P43098 · FAS2_CANAX
- ProteinFatty acid synthase subunit alpha
- GeneFAS2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1885 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase.
Catalytic activity
- a fatty acyl-[ACP] + H+ + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 1304 | For beta-ketoacyl synthase activity | ||||
Sequence: C | ||||||
Active site | 1546 | For beta-ketoacyl synthase activity | ||||
Sequence: H | ||||||
Active site | 1587 | For beta-ketoacyl synthase activity | ||||
Sequence: H | ||||||
Binding site | 1771 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1771-1773 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: DVE | ||||||
Binding site | 1772 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 1773 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1797 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 1807 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 1816-1826 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: EAVFKALGVES | ||||||
Binding site | 1840-1843 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: RDVN | ||||||
Binding site | 1870-1872 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: ISH | ||||||
Binding site | 1871 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 1872 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: H |
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 | fatty-acyl-CoA synthase activity | |
Molecular Function | holo-[acyl-carrier-protein] synthase activity | |
Molecular Function | magnesium ion binding | |
Biological Process | mitotic nuclear membrane biogenesis | |
Biological Process | palmitic 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 3 domains:
- Recommended nameAcyl carrier
- Recommended name3-oxoacyl-[acyl-carrier-protein] reductase
- EC number
- Alternative names
- Recommended name3-oxoacyl-[acyl-carrier-protein] synthase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Candida/Lodderomyces clade > Candida
Accessions
- Primary accessionP43098
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Miscellaneous
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000180284 | 1-1885 | Fatty acid synthase subunit alpha | |||
Sequence: MKPEIEQELSHTLLTELLAYQFASPVRWIETQDVFLKQHNTERIIEIGPSPTLAGMANRTIKAKYESYDAALSLQRQVLCYSKDAKEIYYKPDPADLAPKETPKQEESTPSAPAAATPTPAAAAAPTPAPAPASAGPVESIPDEPVKANLLIHVLVAQKLKKPLDAVPMTKAIKDLVNGKSTVQNEILGDLGKEFGSTPEKPEDTPLEELAEQFQDSFSGQLGKTSTSLIGRLMSSKMPGGFSITTARKYLESRFGLGAGRQDSVLLMALTNEPANRLGSEADAKTFFDGIAQKYASSAGISLSSGAGSGAGAANSGGAVVDSAALDALTAENKKLAKQQLEVLARYLQSRLKQGSLKSFIKEKEASAVLQKELDLWEAEHGEFYAKGIQPTFSALKSRTYDSYWNWARQDVLSMYFDIIFGKLTSVDRETINQCIQIMNRANPTLIKFMQYHIDHCPEYKGETYKLAKRLGQQLIDNCKQVLTEDPVYKDVSRITGPKTKVSAKGNIEYEETQKDSVRKFEQYVYEMAQGGAMTKVSQPTIQEDLARVYKAISKQASKDSKLELQRVYEDLLKVVESSKEIETEQLTKDILQAATVPTTPTEEVDDPCTPSSDDEIASLPDKTSIIQPVSSTIPSQTIPFLHIQKKTKDGWEYNKKLSSLYLDGLESAAINGLTFKDKYVLVTGAGAGSIGAEILQGLISGGAKVIVTTSRFSKKVTEYYQNMYARYGAAGSTLIVVPFNQGSKQDVDALVQYIYDEPKKGGLGWDLDAIIPFAAIPENGNGLDNIDSKSEFAHRIMLTNLLRLLGAVKSKKPTDTRPAQCILPLSPNHGTFGFDGLYSESKISLETLFNRWYSEDWGSKLTVCGAVIGWTRGTGLMSANNIIAEGIEKLGVRTFSQKEMAFNILGLLTPEIVQLCQEEPVMADLNGGLQFIDNLKDFTSKLRTDLLETADIRRAVSIESAIEQKVVNGDNVDANYSKVMVEPRANMKFDFPTLKSYDEIKQIAPELEGMLDLENVVVVTGFAEVGPWGNSRTRWEMEAYGEFSLEGAIEMAWIMGFIKYHNGNLQGKPYSGWVDAKTQTPIDEKDIKSKYEEEILEHSGIRLIEPELFNGYDPKKKQMIQEIVVQHDLEPFECSKETAEQYKHEHGEKCEIFEIEESGEYTVRILKGATLYVPKALRFDRLVAGQIPTGWDARTYGIPEDTISQVDPITLYVLVATVEALLSAGITDPYEFYKYVHVSEVGNCSGSGMGGVSALRGMFKDRYADKPVQNDILQESFINTMSAWVNMLLLSSSGPIKTPVGACATAVESVDIGIETILSGKAKVVLVGGYDDFQEEGSYEFANMNATSNSIEEFKHGRTPKEMSRPTTTTRNGFMEAQGSGIQVIMTADLALKMGVPIHAVLAMTATATDKIGRSVPAPGKGILTTAREHHGNLKYPSPLLNIKYRKRQLNKRLEQIKSWEETELSYLQEEAELAKEEFGDEFSMHEFLKERTEEVYRESKRQVSDAKKQWGNSFYKSDPRIAPLRGALAAFNLTIDDIGVASFHGTSTVANDKNESATINNMMKHLGRSEGNPVFGVFQKYLTGHPKGAAGAWMLNGAIQILESGLVPGNRNADNVDKLLEQYEYVLYPSRSIQTDGIKAVSVTSFGFGQKGAQAVVVHPDYLFAVLDRSTYEEYATKVSARNKKTYRYMHNAITRNTMFVAKDKAPYSDELEQPVYLDPLARVEENKKKLVFSDKTIQSNQSYVGEVAQKTAKALSTLNKSSKGVGVDVELLSAINIDNETFIERNFTGNEVEYCLNTAHPQASFTGTWSAKEAVFKALGVESKGAGASLIDIEITRDVNGAPKVILHGEAKKAAAKAGVKNVNISISHDDFQATAVALSEF | ||||||
Modified residue | 181 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S |
Keywords
- PTM
Interaction
Subunit
[Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta).
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 92-140 | Disordered | ||||
Sequence: PDPADLAPKETPKQEESTPSAPAAATPTPAAAAAPTPAPAPASAGPVES | ||||||
Domain | 146-221 | Carrier | ||||
Sequence: VKANLLIHVLVAQKLKKPLDAVPMTKAIKDLVNGKSTVQNEILGDLGKEFGSTPEKPEDTPLEELAEQFQDSFSGQ | ||||||
Domain | 1121-1661 | Ketosynthase family 3 (KS3) | ||||
Sequence: IQEIVVQHDLEPFECSKETAEQYKHEHGEKCEIFEIEESGEYTVRILKGATLYVPKALRFDRLVAGQIPTGWDARTYGIPEDTISQVDPITLYVLVATVEALLSAGITDPYEFYKYVHVSEVGNCSGSGMGGVSALRGMFKDRYADKPVQNDILQESFINTMSAWVNMLLLSSSGPIKTPVGACATAVESVDIGIETILSGKAKVVLVGGYDDFQEEGSYEFANMNATSNSIEEFKHGRTPKEMSRPTTTTRNGFMEAQGSGIQVIMTADLALKMGVPIHAVLAMTATATDKIGRSVPAPGKGILTTAREHHGNLKYPSPLLNIKYRKRQLNKRLEQIKSWEETELSYLQEEAELAKEEFGDEFSMHEFLKERTEEVYRESKRQVSDAKKQWGNSFYKSDPRIAPLRGALAAFNLTIDDIGVASFHGTSTVANDKNESATINNMMKHLGRSEGNPVFGVFQKYLTGHPKGAAGAWMLNGAIQILESGLVPGNRNADNVDKLLEQYEYVLYPSRSIQTDGIKAVSVTSFGFGQKGAQAVVVH |
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,885
- Mass (Da)207,589
- Last updated1995-11-01 v1
- Checksum4835D57F362372E0
Keywords
- Technical term