Q9DBK0 · ACO12_MOUSE
- ProteinAcetyl-coenzyme A thioesterase
- GeneAcot12
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids556 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Preferentially hydrolyzes acetyl-CoA.
Catalytic activity
- acetyl-CoA + H2O = acetate + CoA + H+This reaction proceeds in the forward direction.
- butanoyl-CoA + H2O = butanoate + CoA + H+This reaction proceeds in the forward direction.
- hexanoyl-CoA + H2O = hexanoate + CoA + H+This reaction proceeds in the forward direction.
Activity regulation
Allosterically regulated by ATP (activator) and ADP (inhibitor) (By similarity).
Cold labile, it dissociates into inactive monomers at low temperature (By similarity).
Cold labile, it dissociates into inactive monomers at low temperature (By similarity).
Pathway
Lipid metabolism; fatty acid metabolism.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | intercellular bridge | |
Cellular Component | nucleoplasm | |
Molecular Function | acetyl-CoA hydrolase activity | |
Molecular Function | ATP binding | |
Molecular Function | carboxylic ester hydrolase activity | |
Molecular Function | identical protein binding | |
Molecular Function | lipid binding | |
Biological Process | acetyl-CoA metabolic process | |
Biological Process | fatty acid metabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcetyl-coenzyme A thioesterase
- 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 > Mus > Mus
Accessions
- Primary accessionQ9DBK0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000053810 | 1-556 | Acetyl-coenzyme A thioesterase | |||
Sequence: MESMVAPGEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFSTSMEISIKVIVQDKFTGIQKLLCVAFSTFVAKPVGKEKVHLKPVLLQTEQEQVEHNLASERRKVRLQHENTFNNIMKESSRFSDSICNEEEGTATTMGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVEVGVRVEAFDCQEWAEGQGRHINSAFLIYNAVDDQEKLITFPRIQPISKDDFRRYQGAIARRRIRLGRKYVISHKKEVPLSAQWDISKKGSLSNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDAISVKVEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSRRKPLKDNNTYTVALRSVVLPSVPSSPQYIRSEVICAGFLIQAVDSNSCTVTYLNQMSDSILPYFAGNIGGWSKSIEEAAASCIKFIENATPDGLKSVL | ||||||
Modified residue | 34 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 97 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 160 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 229 | N6-succinyllysine | ||||
Sequence: K |
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-118 | HotDog ACOT-type 1 | ||||
Sequence: APGEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFSTSMEISIKVIVQDKFTGIQKLLCVAFSTFVAKPVG | ||||||
Domain | 180-295 | HotDog ACOT-type 2 | ||||
Sequence: MGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVEVGVRVEAFDCQEWAEGQGRHINSAFLIYNAVDDQ | ||||||
Domain | 327-536 | START | ||||
Sequence: GRKYVISHKKEVPLSAQWDISKKGSLSNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDAISVKVEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSRRKPLKDNNTYTVALRSVVLPSVPSSPQYIRSEVICAGFLIQAVDSNSCTVTYLNQMSDSILPYFAGNIGGWSKSIEEA |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length556
- Mass (Da)61,762
- Last updated2001-06-01 v1
- Checksum9FE9C487BBCBB812
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB078618 EMBL· GenBank· DDBJ | BAB84021.1 EMBL· GenBank· DDBJ | mRNA | ||
AK004905 EMBL· GenBank· DDBJ | BAB23658.1 EMBL· GenBank· DDBJ | mRNA | ||
AK034622 EMBL· GenBank· DDBJ | BAC28775.1 EMBL· GenBank· DDBJ | mRNA | ||
BC025852 EMBL· GenBank· DDBJ | AAH25852.1 EMBL· GenBank· DDBJ | mRNA |