • Alternative names
    • 2-methyl branched chain acyl-CoA dehydrogenase
    • 2-methylbutyryl-coenzyme A dehydrogenase

Gene names

    • Name
      GH07925p
    • Synonyms
      CG 3902
      , CG18168
      , CG3902-RA
      , CT12987
      , Dmel\CG3902
    • ORF names
      CG3902
      , Dmel_CG3902

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    Q9VVU1

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain38-148Acyl-CoA dehydrogenase/oxidase N-terminal
Domain153-248Acyl-CoA oxidase/dehydrogenase middle
Domain260-406Acyl-CoA dehydrogenase/oxidase C-terminal

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    414
  • Mass (Da)
    45,366
  • Last updated
    2000-05-01 v1
  • Checksum
    97736FBADD20E767
MMNSLKKLPVRMLANAARQQSAAMSSATGLPPPLTFLTDDEKMMKETVAKLAQEQIQPLVKKMDFEHKFDPSVVKAVFENGLMGIEIDTELGGSGCNFMTNIVVVEELSKIDPAVAAFVDIHNTLVNSLMIKFGNAEQKAKYLPKLAQEYAGSFALTEPGAGSDAFSLKTVAKKDGSHYVINGSKMWISNSDVAGVFLIFANAKPEDGYRGITTFIVDRETPGLIVNKPEDKLGIRASGTCQLTFDNVRVPEENILGTFGHGYKYAAGFLNEGRIGIAAQMVGLAQGTFDATIPYLLERKQFGDAIYNFQSMQHQIATVATEIEAARLMTYNAARLQEQGVPFQKEAAMAKYYASEVAQRAAIKCVDWMGGVGFTRDFPQEKYYRDVKIGAIYEGTTNMQLSTIAKCIKKDYAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE014296
EMBL· GenBank· DDBJ
AAF49216.1
EMBL· GenBank· DDBJ
Genomic DNA
BT044429
EMBL· GenBank· DDBJ
ACH92494.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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