Reviewed,
UniProtKB/Swiss-Prot P12276 (FAS_CHICK)
Last modified
June 16, 2009.
Version 101.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Fatty acid synthase EC=2.3.1.85 Including the following 7 domains: 1- Recommended name: [Acyl-carrier-protein] S-acetyltransferase EC=2.3.1.38 2- Recommended name: [Acyl-carrier-protein] S-malonyltransferase EC=2.3.1.39 3- Recommended name: 3-oxoacyl-[acyl-carrier-protein] synthase EC=2.3.1.41 4- Recommended name: 3-oxoacyl-[acyl-carrier-protein] reductase EC=1.1.1.100 5- Recommended name: 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase EC=4.2.1.61 6- Recommended name: Enoyl-[acyl-carrier-protein] reductase EC=1.3.1.10 7- Recommended name: Oleoyl-[acyl-carrier-protein] hydrolase EC=3.1.2.14 | ||||
| Gene names |
| ||||
| Organism | Gallus gallus (Chicken) | ||||
| Taxonomic identifier | 9031 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus |
Protein attributes
| Sequence length | 2512 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| 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 7 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+. Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein]. Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein]. Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH. (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] = hexadec-2-enoyl-[acyl-carrier-protein] + H2O. Acyl-[acyl-carrier-protein] + NADP+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH. Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate. |
| Subunit structure | Homodimer which is arranged in a head to tail fashion. |
| Sequence similarities | Contains 1 acyl carrier domain. |
| Sequence caution | The sequence AAA82106.1 differs from that shown. Reason: Frameshift at position 2352. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 2 (identifier: P12276-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 1 (identifier: P12276-2) The sequence of this isoform differs from the canonical sequence as follows: 2349-2349: T → TQCFSFSLF |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.1 | ||||||
| Chain | 2 – 2512 | 2511 | Fatty acid synthase | PRO_0000180273 | |||||
Regions | |||||||||
| Domain | 2125 – 2181 | 57 | Acyl carrier | ||||||
| Nucleotide binding | 1675 – 1692 | 18 | NADP (ER) | ||||||
| Nucleotide binding | 1889 – 1904 | 16 | NADP (KR) | ||||||
| Region | 2 – ?412 | 411 | Beta-ketoacyl synthase | ||||||
| Region | 427 – 815 | 389 | Acyl and malonyl transferases | ||||||
| Region | 1638 – 1866 | 229 | Enoyl reductase | ||||||
| Region | 1867 – 2119 | 253 | Beta-ketoacyl reductase | ||||||
| Region | 2209 – 2511 | 303 | Thioesterase | ||||||
Sites | |||||||||
| Active site | 161 | 1 | For beta-ketoacyl synthase activity By similarity | ||||||
| Active site | 580 | 1 | For acyl/malonyl transferase activity By similarity | ||||||
| Active site | 878 | 1 | For beta-hydroxyacyl dehydratase activity By similarity | ||||||
| Active site | 2309 | 1 | For thioesterase activity By similarity | ||||||
| Active site | 2482 | 1 | For thioesterase activity By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylglutamate | ||||||
| Modified residue | 1708 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
| Modified residue | 2158 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 2349 | 1 | T → TQCFSFSLF in isoform 1. | VSP_000149 | |||||
Experimental info | |||||||||
| Sequence conflict | 78 – 79 | 2 | QL → PV in AAA48767. Ref.2 | ||||||
| Sequence conflict | 117 | 1 | L → A in AAA48767. Ref.2 | ||||||
| Sequence conflict | 676 | 1 | R → S in AAA48767. Ref.2 | ||||||
| Sequence conflict | 1170 | 1 | K → N in AAA48767. Ref.2 | ||||||
| Sequence conflict | 1179 | 1 | A → T in AAA48767. Ref.2 | ||||||
| Sequence conflict | 1192 | 1 | R → H in AAA48767. Ref.2 | ||||||
| Sequence conflict | 1199 | 1 | P → L in AAA48767. Ref.2 | ||||||
| Sequence conflict | 1287 – 1288 | 2 | DN → ND in AAA48767. Ref.2 | ||||||
| Sequence conflict | 1373 | 1 | K → E in AAA48767. Ref.2 | ||||||
| Sequence conflict | 1534 | 1 | C → Y in AAA48767. Ref.2 | ||||||
| Sequence conflict | 1578 | 1 | W → R in AAA48767. Ref.2 | ||||||
| Sequence conflict | 1686 – 1697 | 12 | QAAIA…LSMGC → ASSHCHRLEHGLA in AAA48767. Ref.2 | ||||||
| Sequence conflict | 1733 | 1 | Q → E in AAA48767. Ref.2 | ||||||
| Sequence conflict | 1746 | 1 | S → N in AAA48767. Ref.2 | ||||||
Sequences
