R4FP64 · R4FP64_RHOPR
- ProteinIsovaleryl-CoA dehydrogenase, mitochondrial
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids420 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Catalyzes the conversion of isovaleryl-CoA/3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA as an intermediate step in the leucine (Leu) catabolic pathway. To a lesser extent, is also able to catalyze the oxidation of other saturated short-chain acyl-CoA thioesters as pentanoyl-CoA, hexenoyl-CoA and butenoyl-CoA.
Catalytic activity
- 3-methylbutanoyl-CoA + oxidized [electron-transfer flavoprotein] + H+ = 3-methyl-(2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein]
- hexanoyl-CoA + oxidized [electron-transfer flavoprotein] + H+ = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]
- pentanoyl-CoA + oxidized [electron-transfer flavoprotein] + H+ = (2E)-pentenoyl-CoA + reduced [electron-transfer flavoprotein]
Cofactor
Pathway
Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 1/3.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 157-166 | FAD (UniProtKB | ChEBI) | |||
Binding site | 166 | substrate | |||
Binding site | 190-192 | FAD (UniProtKB | ChEBI) | |||
Binding site | 269 | substrate | |||
Active site | 278 | Proton acceptor | |||
Binding site | 304 | FAD (UniProtKB | ChEBI) | |||
Binding site | 315 | FAD (UniProtKB | ChEBI) | |||
Binding site | 372-376 | FAD (UniProtKB | ChEBI) | |||
Binding site | 399-400 | substrate | |||
Binding site | 401-403 | FAD (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Molecular Function | 3-methylbutanoyl-CoA dehydrogenase activity | |
Molecular Function | flavin adenine dinucleotide binding | |
Biological Process | L-leucine catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIsovaleryl-CoA dehydrogenase, mitochondrial
- EC number
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Hemiptera > Heteroptera > Panheteroptera > Cimicomorpha > Reduviidae > Triatominae > Rhodnius
Accessions
- Primary accessionR4FP64
Organism-specific databases
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 38-152 | Acyl-CoA dehydrogenase/oxidase N-terminal | |||
Domain | 156-253 | Acyl-CoA oxidase/dehydrogenase middle | |||
Domain | 265-413 | Acyl-CoA dehydrogenase/oxidase C-terminal | |||
Sequence similarities
Belongs to the acyl-CoA dehydrogenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length420
- Mass (Da)46,346
- Last updated2013-06-26 v1
- MD5 Checksum05BE13857CDC07F19E2C4AF9A8DC75E4
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GAHY01001039 EMBL· GenBank· DDBJ | JAA76471.1 EMBL· GenBank· DDBJ | mRNA |