Reviewed,
UniProtKB/Swiss-Prot P36189 (FAS_ANSAN)
Last modified
January 19, 2010.
Version 49.
History...
Clusters with 100%,
90%,
50% identity |
Third-party data |
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Names and origin
| Protein names | Recommended name: Fatty acid synthase EC=2.3.1.85 | ||||
| Gene names |
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| Organism | Anser anser anser (Western graylag goose) | ||||
| Taxonomic identifier | 8844 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Anseriformes › Anatidae › Anser |
Protein attributes
| Sequence length | 352 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has seven catalytic activities and an acyl carrier protein. |
| Catalytic activity | Acetyl-CoA + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + (n+1) CoA + n CO2 + 2n NADP+. |
| Subunit structure | Homodimer which monomers are arranged in a head to tail fashion. |
| Induction | By triiodothyronine. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Lipid synthesis |
| Ligand | NAD NADP Phosphopantetheine |
| Molecular function | Hydrolase Ligase Oxidoreductase Transferase |
| Technical term | Direct protein sequencing Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | fatty-acid synthase activity Inferred from electronic annotation. Source: EC hydrolase activityInferred from electronic annotation. Source: UniProtKB-KW ligase activityInferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›352 | ›352 | Fatty acid synthase | PRO_0000180272 | |||||
Regions | |||||||||
| Region | 1 – ›352 | ›352 | Beta-ketoacyl synthase | ||||||
Sites | |||||||||
| Active site | 161 | 1 | For beta-ketoacyl synthase activity By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 352 | 1 | |||||||
Sequences
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References
| [1] | "Isolation and partial characterization of the gene for goose fatty acid synthase." Kameda K., Goodridge A.G. J. Biol. Chem. 266:419-426(1991) [PubMed: 1702426] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | "Specific modification of the condensation domain of fatty acid synthase and the determination of the primary structure of the modified active site peptides." Pouloe A.J., Bonsall R.F., Kolattukudy P.E. Arch. Biochem. Biophys. 230:117-128(1984) [PubMed: 6712225] [Abstract] Cited for: PROTEIN SEQUENCE OF 152-173. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M60622 mRNA. Translation: AAA49316.1. |
| PIR | A39042. |
3D structure databases | |
| SMR | P36189. Positions 2-352. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P36189. |
Family and domain databases | |
| InterPro | IPR000794. Beta-ketoacyl_synthase. IPR018201. Ketoacyl_synth_AS. IPR014031. Ketoacyl_synth_C. IPR014030. Ketoacyl_synth_N. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. [Graphical view] |
| Gene3D | G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits. |
| PANTHER | PTHR11712. Ketoacyl_synth. 1 hit. |
| Pfam | PF00109. ketoacyl-synt. 1 hit. PF02801. Ketoacyl-synt_C. 1 hit. [Graphical view] |
| PROSITE | PS00606. B_KETOACYL_SYNTHASE. 1 hit. PS00012. PHOSPHOPANTETHEINE. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FAS_ANSAN | ||||||||
| Accession | Primary (citable) accession number: P36189 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

Clusters with