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References
| [1] | "Amino-terminal blocking group and sequence of the animal fatty acid synthase." Huang W.-Y., Chirala S.S., Wakil S.J. Arch. Biochem. Biophys. 314:45-49(1994) [PubMed: 7944406] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-12. Strain: White leghorn. Tissue: Liver. |
| [2] | "Molecular cloning and sequencing of chicken liver fatty acid synthase cDNA." Holzer K.P., Liu W., Hammes G.G. Proc. Natl. Acad. Sci. U.S.A. 86:4387-4391(1989) [PubMed: 2734291] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 75-1775. Tissue: Liver. |
| [3] | "A novel cDNA extension procedure. Isolation of chicken fatty acid synthase cDNA clones." Chirala S.S., Kasturi R., Pazirandeh M., Stolow D.T., Huang W.-Y., Wakil S.J. J. Biol. Chem. 264:3750-3757(1989) [PubMed: 2917973] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1568-2512, PARTIAL PROTEIN SEQUENCE. |
| [4] | "Molecular cloning and sequencing of DNA complementary to chicken liver fatty acid synthase mRNA." Yuan Z., Liu W., Hammes G.G. Proc. Natl. Acad. Sci. U.S.A. 85:6328-6331(1988) [PubMed: 2842766] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1752-2512. |
| [5] | "Characterization of a genomic and cDNA clone coding for the thioesterase domain and 3' noncoding region of the chicken liver fatty acid synthase gene." Kasturi R., Chirala S.S., Pazirandeh M., Wakil S.J. Biochemistry 27:7778-7785(1988) [PubMed: 3207710] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 2202-2512. |
| [6] | "Complete amino acid sequence of chicken liver acyl carrier protein derived from the fatty acid synthase." Huang W.-Y., Stoops J.K., Wakil S.J. Arch. Biochem. Biophys. 270:92-98(1989) [PubMed: 2648999] [Abstract] Cited for: PROTEIN SEQUENCE OF 2122-2210. |
| [7] | "Complete amino acid sequence of the thioesterase domain of chicken liver fatty acid synthase." Yang C.-Y., Huang W.-Y., Chirala S.S., Wakil S.J. Biochemistry 27:7773-7777(1988) [PubMed: 3207709] [Abstract] Cited for: PROTEIN SEQUENCE OF 2210-2509. Strain: White leghorn. |
| [8] | "Amino acid sequences of pyridoxal 5'-phosphate binding sites and fluorescence resonance energy transfer in chicken liver fatty acid synthase." Chang S.I., Hammes G.G. Biochemistry 28:3781-3788(1989) [PubMed: 2751995] [Abstract] Cited for: PROTEIN SEQUENCE OF 668-675 AND 1699-1710. |
Cross-references
Sequence databases | |
|---|---|
| J03860 mRNA. Translation: AAA48767.1. J04485 mRNA. Translation: AAB46389.1. J02839 Genomic DNA. Translation: AAA82106.1. Frameshift. | |
| IPI | IPI00572922. IPI00597845. |
| PIR | XYCHFA. S57248. |
| RefSeq | NP_990486.1. |
| UniGene | Gga.33829 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1N8L based on UniProtKB P12785. |
| SMR | P12276. Positions 2218-2503. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P12276. |
Genome annotation databases | |
| Ensembl | ENSGALG00000002747. Gallus gallus. [Contig view] |
| GeneID | 396061. |
| KEGG | gga:396061. |
Phylogenomic databases | |
| HOGENOM | P12276. |
| HOVERGEN | P12276. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.100. 4. 1.3.1.10. 4. 2.3.1.38. 4. 2.3.1.39. 4. 2.3.1.41. 4. 2.3.1.85. 4. 3.1.2.14. 4. 4.2.1.61. 4. |
Family and domain databases | |
| InterPro | IPR001227. Ac_transferase_reg. IPR009081. Acyl_carrier_prot-like. IPR014043. Acyl_transferase. IPR013149. ADH_Zn-bd. IPR000794. Beta-ketoacyl_synthase. IPR002198. DH_sc/Rdtase_SDR. IPR018201. Ketoacyl_synth_AS. IPR014031. Ketoacyl_synth_C. IPR014030. Ketoacyl_synth_N. IPR016040. NAD(P)-bd_dom. IPR006163. Phsphopanteth_bd. IPR006162. Ppantne_S. IPR001031. Thioesterase. IPR016038. Thiolase-like_subgr. [Graphical view] |
| Gene3D | G3DSA:3.40.366.10. Ac_transferase_reg. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 2 hits. G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits. |
| PANTHER | PTHR11712. Ketoacyl_synth. 1 hit. |
| Pfam | PF00698. Acyl_transf_1. 1 hit. PF00106. adh_short. 1 hit. PF00107. ADH_zinc_N. 1 hit. PF00109. ketoacyl-synt. 1 hit. PF02801. Ketoacyl-synt_C. 1 hit. PF00550. PP-binding. 1 hit. PF00975. Thioesterase. 1 hit. [Graphical view] |
| PROSITE | PS50075. ACP_DOMAIN. 1 hit. PS00606. B_KETOACYL_SYNTHASE. 1 hit. PS00012. PHOSPHOPANTETHEINE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FAS_CHICK | ||||||||
| Accession | Primary (citable) accession number: P12276 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
