A0A7J7FC18 · A0A7J7FC18_DICBM
- ProteinIsovaleryl-CoA dehydrogenase, mitochondrial
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids459 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- 3-methylbutanoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = 3-methyl-(2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein]
- H+ + hexanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]
- H+ + oxidized [electron-transfer flavoprotein] + pentanoyl-CoA = (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 | 198-207 | FAD (UniProtKB | ChEBI) | ||||
Sequence: LAMSESNAGS | ||||||
Binding site | 207 | substrate | ||||
Sequence: S | ||||||
Binding site | 231-233 | FAD (UniProtKB | ChEBI) | ||||
Sequence: WIT | ||||||
Binding site | 255-256 | substrate | ||||
Sequence: SR | ||||||
Binding site | 310 | substrate | ||||
Sequence: Y | ||||||
Binding site | 317-320 | substrate | ||||
Sequence: DLER | ||||||
Active site | 319 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 345 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 356 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 413-417 | FAD (UniProtKB | ChEBI) | ||||
Sequence: QCFGG | ||||||
Binding site | 440-441 | substrate | ||||
Sequence: AG | ||||||
Binding site | 442-444 | FAD (UniProtKB | ChEBI) | ||||
Sequence: TSE |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | isovaleryl-CoA dehydrogenase activity | |
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
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Rhinocerotidae > Diceros
Accessions
- Primary accessionA0A7J7FC18
Proteomes
PTM/Processing
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 46-79 | Acyl-CoA dehydrogenase/oxidase N-terminal | ||||
Sequence: SEEQKQLRQTVAKFLQDHLAPHAQEIDHSNEFKN | ||||||
Region | 75-94 | Disordered | ||||
Sequence: NEFKNLRVSHEAHTGGTGGQ | ||||||
Domain | 106-193 | Acyl-CoA dehydrogenase/oxidase N-terminal | ||||
Sequence: AWKGSHSLLEFWKQLGKLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGTHSNLCLNQIVRNGNEAQKEKYLPKLISGE | ||||||
Domain | 197-294 | Acyl-CoA oxidase/dehydrogenase middle | ||||
Sequence: ALAMSESNAGSDVVSMKLKAEKKGDHYILNGNKFWITNGPDADILIVYAKTDLAAVPASRGITAFIVEKDMPGFSTSKKLDKLGMRGSNTCELIFEDC | ||||||
Domain | 307-453 | Acyl-CoA dehydrogenase/oxidase C-terminal | ||||
Sequence: KGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHMREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTSKDCAAVILYSAECATQVALDGIQCFGGNGXXXDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRA |
Sequence similarities
Belongs to the acyl-CoA dehydrogenase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length459
- Mass (Da)49,700
- Last updated2021-04-07 v1
- Checksum81D8C51E55CD2511
Keywords
- Technical term