P41367 · ACADM_PIG
- ProteinMedium-chain specific acyl-CoA dehydrogenase, mitochondrial
- GeneACADM
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids421 (go to sequence)
- Protein existenceEvidence at protein 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 (PubMed:3233192).
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:3233192).
Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).
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 (By similarity).
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:3233192).
Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).
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 (By similarity).
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: YCVTEPGAGS | ||||||
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: QVFGG | ||||||
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 | axon | |
Cellular Component | cytoplasm | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrial membrane | |
Cellular Component | mitochondrion | |
Molecular Function | acyl-CoA dehydrogenase activity | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | identical protein binding | |
Molecular Function | medium-chain fatty acyl-CoA dehydrogenase activity | |
Biological Process | cardiac muscle cell differentiation | |
Biological Process | carnitine biosynthetic process | |
Biological Process | carnitine metabolic process, CoA-linked | |
Biological Process | fatty acid beta-oxidation | |
Biological Process | fatty acid beta-oxidation using acyl-CoA dehydrogenase | |
Biological Process | glycogen biosynthetic process | |
Biological Process | liver development | |
Biological Process | medium-chain fatty acid catabolic process | |
Biological Process | post-embryonic development | |
Biological Process | regulation of gluconeogenesis | |
Biological Process | response to cold | |
Biological Process | response to starvation |
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
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus
Accessions
- Primary accessionP41367
- 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: MAAMFRRSCRVLRSLSHFGWRSQHT | ||||||
Chain | PRO_0000000505 | 26-421 | Medium-chain specific acyl-CoA dehydrogenase, mitochondrial | |||
Sequence: KAVPQCEPGSGFSFELTEQQKEFQATARKFAREEIIPVAAEYDRTGEYPVPLLKRAWELGLMNTHIPESFGGLGLGIIDSCLITEELAYGCTGVQTAIEANTLGQVPLIIGGNYQQQKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPASKAFTGFIVEADTPGVQIGRKEINMGQRCSDTRGIVFEDVRVPKENVLTGEGAGFKIAMGTFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLLAEHQGISFLLADMAMKVELARLSYQRAAWEIDSGRRNTYYASIAKAYAADIANQLATDAVQVFGGNGFNTEYPVEKLMRDAKIYQIYEGTAQIQRIIIAREHIGRYKN | ||||||
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
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length421
- Mass (Da)46,485
- Last updated2007-05-29 v3
- Checksum73BC66092D5E02CB
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A4X1UK62 | A0A4X1UK62_PIG | ACADM | 394 | ||
A0A2C9F350 | A0A2C9F350_PIG | ACADM | 416 | ||
A0A5G2R006 | A0A5G2R006_PIG | ACADM | 384 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 8 | in Ref. 1; AAA83759 | ||||
Sequence: S → G | ||||||
Sequence conflict | 40 | in Ref. 1; AAA83759 | ||||
Sequence: E → K | ||||||
Sequence conflict | 283 | in Ref. 1; AAA83759 | ||||
Sequence: P → S | ||||||
Sequence conflict | 305 | in Ref. 1; AAA83759 | ||||
Sequence: E → G | ||||||
Sequence conflict | 331 | in Ref. 1; AAA83759 | ||||
Sequence: E → D |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U40845 EMBL· GenBank· DDBJ | AAA83759.1 EMBL· GenBank· DDBJ | mRNA | ||
AY705916 EMBL· GenBank· DDBJ | AAW30430.1 EMBL· GenBank· DDBJ | mRNA |