Q3SZB4 · ACADM_BOVIN
- ProteinMedium-chain specific acyl-CoA dehydrogenase, mitochondrial
- GeneACADM
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids421 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Medium-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. 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. Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). Among the different mitochondrial acyl-CoA dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 6 to 12 carbons long primary chains.
Catalytic activity
- a medium-chain 2,3-saturated fatty acyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]This reaction proceeds in the forward direction.
- H+ + oxidized [electron-transfer flavoprotein] + pentanoyl-CoA = (2E)-pentenoyl-CoA + reduced [electron-transfer flavoprotein]This reaction proceeds in the forward direction.
- H+ + hexanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]This reaction proceeds in the forward direction.
- H+ + octanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-octenoyl-CoA + reduced [electron-transfer flavoprotein]This reaction proceeds in the forward direction.
- decanoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = (2E)-decenoyl-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.
Cofactor
Pathway
Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 158-167 | FAD (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: YCVTEPVAGS | ||||||
Binding site | 167 | octanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 191-193 | FAD (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: WIT | ||||||
Binding site | 216 | octanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 278 | octanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 281 | octanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 306-308 | FAD (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: RKT | ||||||
Binding site | 316-317 | FAD (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: HQ | ||||||
Binding site | 349 | octanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 351 | octanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 374-378 | FAD (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: QIFGG | ||||||
Active site | 401 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 401 | octanoyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 402-405 | FAD (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: GTAQ |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Molecular Function | acyl-CoA dehydrogenase activity | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | medium-chain fatty acyl-CoA dehydrogenase activity | |
Biological Process | fatty acid beta-oxidation | |
Biological Process | fatty acid beta-oxidation using acyl-CoA dehydrogenase | |
Biological Process | medium-chain fatty acid catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMedium-chain specific acyl-CoA dehydrogenase, mitochondrial
- EC number
- Short namesMCAD
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionQ3SZB4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-25 | Mitochondrion | ||||
Sequence: MIALFRRSCGVLRSLSHFDWRSQHT | ||||||
Chain | PRO_0000281995 | 26-421 | Medium-chain specific acyl-CoA dehydrogenase, mitochondrial | |||
Sequence: KTALQREPGSGFSFEFTEQQKEFQATARKFAREEIIPLAAEYDKTGEYPVPLIKRAWELGLMNTHIPESCGGLGLGTFDSCLISEELAYGCTGVQTAIEANSLGQMPVIIAGNDQQQKKYLGRMTEEPLMCAYCVTEPVAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPASKAFTGFIVEADTPGVQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAAAVGLAQRALDEATKYALERKTFGKLLIEHQGISFLLAEMAMKVELARLSYQRAAWEVDSGRRNTYYASIAKAYAGDIANQLASDAVQIFGGNGFNTEYPVEKLMRDAKIYQIYEGTAQIQRLIIAREHIGRYKK | ||||||
Modified residue | 69 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 69 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 79 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 179 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 212 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 212 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 217 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 217 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 259 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 259 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 271 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 271 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 279 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 301 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 351 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Acetylated. Could occur at proximity of the cofactor-binding sites and reduce the catalytic activity. Could be deacetylated by SIRT3.
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Homotetramer. Interacts with the heterodimeric electron transfer flavoprotein ETF.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length421
- Mass (Da)46,573
- Last updated2005-10-11 v1
- ChecksumC43979D54E7A3A8D
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AAA9SG93 | A0AAA9SG93_BOVIN | ACADM | 389 | ||
A0AAA9TBT5 | A0AAA9TBT5_BOVIN | ACADM | 425 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
EU009460 EMBL· GenBank· DDBJ | ABS70460.1 EMBL· GenBank· DDBJ | mRNA | ||
BC102989 EMBL· GenBank· DDBJ | AAI02990.1 EMBL· GenBank· DDBJ | mRNA |