Q3L887 · FADE5_MYCS2
- ProteinBroad-specificity linear acyl-CoA dehydrogenase FadE5
- GenefadE5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids611 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acyl-CoA dehydrogenase that exhibits broad specificity for linear acyl-CoA substrates, with a preference for long-chain substrates.
Catalytic activity
- a long-chain 2,3-saturated fatty acyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]
- H+ + octadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-octadecenoyl-CoA + reduced [electron-transfer flavoprotein]
- H+ + hexadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer flavoprotein]
- dodecanoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = (2E)-dodecenoyl-CoA + reduced [electron-transfer flavoprotein]
- decanoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = (2E)-decenoyl-CoA + reduced [electron-transfer flavoprotein]
- H+ + hexanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]
- butanoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = (2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein]
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
285.9 μM | butanoyl-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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 162-165 | FAD (UniProtKB | ChEBI) | ||||
Sequence: MVLT | ||||||
Binding site | 171 | a 2,3-saturated acyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 171 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 198 | FAD (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 224-225 | a 2,3-saturated acyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: TK | ||||||
Binding site | 301 | a 2,3-saturated acyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 326 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 338 | a 2,3-saturated acyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 420-424 | FAD (UniProtKB | ChEBI) | ||||
Sequence: QTLGG | ||||||
Active site | 447 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 447 | a 2,3-saturated acyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 449 | FAD (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 456 | a 2,3-saturated acyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 460-461 | a 2,3-saturated acyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: RK |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | long-chain fatty acyl-CoA dehydrogenase activity | |
Molecular Function | medium-chain fatty acyl-CoA dehydrogenase activity | |
Molecular Function | short-chain fatty acyl-CoA dehydrogenase activity | |
Biological Process | fatty acid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBroad-specificity linear acyl-CoA dehydrogenase FadE5
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycolicibacterium
Accessions
- Primary accessionQ3L887
- Secondary accessions
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 447 | Loss of activity. | ||||
Sequence: E → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000452497 | 1-611 | Broad-specificity linear acyl-CoA dehydrogenase FadE5 | |||
Sequence: MSHYKSNVRDQVFNLFEVFGVDKVLGADKFSDLDADTAREMLTEIARLAEGPIAESFVEGDRNPPVFDPETHTVTLPEGFKKSMRALFDGGWDKVGLAEHLGGIPMPRALQWALIEHILGANPAAYMYAMGPGMSEIFYNNGTDEQKKWATIAAERGWGATMVLTEPDAGSDVGAGRTKAVQQPDGTWHIEGVKRFITSADSDDLFENIMHLVLARPEGAGPGTKGLSLFFVPKFHFDHETGEIGERNGVFVTNVEHKMGLKVSATCELSLGQHGIPAVGWLVGEVHNGIAQMFDVIEQARMMVGTKAIATLSTGYLNALEYAKERVQGADMTQMTDKTAPRVTITHHPDVRRSLMTQKAYAEGLRAIYLYTATFQDAEVAQAVHGVDGDLAARVNDLLLPIVKGFGSETAYAKLTESLQTLGGSGFLQDYPIEQYIRDSKIDSLYEGTTAIQAQDFFFRKIIRDKGQALAYVAGEIEQFIKNENGNGRLKTERELLATALADVQGMAASLTGYLMAAQEDAASIYKVGLGSVRFLMAVGDLLSGWLLARQAAVAIEKLDAGATGADKSFYEGKIAAASFFAKNMLPLLTSTRQIIENLDNDVMELDEAAF |
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length611
- Mass (Da)66,532
- Last updated2005-11-08 v1
- Checksum41D1ABFE887E0206
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |