Q9D404 · OXSM_MOUSE
- Protein3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- GeneOxsm
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids459 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function.
Catalytic activity
- a fatty acyl-[ACP] + H+ + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]This reaction proceeds in the forward direction.
- butanoyl-[ACP] + H+ + malonyl-[ACP] = 3-oxohexanoyl-[ACP] + CO2 + holo-[ACP]This reaction proceeds in the forward direction.
- H+ + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] + CO2 + holo-[ACP]This reaction proceeds in the forward direction.
- H+ + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] + CO2 + holo-[ACP]This reaction proceeds in the forward direction.
- decanoyl-[ACP] + H+ + malonyl-[ACP] = 3-oxododecanoyl-[ACP] + CO2 + holo-[ACP]This reaction proceeds in the forward direction.
- dodecanoyl-[ACP] + H+ + malonyl-[ACP] = 3-oxotetradecanoyl-[ACP] + CO2 + holo-[ACP]This reaction proceeds in the forward direction.
- H+ + malonyl-[ACP] + tetradecanoyl-[ACP] = 3-oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]This reaction proceeds in the forward direction.
Activity regulation
Inhibited by cerulenin.
Pathway
Lipid metabolism; fatty acid biosynthesis.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 209 | For beta-ketoacyl synthase activity | ||||
Sequence: C | ||||||
Active site | 348 | For beta-ketoacyl synthase activity | ||||
Sequence: H | ||||||
Active site | 385 | For beta-ketoacyl synthase activity | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Molecular Function | 3-oxoacyl-[acyl-carrier-protein] synthase activity | |
Biological Process | acyl-CoA metabolic process | |
Biological Process | fatty acid biosynthetic process | |
Biological Process | medium-chain fatty acid biosynthetic process | |
Biological Process | short-chain fatty acid biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- 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 accessionQ9D404
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-27 | Mitochondrion | ||||
Sequence: MLSKCLQHFLKATISHPYPASYSWLIS | ||||||
Chain | PRO_0000232661 | 28-459 | 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial | |||
Sequence: KHRFYGTVPAAMLRRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPRGPHEGQFNEENFVSKSDAKSMSSSTIMAVGAAELALKDSGWHPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSSNPDPKLACRPFHPERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAENRAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEGRCIGLTNSFGFGGTNATLCIAGM | ||||||
Modified residue | 109 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 109 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 113 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 174 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 174 | N6-succinyllysine; alternate | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 41-458 | Ketosynthase family 3 (KS3) | ||||
Sequence: RRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPRGPHEGQFNEENFVSKSDAKSMSSSTIMAVGAAELALKDSGWHPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSSNPDPKLACRPFHPERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAENRAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEGRCIGLTNSFGFGGTNATLCIAG |
Sequence similarities
Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length459
- Mass (Da)48,628
- Last updated2001-06-01 v1
- Checksum47F9733FBBF08BE1
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK016905 EMBL· GenBank· DDBJ | BAB30490.1 EMBL· GenBank· DDBJ | mRNA | ||
AK083617 EMBL· GenBank· DDBJ | BAC38969.1 EMBL· GenBank· DDBJ | mRNA | ||
AK084829 EMBL· GenBank· DDBJ | BAC39286.1 EMBL· GenBank· DDBJ | mRNA |