P34229 · FAS1_YARLI
- ProteinFatty acid synthase subunit beta
- GeneFAS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids2086 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.
Catalytic activity
- acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 286 | For acetyltransferase activity | ||||
Sequence: S | ||||||
Active site | 1842 | For malonyltransferase activity | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | fatty acid synthase complex | |
Molecular Function | (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity | |
Molecular Function | [acyl-carrier-protein] S-acetyltransferase activity | |
Molecular Function | [acyl-carrier-protein] S-malonyltransferase activity | |
Molecular Function | enoyl-[acyl-carrier-protein] reductase (NADH) activity | |
Molecular Function | fatty acid synthase activity | |
Molecular Function | fatty acyl-[ACP] hydrolase activity | |
Molecular Function | fatty-acyl-CoA synthase activity | |
Biological Process | long-chain fatty acid biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFatty acid synthase subunit beta
- EC number
Including 5 domains:
- Recommended name3-hydroxyacyl-[acyl-carrier-protein] dehydratase
- EC number
- Recommended nameEnoyl-[acyl-carrier-protein] reductase [NADH]
- EC number
- Recommended name[Acyl-carrier-protein] acetyltransferase
- EC number
- Recommended name[Acyl-carrier-protein] malonyltransferase
- EC number
- Recommended nameS-acyl fatty acid synthase thioesterase
- EC number
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Dipodascaceae > Yarrowia
Accessions
- Primary accessionP34229
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000180283 | 1-2086 | Fatty acid synthase subunit beta | |||
Sequence: MYPTTGVNTPQSAASLRPLVLSHGQTEHSLLVPTSLYINCTTLRDQFYASLPPATEDKADDDEPSSSTELLAAFLGFTAKTVEEEPGPYDDVLSLVLNEFETRYLRGNDIHAVASSLLQDEDVPTTVGKIKRVIRAYYAARIACNRPIKAHSSALFRAASEDSDNVSLYAIFGGQGNTEDYFEELREIYDIYQGLVGDFIRECGAQLLALSRDHIAAEKIYTKGFDIVKWLEHPETIPDFEYLISAPISVPIIGVIQLAHYAVTCRVLGLNPGQVRDNLKGATGHSQGLITAIAISASDSWDEFYNSASRILKIFFFIGVRVQQAYPSTFLPPSTLEDSVKQGEGKPTPMLSIRDLSLNQVQEFVDATNLHLPEDKQIVVSLINGPRNVVVTGPPQSLYGLCLVLRKQKAETGLDQSRVPHSQRKLKFTHRFLPITSPFHSYLLEKSTDLIINDLESSGVEFVSSELKVPVYDTFDGSVLSQLPKGIVSRLVNLITHLPVKWEKATQFQASHIVDFGPGGASGLGLLTHKNKDGTGVRTILAGVIDQPLEFGFKQELFDRQESSIVFAQNWAKEFSPKLVKISSTNEVYVDTKFSRLTGRAPIMVAGMTPTTVNPKFVAATMNSGYHIELGGGGYFAPGMMTKALEHIEKNTPPGSGITINLIYVNPRLIQWGIPLIQELRQKGFPIEGLTIGAGVPSLEVANEWIQDLGVKHIAFKPGSIEAISSVIRIAKANPDFPIILQWTGGRGGGHHSFEDFHAPILQMYSKIRRCSNIVLIAGSGFGASTDSYPYLTGSWSRDFDYPPMPFDGILVGSRVMVAKEAFTSLGAKQLIVDSPGVEDSEWEKTYDKPTGGVITVLSEMGEPIHKLATRGVLFWHEMDKTVFSLPKKKRLEVLKSKRAYIIKRLNDDFQKTWFAKNAQGQVCDLEDLTYAEVIQRLVDLMYVKKESRWIDVTLRNLAGTFIRRVEERFSTETGASSVLQSFSELDSEPEKVVERVFELFPASTTQIINAQDKDHFLMLCLNPMQKPVPFIPVLDDNFEFFFKKDSLWQCEDLAAVVDEDVGRICILQGPVAVKHSKIVNEPVKEILDSMHEGHIKQLLEDGEYAGNMANIPQVECFGGKPAQNFGDVALDSVMVLDDLNKTVFKIETGTSALPSAADWFSLLAGDKNSWRQVFLSTDTIVQTTKMISNPLHRLLEPIAGLQVEIEHPDEPENTVISAFEPINGKVTKVLELRKGAGDVISLQLIEARGVDRVPVALPLEFKYQPQIGYAPIVEVMTDRNTRIKEFYWKLWFGQDSKFEIDTDITEEIIGDDVTISGKAIADFVHAVGNKGEAFVGRSTSAGTVFAPMDFAIVLGWKAIIKAIFPRAIDADILRLVHLSNGFKMMPGADPLQMGDVVSATAKIDTVKNSATGKTVAVRGLLTRDGKPVMEVVSEFFYRGEFSDFQNTFERREEVPMQLTLKDAKAVAILCSKEWFEYNGDDTKDLEGKTIVFRNSSFIKYKNETVFSSVHTTGKVLMELPSKEVIEIATVNYQAGESHGNPVIDYLERNGTTIEQPVEFEKPIPLSKADDLLSFKAPSSNEPYAGVSGDYNPIHVSRAFASYASLPGTITHGMYSSAAVRSLIEVWAAENNVSRVRAFSCQFQGMVLPNDEIVTRLEHVGMINGRKIIKVTSTNRETEAVVLSGEAEVEQPISTFVFTGQGSQEQGMGMDLYASSEVAKKVWDKADEHFLQNYGFSIIKIVVENPKELDIHFGGPKGKKIRDNYISMMFETIDEKTGNLISEKIFKEIDETTDSFTFKSPTGLLSATQFTQPALTLMEKASFEDMKAKGLVPVDATFAGHSLGEYSALASLGDVMPIESLVDVVFYRGMTMQVAVPRDAQGRSNYGMCAVNPSRISTTFNDAALRFVVDHISEQTKWLLEIVNYNVENSQYVTAGDLRALDTLTNVLNVLKLEKINIDKLLESLPLEKVKEHLSEIVTEVAKKSVAKPQPIELERGFAVIPLKGISVPFHSSYLRNGVKPFQNFLVKKVPKNAVKPANLIGKYIPNLTAKPFEITKEYFEEVYKLTGSEKVKSIINNWESYESKQ |
Interaction
Subunit
[Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-480 | Acetyltransferase | ||||
Sequence: MYPTTGVNTPQSAASLRPLVLSHGQTEHSLLVPTSLYINCTTLRDQFYASLPPATEDKADDDEPSSSTELLAAFLGFTAKTVEEEPGPYDDVLSLVLNEFETRYLRGNDIHAVASSLLQDEDVPTTVGKIKRVIRAYYAARIACNRPIKAHSSALFRAASEDSDNVSLYAIFGGQGNTEDYFEELREIYDIYQGLVGDFIRECGAQLLALSRDHIAAEKIYTKGFDIVKWLEHPETIPDFEYLISAPISVPIIGVIQLAHYAVTCRVLGLNPGQVRDNLKGATGHSQGLITAIAISASDSWDEFYNSASRILKIFFFIGVRVQQAYPSTFLPPSTLEDSVKQGEGKPTPMLSIRDLSLNQVQEFVDATNLHLPEDKQIVVSLINGPRNVVVTGPPQSLYGLCLVLRKQKAETGLDQSRVPHSQRKLKFTHRFLPITSPFHSYLLEKSTDLIINDLESSGVEFVSSELKVPVYDTFDGSVL | ||||||
Region | 492-879 | Enoyl reductase | ||||
