P08757 (FAS_CAPHI) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 68.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Fatty acid synthase EC=2.3.1.85 | ||||
| Gene names |
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| Organism | Capra hircus (Goat) | ||||
| Taxonomic identifier | 9925 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Capra![]() |
Protein attributes
| Sequence length | 35 AA. |
| Sequence status | Fragment. |
| Protein existence | Inferred from homology |
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 7 catalytic activities and an acyl carrier protein. This fragment is from the acyltransferase domain of the fatty acid synthetase. |
| 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 is arranged in a head to tail fashion. |
| Subcellular location | Cytoplasm By similarity. Melanosome By similarity. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism |
| Cellular component | Cytoplasm |
| Ligand | NAD NADP |
| Molecular function | Hydrolase Transferase |
| Technical term | Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological_process | fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | fatty acid synthase activity Inferred from electronic annotation. Source: EC hydrolase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Amino acid sequence around the active-site serine residue in the acyltransferase domain of goat mammary fatty acid synthetase." Mikkelsen J., Hoejrup P., Rasmussen M.M., Roepstorff P., Knudsen J. Biochem. J. 227:21-27(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| PIR | S07131. |
3D structure databases | |
| ProteinModelPortal | P08757. |
| SMR | P08757. Positions 1-35. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.40.366.10. 1 hit. |
| InterPro | IPR001227. Ac_transferase_dom. IPR014043. Acyl_transferase. [Graphical view] |
| Pfam | PF00698. Acyl_transf_1. 1 hit. [Graphical view] |
| PROSITE | PS00606. B_KETOACYL_SYNTHASE. Partial match. PS00012. PHOSPHOPANTETHEINE. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FAS_CAPHI | ||||||||
| Accession | Primary (citable) accession number: P08757 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||

Clusters with
