P45953 · ACADV_RAT
- ProteinVery long-chain specific acyl-CoA dehydrogenase, mitochondrial
- GeneAcadvl
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids655 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Very long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (PubMed:1730632, PubMed:8034667).
The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (PubMed:1730632, PubMed:8034667).
Among the different mitochondrial acyl-CoA dehydrogenases, very long-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 12 to 24 carbons long primary chains (PubMed:1730632).
The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (PubMed:1730632, PubMed:8034667).
Among the different mitochondrial acyl-CoA dehydrogenases, very long-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 12 to 24 carbons long primary chains (PubMed:1730632).
Catalytic activity
- a very-long-chain 2,3-saturated fatty acyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = a very-long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]This reaction proceeds in the forward direction.
- dodecanoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = (2E)-dodecenoyl-CoA + reduced [electron-transfer flavoprotein]This reaction proceeds in the forward direction.
- H+ + oxidized [electron-transfer flavoprotein] + tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + reduced [electron-transfer flavoprotein]This reaction proceeds in the forward direction.
- H+ + hexadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer flavoprotein]This reaction proceeds in the forward direction.
- H+ + octadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-octadecenoyl-CoA + reduced [electron-transfer flavoprotein]This reaction proceeds in the forward direction.
- eicosanoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = (2E)-eicosenoyl-CoA + reduced [electron-transfer flavoprotein]This reaction proceeds in the forward direction.
- docosanoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = (2E)-docosenoyl-CoA + reduced [electron-transfer flavoprotein]
- H+ + oxidized [electron-transfer flavoprotein] + tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + reduced [electron-transfer flavoprotein]This reaction proceeds in the forward direction.
Cofactor
Pathway
Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 214-223 | FAD (UniProtKB | ChEBI) | ||||
Sequence: FCLTEPSSGS | ||||||
Binding site | 249-251 | FAD (UniProtKB | ChEBI) | ||||
Sequence: WIS | ||||||
Binding site | 461-463 | substrate | ||||
Sequence: FEG | ||||||
Active site | 462 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 464-466 | FAD (UniProtKB | ChEBI) | ||||
Sequence: TND | ||||||
Binding site | 562 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrial membrane | |
Cellular Component | mitochondrial nucleoid | |
Cellular Component | mitochondrion | |
Molecular Function | acyl-CoA dehydrogenase activity | |
Molecular Function | fatty-acyl-CoA binding | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | identical protein binding | |
Molecular Function | long-chain fatty acyl-CoA dehydrogenase activity | |
Molecular Function | very-long-chain fatty acyl-CoA dehydrogenase activity | |
Biological Process | epithelial cell differentiation | |
Biological Process | fatty acid beta-oxidation | |
Biological Process | fatty acid beta-oxidation using acyl-CoA dehydrogenase | |
Biological Process | fatty acid catabolic process | |
Biological Process | negative regulation of fatty acid biosynthetic process | |
Biological Process | negative regulation of fatty acid oxidation | |
Biological Process | regulation of cholesterol metabolic process | |
Biological Process | response to cold | |
Biological Process | temperature homeostasis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameVery long-chain specific acyl-CoA dehydrogenase, mitochondrial
- EC number
- Short namesVLCAD
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP45953
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-40 | Mitochondrion | ||||
Sequence: MQSARMTPSVGRQLLRLGARSSRSAALQGQPRPTSAQRLY | ||||||
Chain | PRO_0000000518 | 41-655 | Very long-chain specific acyl-CoA dehydrogenase, mitochondrial | |||
Sequence: ASEATQAVLEKPETLSSDASTREKPARAESKSFAVGMFKGQLTTDQVFPYPSVLNEGQTQFLKELVGPVARFFEEVNDPAKNDSLEKVEEDTLQGLKELGAFGLQVPSELGGLGLSNTQYARLAEIVGMHDLGVSVTLGAHQSIGFKGILLYGTKAQKEKYLPRVASGQALAAFCLTEPSSGSDVASIRSSAVPSPCGKYYTLNGSKIWISNGGLADIFTVFAKTPIKDAATGAVKEKITAFVVERSFGGVTHGLPEKKMGIKASNTSEVYFDGVKVPAENVLGEVGDGFKVAVNILNNGRFGMAATLAGTMKAIIAKAVDHATNRTQFGDKIHNFGVIQEKLARMAILQYVTESMAYMLSANMDQGFKDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDIRIFRIFEGTNDILRLFVALQGCMDKGKELTGLGNALKNPLGNVGLLIGEASKQLRRRTGIGSGLSLSGIVHPELSRSGELAVQALEQFATVVEAKLMKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGYPTAQHEKMLCDSWCIEAATRIRENMASLQSNPQQQELFRNFRSISKAMVENGGLVTSNPLRV | ||||||
Modified residue | 51 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 71 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 71 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 127 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 127 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 195 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 237 | S-nitrosocysteine | ||||
Sequence: C | ||||||
Modified residue | 239 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 239 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 268 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 276 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 276 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 278 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 278 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 298 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 316 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 331 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 331 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 372 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 482 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 482 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 517 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 522 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 550 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 556 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 556 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 639 | N6-succinyllysine | ||||
Sequence: K |
Post-translational modification
S-nitrosylation at Cys-237 in liver improves catalytic efficiency.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed (at protein level).
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-70 | Disordered | ||||
Sequence: MQSARMTPSVGRQLLRLGARSSRSAALQGQPRPTSAQRLYASEATQAVLEKPETLSSDASTREKPARAES | ||||||
Compositional bias | 23-42 | Polar residues | ||||
Sequence: RSAALQGQPRPTSAQRLYAS | ||||||
Region | 41-482 | Catalytic | ||||
Sequence: ASEATQAVLEKPETLSSDASTREKPARAESKSFAVGMFKGQLTTDQVFPYPSVLNEGQTQFLKELVGPVARFFEEVNDPAKNDSLEKVEEDTLQGLKELGAFGLQVPSELGGLGLSNTQYARLAEIVGMHDLGVSVTLGAHQSIGFKGILLYGTKAQKEKYLPRVASGQALAAFCLTEPSSGSDVASIRSSAVPSPCGKYYTLNGSKIWISNGGLADIFTVFAKTPIKDAATGAVKEKITAFVVERSFGGVTHGLPEKKMGIKASNTSEVYFDGVKVPAENVLGEVGDGFKVAVNILNNGRFGMAATLAGTMKAIIAKAVDHATNRTQFGDKIHNFGVIQEKLARMAILQYVTESMAYMLSANMDQGFKDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDIRIFRIFEGTNDILRLFVALQGCMDKGK | ||||||
Region | 483-516 | Membrane-anchoring | ||||
Sequence: ELTGLGNALKNPLGNVGLLIGEASKQLRRRTGIG |
Sequence similarities
Belongs to the acyl-CoA dehydrogenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length655
- Mass (Da)70,749
- Last updated1995-11-01 v1
- ChecksumE808EDEB0E4595D7
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q5M9H2 | Q5M9H2_RAT | Acadvl | 655 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 23-42 | Polar residues | ||||
Sequence: RSAALQGQPRPTSAQRLYAS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D30647 EMBL· GenBank· DDBJ | BAA06331.1 EMBL· GenBank· DDBJ | mRNA |