Sequence: VNLITHLPVKWEKATQFQASHIVDFGPGGASGLGLLTHKNKDGTGVRTILAGVIDQPLEFGFKQELFDRQESSIVFAQNWAKEFSPKLVKISSTNEVYVDTKFSRLTGRAPIMVAGMTPTTVNPKFVAATMNSGYHIELGGGGYFAPGMMTKALEHIEKNTPPGSGITINLIYVNPRLIQWGIPLIQELRQKGFPIEGLTIGAGVPSLEVANEWIQDLGVKHIAFKPGSIEAISSVIRIAKANPDFPIILQWTGGRGGGHHSFEDFHAPILQMYSKIRRCSNIVLIAGSGFGASTDSYPYLTGSWSRDFDYPPMPFDGILVGSRVMVAKEAFTSLGAKQLIVDSPGVEDSEWEKTYDKPTGGVITVLSEMGEPIHKLATRGVLFWHEM | ||||||
Region | 1166-1657 | Dehydratase | ||||
Sequence: GDKNSWRQVFLSTDTIVQTTKMISNPLHRLLEPIAGLQVEIEHPDEPENTVISAFEPINGKVTKVLELRKGAGDVISLQLIEARGVDRVPVALPLEFKYQPQIGYAPIVEVMTDRNTRIKEFYWKLWFGQDSKFEIDTDITEEIIGDDVTISGKAIADFVHAVGNKGEAFVGRSTSAGTVFAPMDFAIVLGWKAIIKAIFPRAIDADILRLVHLSNGFKMMPGADPLQMGDVVSATAKIDTVKNSATGKTVAVRGLLTRDGKPVMEVVSEFFYRGEFSDFQNTFERREEVPMQLTLKDAKAVAILCSKEWFEYNGDDTKDLEGKTIVFRNSSFIKYKNETVFSSVHTTGKVLMELPSKEVIEIATVNYQAGESHGNPVIDYLERNGTTIEQPVEFEKPIPLSKADDLLSFKAPSSNEPYAGVSGDYNPIHVSRAFASYASLPGTITHGMYSSAAVRSLIEVWAAENNVSRVRAFSCQFQGMVLPNDEIVTRL | ||||||
Domain | 1550-1680 | MaoC-like | ||||
Sequence: NGTTIEQPVEFEKPIPLSKADDLLSFKAPSSNEPYAGVSGDYNPIHVSRAFASYASLPGTITHGMYSSAAVRSLIEVWAAENNVSRVRAFSCQFQGMVLPNDEIVTRLEHVGMINGRKIIKVTSTNRETEA | ||||||
Region | 1658-1879 | Malonyl/palmitoyl transferase | ||||
Sequence: EHVGMINGRKIIKVTSTNRETEAVVLSGEAEVEQPISTFVFTGQGSQEQGMGMDLYASSEVAKKVWDKADEHFLQNYGFSIIKIVVENPKELDIHFGGPKGKKIRDNYISMMFETIDEKTGNLISEKIFKEIDETTDSFTFKSPTGLLSATQFTQPALTLMEKASFEDMKAKGLVPVDATFAGHSLGEYSALASLGDVMPIESLVDVVFYRGMTMQVAVPRD |
Sequence similarities
Belongs to the fungal fatty acid synthetase subunit beta family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,086
- Mass (Da)231,342
- Last updated2004-10-11 v2
- Checksum060F6CEA44F235B2
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 1-11 | in Ref. 1; CAA42211 | ||||
Sequence: MYPTTGVNTPQ → M | ||||||
Sequence conflict | 529-530 | in Ref. 1; CAA42211 | ||||
Sequence: HK → TR | ||||||
Sequence conflict | 1240 | in Ref. 1; CAA42211 | ||||
Sequence: V → G | ||||||
Sequence conflict | 1612 | in Ref. 1; CAA42211 | ||||
Sequence: H → Q | ||||||
Sequence conflict | 2077 | in Ref. 1; CAA42211 | ||||
Sequence: N → D |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X59690 EMBL· GenBank· DDBJ | CAA42211.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CR382128 EMBL· GenBank· DDBJ | CAG83163.1 EMBL· GenBank· DDBJ | Genomic DNA |