Fatty acid synthase - Anser anser anser (Western graylag goose)

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P36189 (FAS_ANSAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 61. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
Fatty acid synthase
EC=2.3.1.85

Gene names

Name:	FASN
Synonyms:	FAS

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 Fatty acid metabolism Lipid biosynthesis Lipid metabolism
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
Molecular_function	fatty acid synthase activity Inferred from electronic annotation. Source: EC hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW ligase activity Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity Inferred 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

For beta-ketoacyl synthase activity By similarity

Experimental info

Non-terminal residue

352

Sequences

Sequence

Length

Mass (Da)

Tools

P36189 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 908530BF76762335
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FASTA

352

37,912

        10         20         30         40         50         60 
MEDVVIAGIA GKLPESENLQ EFWEKLLNGV DMVTEDDRRW KPGMYGLPKR NGKLKDISKF 

        70         80         90        100        110        120 
DASFFGVHPK QAHTMDPQLR LLLEVSYEAI LDGGINPATL RGTDTGVWVG ASGSEAGEAF 

       130        140        150        160        170        180 
SQDPEQLLGY SMIGCQRAMF ANRISYFYDF KGPSLSIDTA CSSSLMALEN AYKAIRNGRC 

       190        200        210        220        230        240 
SAAVVGGVNL LLKPNTSVQF MKLGMLSPDG ACKVFDASGD GYCRSEAVVV VLLTKKSMAK 

       250        260        270        280        290        300 
RIYATIVNAG SNTDGFKEQG VTFPSGDMQR QLVSSLHREC GIKPGDIEYV ETHGTGTKVG 

       310        320        330        340        350 
DPQEVNGLAD LFCQCEREPL LIGSTKSNMG HPEPASGLAA LAKVVLSLEH GL

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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] [Europe PMC] [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] [Europe PMC] [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
ProteinModelPortal	P36189.
ModBase	Search...
Proteomic databases
PRIDE	P36189.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.40.47.10. 2 hits.
InterPro	IPR018201. Ketoacyl_synth_AS. IPR014031. Ketoacyl_synth_C. IPR014030. Ketoacyl_synth_N. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. [Graphical view]
Pfam	PF00109. ketoacyl-synt. 1 hit. PF02801. Ketoacyl-synt_C. 1 hit. [Graphical view]
SUPFAM	SSF53901. Thiolase-like. 1 hit.
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

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	April 3, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

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