P21775 · THIKA_RAT
- Protein3-ketoacyl-CoA thiolase A, peroxisomal
- GeneAcaa1a
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids434 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Responsible for the thiolytic cleavage of straight chain 3-keto fatty acyl-CoAs (3-oxoacyl-CoAs) (PubMed:9325339).
Plays an important role in fatty acid peroxisomal beta-oxidation (PubMed:9325339).
Catalyzes the cleavage of short, medium, long, and very long straight chain 3-oxoacyl-CoAs (PubMed:9325339).
Medium chain straight 3-oxoacyl-CoAs are preferred substrates (PubMed:9325339).
Plays an important role in fatty acid peroxisomal beta-oxidation (PubMed:9325339).
Catalyzes the cleavage of short, medium, long, and very long straight chain 3-oxoacyl-CoAs (PubMed:9325339).
Medium chain straight 3-oxoacyl-CoAs are preferred substrates (PubMed:9325339).
Catalytic activity
- acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoAThis reaction proceeds in the backward direction.
- acetyl-CoA + hexanoyl-CoA = 3-oxooctanoyl-CoA + CoAThis reaction proceeds in the backward direction.
- 3-oxohexadecanedioyl-CoA + CoA = acetyl-CoA + tetradecanedioyl-CoAThis reaction proceeds in the forward direction.
- 3-oxo-(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + CoA = (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + acetyl-CoAThis reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
7.7 μM | acetoacetyl-CoA | |||||
9.1 μM | 3-oxooctanoyl-CoA | |||||
7.8 μM | 3-oxohexadecanoyl-CoA | |||||
3.4 μM | 3-oxohexadecanedioyl-CoA |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
26.8 μmol/min/mg | towards acetoacetyl-CoA | ||||
145 μmol/min/mg | towards 3-oxooctanoyl-CoA | ||||
14.3 μmol/min/mg | towards 3-oxohexadecanoyl-CoA | ||||
128 μmol/min/mg | towards 3-oxohexadecanedioyl-CoA |
pH Dependence
Optimum pH is 8 with acetoacetyl-CoA and 3-oxooctanoyl-CoA as substrates.
Pathway
Lipid metabolism; peroxisomal fatty acid beta-oxidation.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 133 | Acyl-thioester intermediate | ||||
Sequence: C | ||||||
Active site | 387 | Proton acceptor | ||||
Sequence: H | ||||||
Active site | 418 | Proton acceptor | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | peroxisome | |
Molecular Function | acetate CoA-transferase activity | |
Molecular Function | acetyl-CoA C-acetyltransferase activity | |
Molecular Function | acetyl-CoA C-acyltransferase activity | |
Molecular Function | acetyl-CoA C-myristoyltransferase activity | |
Molecular Function | palmitoyl-CoA oxidase activity | |
Biological Process | bile acid metabolic process | |
Biological Process | fatty acid beta-oxidation | |
Biological Process | fatty acid beta-oxidation using acyl-CoA oxidase | |
Biological Process | phenylacetate catabolic process | |
Biological Process | response to nutrient | |
Biological Process | response to steroid hormone | |
Biological Process | response to xenobiotic stimulus | |
Biological Process | very long-chain fatty acid metabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3-ketoacyl-CoA thiolase A, peroxisomal
- EC number
- Alternative names
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 accessionP21775
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Transported into peroxisomes following association with PEX7.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-36 | Peroxisome | ||||
Sequence: MSESVGRTSAMHRLQVVLGHLAGRPESSSALQAAPC | ||||||
Chain | PRO_0000034070 | 37-434 | 3-ketoacyl-CoA thiolase A, peroxisomal | |||
Sequence: SATFPQASASDVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSNRGNPGNISSRLLESDKARDCLIPMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDDKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQALYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAYGVVSMCIGTGMGAAAVFEYPGN | ||||||
Modified residue | 183 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 244 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Peroxisomal thiolase is markedly induced (at the level of transcription) by various hypolipidemic compounds in parallel with the other two enzymes of the peroxisomal beta-oxidation system.
Interaction
Subunit
Homodimer. Interacts (via PTS2-type peroxisomal targeting signal region) with PEX7; leading to its translocation into peroxisomes.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 11-36 | PTS2-type peroxisomal targeting signal | ||||
Sequence: MHRLQVVLGHLAGRPESSSALQAAPC |
Domain
The PTS2-type peroxisomal targeting signal, which mediates interaction with PEX7 and localization to peroxisomes, is cleaved following import into peroxisomes.
Sequence similarities
Belongs to the thiolase-like superfamily. Thiolase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P21775-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length434
- Mass (Da)44,839
- Last updated2021-02-10 v3
- Checksum85189FB6D294E135
P21775-2
- Name2
- Differences from canonical
- 344-434: LTVNDIDIFEINEAFASQALYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAYGVVSMCIGTGMGAAAVFEYPGN → PLLCGEAGNSCREGEPPGGCNSPGPPPGLHRSKAGGHAAQ
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AHC5 | A0A8I6AHC5_RAT | Acaa1a | 434 | ||
F1LPD6 | F1LPD6_RAT | Acaa1a | 428 | ||
A0A8I6AHJ8 | A0A8I6AHJ8_RAT | Acaa1a | 331 | ||
A0A8I6G309 | A0A8I6G309_RAT | Acaa1a | 383 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 39 | in Ref. 3; AAH89821 | ||||
Sequence: T → S | ||||||
Sequence conflict | 245 | in Ref. 3; AAH89821 | ||||
Sequence: G → S | ||||||
Alternative sequence | VSP_023746 | 344-434 | in isoform 2 | |||
Sequence: LTVNDIDIFEINEAFASQALYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAYGVVSMCIGTGMGAAAVFEYPGN → PLLCGEAGNSCREGEPPGGCNSPGPPPGLHRSKAGGHAAQ | ||||||
Sequence conflict | 409 | in Ref. 1; AAA41471 | ||||
Sequence: R → T |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M32801 EMBL· GenBank· DDBJ | AAA41471.1 EMBL· GenBank· DDBJ | mRNA | ||
D90058 EMBL· GenBank· DDBJ | BAA14106.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC089821 EMBL· GenBank· DDBJ | AAH89821.1 EMBL· GenBank· DDBJ | mRNA |