Q3L887 · FADE5_MYCS2

Function

function

Acyl-CoA dehydrogenase that exhibits broad specificity for linear acyl-CoA substrates, with a preference for long-chain substrates.

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
285.9 μMbutanoyl-CoA
kcat is 0.53 sec-1 with butanoyl-CoA as substrate.

Pathway

Lipid metabolism; fatty acid metabolism.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site162-165FAD (UniProtKB | ChEBI)
Binding site171a 2,3-saturated acyl-CoA (UniProtKB | ChEBI)
Binding site171FAD (UniProtKB | ChEBI)
Binding site198FAD (UniProtKB | ChEBI)
Binding site224-225a 2,3-saturated acyl-CoA (UniProtKB | ChEBI)
Binding site301a 2,3-saturated acyl-CoA (UniProtKB | ChEBI)
Binding site326FAD (UniProtKB | ChEBI)
Binding site338a 2,3-saturated acyl-CoA (UniProtKB | ChEBI)
Binding site420-424FAD (UniProtKB | ChEBI)
Active site447Proton acceptor
Binding site447a 2,3-saturated acyl-CoA (UniProtKB | ChEBI)
Binding site449FAD (UniProtKB | ChEBI)
Binding site456a 2,3-saturated acyl-CoA (UniProtKB | ChEBI)
Binding site460-461a 2,3-saturated acyl-CoA (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionlong-chain fatty acyl-CoA dehydrogenase activity
Molecular Functionmedium-chain fatty acyl-CoA dehydrogenase activity
Molecular Functionshort-chain fatty acyl-CoA dehydrogenase activity
Biological Processfatty acid metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Broad-specificity linear acyl-CoA dehydrogenase FadE5
  • Alternative names
    • Long-chain-acyl-CoA dehydrogenase
      (EC:1.3.8.8
      ) . EC:1.3.8.8 (UniProtKB | ENZYME | Rhea)
    • Medium-chain-acyl-CoA dehydrogenase
      (EC:1.3.8.7
      ) . EC:1.3.8.7 (UniProtKB | ENZYME | Rhea)
    • Short-chain-acyl-CoA dehydrogenase
      (EC:1.3.8.1
      ) . EC:1.3.8.1 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      fadE5
    • Ordered locus names
      MSMEG_0406
      , MSMEI_0396

Organism names

Accessions

  • Primary accession
    Q3L887
  • Secondary accessions
    • A0QPI1
    • I7FWC0

Proteomes

Phenotypes & Variants

Disruption phenotype

Disruption of the gene does not affect the growth rate, but mutant shows decreased resistance to ethambutol and streptomycin.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis447Loss of activity.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004524971-611Broad-specificity linear acyl-CoA dehydrogenase FadE5

Proteomic databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    611
  • Mass (Da)
    66,532
  • Last updated
    2005-11-08 v1
  • Checksum
    41D1ABFE887E0206
MSHYKSNVRDQVFNLFEVFGVDKVLGADKFSDLDADTAREMLTEIARLAEGPIAESFVEGDRNPPVFDPETHTVTLPEGFKKSMRALFDGGWDKVGLAEHLGGIPMPRALQWALIEHILGANPAAYMYAMGPGMSEIFYNNGTDEQKKWATIAAERGWGATMVLTEPDAGSDVGAGRTKAVQQPDGTWHIEGVKRFITSADSDDLFENIMHLVLARPEGAGPGTKGLSLFFVPKFHFDHETGEIGERNGVFVTNVEHKMGLKVSATCELSLGQHGIPAVGWLVGEVHNGIAQMFDVIEQARMMVGTKAIATLSTGYLNALEYAKERVQGADMTQMTDKTAPRVTITHHPDVRRSLMTQKAYAEGLRAIYLYTATFQDAEVAQAVHGVDGDLAARVNDLLLPIVKGFGSETAYAKLTESLQTLGGSGFLQDYPIEQYIRDSKIDSLYEGTTAIQAQDFFFRKIIRDKGQALAYVAGEIEQFIKNENGNGRLKTERELLATALADVQGMAASLTGYLMAAQEDAASIYKVGLGSVRFLMAVGDLLSGWLLARQAAVAIEKLDAGATGADKSFYEGKIAAASFFAKNMLPLLTSTRQIIENLDNDVMELDEAAF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY439015
EMBL· GenBank· DDBJ
AAU04876.1
EMBL· GenBank· DDBJ
Genomic DNA
CP000480
EMBL· GenBank· DDBJ
ABK75628.1
EMBL· GenBank· DDBJ
Genomic DNA
CP001663
EMBL· GenBank· DDBJ
AFP36877.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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