A0AA35J8B8 · A0AA35J8B8_SACUV
- ProteinFatty acid synthase subunit alpha
- GeneSUVC16G0500
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1887 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- a (3R)-hydroxyacyl-[ACP] + NADP+ = a 3-oxoacyl-[ACP] + NADPH + H+
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 1306 | For beta-ketoacyl synthase activity | |||
Binding site | 1772 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 1772-1774 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 1773 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 1774 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 1798 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 1808 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 1817-1833 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 1841-1844 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 1871-1873 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 1872 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 1873 | Mg2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | fatty acid synthase complex | |
Molecular Function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity | |
Molecular Function | 3-oxoacyl-[acyl-carrier-protein] synthase activity | |
Molecular Function | fatty acid synthase activity | |
Molecular Function | holo-[acyl-carrier-protein] synthase activity | |
Molecular Function | magnesium ion binding | |
Biological Process | long-chain fatty acid biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFatty acid synthase subunit alpha
- EC number
Including 2 domains:
- Recommended name3-oxoacyl-[acyl-carrier-protein] reductase
- EC number
- Recommended name3-oxoacyl-[acyl-carrier-protein] synthase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionA0AA35J8B8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 183 | O-(pantetheine 4'-phosphoryl)serine | |||
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 148-223 | Carrier | |||
Domain | 1124-1658 | Ketosynthase family 3 (KS3) | |||
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,887
- Mass (Da)206,568
- Last updated2024-01-24 v1
- MD5 ChecksumFCFA41C4DA10378B1823D8F7F2B71A54
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
OX365927 EMBL· GenBank· DDBJ | CAI4052533.1 EMBL· GenBank· DDBJ | Genomic DNA |