FAS1 tetrafunctional fatty acid synthase subunit FAS1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: FAS1
Official Full Name: tetrafunctional fatty acid synthase subunit FAS1
Primary source: SGD:S000001665
Locus tag: YKL182W
See related: AllianceGenome:SGD:S000001665; FungiDB:YKL182W; VEuPathDB:YKL182W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables several functions, including (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity; S-acyltransferase activity; and enoyl-[acyl-carrier-protein] reductase (NADPH) activity. Contributes to fatty acid synthase activity. Involved in long-chain fatty acid biosynthetic process. Located in cytosol and lipid droplet. Part of fatty acid synthase complex. [provided by Alliance of Genome Resources, Oct 2024]
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Genomic context

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See FAS1 in Genome Data Viewer

Location:: chromosome: XI

Exon count:: 1

Sequence:: Chromosome: XI; NC_001143.9 (100671..106826)

Chromosome XI - NC_001143.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001143.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Analysis of the co-translational assembly of the fungal fatty acid synthase (FAS).
Title: Analysis of the co-translational assembly of the fungal fatty acid synthase (FAS).
This study shows that single mutations at domain-domain interfaces can severely perturb substrate shuttling in FAS1.
Title: Analysis and engineering of substrate shuttling by the acyl carrier protein (ACP) in fatty acid synthases (FASs).
Overexpression of FAS1, FAS2 and Acc1 leads to accumulation of sterols.
Title: Overexpression of genes of the fatty acid biosynthetic pathway leads to accumulation of sterols in Saccharomyces cerevisiae.
Results structurally and functionally characterized the FAS type I PPT as part of the multienzyme protein and as an isolated domain.
Title: Multimeric options for the auto-activation of the Saccharomyces cerevisiae FAS type I megasynthase.
The crystal structure of the 2.6-MDa Saccharomyces cerevisiae fatty acid synthase (FAS) multienzyme in complex with the antibiotic cerulenin, is presented.
Title: Inhibition of the fungal fatty acid synthase type I multienzyme complex.
Fatty acid synthase (Fas) plays a key role during the cellular response of Saccharomyces cerevisiae to H2O2.
Title: Down-regulation of fatty acid synthase increases the resistance of Saccharomyces cerevisiae cells to H2O2.
Sfh2p inhibits fatty acid synthase activity in response to haem depletion
Title: SFH2 regulates fatty acid synthase activity in the yeast Saccharomyces cerevisiae and is critical to prevent saturated fatty acid accumulation in response to haem and oleic acid depletion.
Study determined crystal structure of fatty acid synthase, which illuminates how this enzyme is initially activated and then carries out multiple steps of synthesis in each of six sterically isolated reaction chambers.
Title: The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together.

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity	IDA Inferred from Direct Assay more info	PubMed
enables (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity	IEA Inferred from Electronic Annotation more info
enables (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables [acyl-carrier-protein] S-acetyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables [acyl-carrier-protein] S-acetyltransferase activity	IEA Inferred from Electronic Annotation more info
enables [acyl-carrier-protein] S-acetyltransferase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables [acyl-carrier-protein] S-malonyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables [acyl-carrier-protein] S-malonyltransferase activity	IEA Inferred from Electronic Annotation more info
enables [acyl-carrier-protein] S-malonyltransferase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables enoyl-[acyl-carrier-protein] reductase (NADH) activity	IEA Inferred from Electronic Annotation more info
enables enoyl-[acyl-carrier-protein] reductase (NADPH) activity	IDA Inferred from Direct Assay more info	PubMed
enables enoyl-[acyl-carrier-protein] reductase (NADPH) activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables fatty acid synthase activity	IEA Inferred from Electronic Annotation more info
contributes_to fatty acid synthase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables fatty acyl-[ACP] hydrolase activity	IEA Inferred from Electronic Annotation more info
enables fatty-acyl-CoA synthase activity	IEA Inferred from Electronic Annotation more info
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables lyase activity	IEA Inferred from Electronic Annotation more info
enables oxidoreductase activity	IEA Inferred from Electronic Annotation more info
enables palmitoyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables palmitoyltransferase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables transferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in fatty acid biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in long-chain fatty acid biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in long-chain fatty acid biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
part_of fatty acid synthase complex	IBA Inferred from Biological aspect of Ancestor more info
part_of fatty acid synthase complex	IDA Inferred from Direct Assay more info	PubMed
part_of fatty acid synthase complex	IEA Inferred from Electronic Annotation more info
located_in lipid droplet	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	HDA more info	PubMed

General protein information

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Preferred Names: tetrafunctional fatty acid synthase subunit FAS1

NP_012739.1

EC 1.3.1.9

EC 2.3.1.38

EC 2.3.1.39

EC 2.3.1.86

EC 3.1.2.14

EC 4.2.1.59

Beta subunit of fatty acid synthetase; complex catalyzes the synthesis of long-chain saturated fatty acids; contains acetyltransacylase, dehydratase, enoyl reductase, malonyl transacylase, and palmitoyl transacylase activities; specific target of the broad-spectrum antifungal NPD6433

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001143.9 Reference assembly

Range

100671..106826

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179748.1 → NP_012739.1 TPA: tetrafunctional fatty acid synthase subunit FAS1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_012739.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VX19, P07149, Q05747

UniProtKB/TrEMBL

A6ZZE4, C7GJ28, N1P0M8

Conserved Domains (5) summary

COG0331
Location:159 → 536

FabD; Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]

COG4981
Location:559 → 1350

COG4981; Enoyl reductase domain of yeast-type FAS1 [Lipid transport and metabolism]

cd03447
Location:1536 → 1660

FAS_MaoC; the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and 17-beta-hydroxysteriod dehydrogenase (HSD).

pfam00698
Location:1663 → 2037

Acyl_transf_1; Acyl transferase domain

pfam17828
Location:5 → 131

FAS_N; N-terminal domain in fatty acid synthase subunit beta