P15650 · ACADL_RAT
- ProteinLong-chain specific acyl-CoA dehydrogenase, mitochondrial
- GeneAcadl
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids430 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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:3968063).
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:3968063).
Among the different mitochondrial acyl-CoA dehydrogenases, long-chain specific acyl-CoA dehydrogenase can act on saturated and unsaturated acyl-CoAs with 6 to 24 carbons with a preference for 8 to 18 carbons long primary chains (PubMed:15466478, PubMed:3968063).
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:3968063).
Among the different mitochondrial acyl-CoA dehydrogenases, long-chain specific acyl-CoA dehydrogenase can act on saturated and unsaturated acyl-CoAs with 6 to 24 carbons with a preference for 8 to 18 carbons long primary chains (PubMed:15466478, PubMed:3968063).
Catalytic activity
- a long-chain 2,3-saturated fatty acyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-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.
- H+ + octadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-octadecenoyl-CoA + reduced [electron-transfer flavoprotein]This reaction proceeds in the forward direction.
- (5E)-tetradecenoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = (2E,5E)-tetradecadienoyl-CoA + reduced [electron-transfer flavoprotein]This reaction proceeds in the forward direction.
- (5Z)-tetradecenoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = (2E,5Z)-tetradecadienoyl-CoA + reduced [electron-transfer flavoprotein]This reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = (2E,9Z)-octadecadienoyl-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.
- 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]This reaction proceeds in the forward direction.
- H+ + oxidized [electron-transfer flavoprotein] + tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + reduced [electron-transfer flavoprotein]This reaction proceeds in the forward direction.
Cofactor
Activity regulation
Inhibited by crotonyl-CoA, 2-octenoyl-CoA and 2-hexadecenoyl-CoA.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
123 μM | octanoyl-CoA | 8.0 | 32 | |||
24.3 μM | decanoyl-CoA | 8.0 | 32 | |||
9 μM | dodecanoyl-CoA | 8.0 | 32 | |||
7.4 μM | tetradecanoyl-CoA | 8.0 | 32 | |||
2.5 μM | hexadecanoyl-CoA | 8.0 | 32 | |||
5.4 μM | octadecanoyl-CoA | 8.0 | 32 | |||
6.5 μM | (9Z)-octadecenoyl-CoA | 8.0 | 32 | |||
0.41 μM | tetradecanoyl-CoA | |||||
0.4 μM | (5Z)-tetradecenoyl-CoA | |||||
1.6 μM | (5E)-tetradecenoyl-CoA |
pH Dependence
Optimum pH is 8.0.
Pathway
Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 170-179 | FAD (UniProtKB | ChEBI) | ||||
Sequence: IAMTEPGAGS | ||||||
Binding site | 179 | substrate | ||||
Sequence: S | ||||||
Binding site | 203-205 | FAD (UniProtKB | ChEBI) | ||||
Sequence: FIT | ||||||
Binding site | 227-228 | substrate | ||||
Sequence: AH | ||||||
Binding site | 282 | substrate | ||||
Sequence: Y | ||||||
Binding site | 289-292 | substrate | ||||
Sequence: PQER | ||||||
Active site | 291 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 317 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 328 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 385-389 | FAD (UniProtKB | ChEBI) | ||||
Sequence: QLHGG | ||||||
Binding site | 412-413 | substrate | ||||
Sequence: GG | ||||||
Binding site | 414-416 | FAD (UniProtKB | ChEBI) | ||||
Sequence: TNE |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameLong-chain specific acyl-CoA dehydrogenase, mitochondrial
- EC number
- Short namesLCAD
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 accessionP15650
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-30 | Mitochondrion | ||||
Sequence: MAARLLLRSLRVLSARSATLPPPSARCSHS | ||||||
Chain | PRO_0000000513 | 31-430 | Long-chain specific acyl-CoA dehydrogenase, mitochondrial | |||
Sequence: GAEARLETPSAKKLTDIGIRRIFSSEHDIFRESVRKFFQEEVIPYHEEWEKAGEVSRELWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYSNCTGPGFSLHSDIVMPYIANYGTKEQIEQFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSDLVIVVAVTNREARSPAHGISLFLVENGMKGFIKGKKLHKMGMKAQDTAELFFEDVRLPASALLGEENKGFYYLMQELPQERLLIADLAISACEFMFEETRNYVRQRKAFGKTVAHIQTVQHKLAELKTNICVTRAFVDSCLQLHETKRLDSASASMAKYWASELQNTVAYQCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQIVSDS | ||||||
Modified residue | 42 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 54 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 55 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 66 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 66 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 81 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 81 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 92 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 95 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 165 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 191 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 240 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 254 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 254 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 279 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 279 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 318 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 322 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 322 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 358 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 362 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Acetylation at Lys-318 and Lys-322 in proximity of the cofactor-binding sites strongly reduces catalytic activity. These sites are deacetylated by SIRT3.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length430
- Mass (Da)47,873
- Last updated1990-04-01 v1
- ChecksumBEE1C7E0FDD84D2E
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6GMH0 | A0A8I6GMH0_RAT | Acadl | 406 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J05029 EMBL· GenBank· DDBJ | AAA40668.1 EMBL· GenBank· DDBJ | mRNA | ||
L11276 EMBL· GenBank· DDBJ | AAA41514.1 EMBL· GenBank· DDBJ | mRNA | ||
BC062006 EMBL· GenBank· DDBJ | AAH62006.1 EMBL· GenBank· DDBJ | mRNA |