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UniProtKB/Swiss-Prot entry P07149


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FAS1_YEAST
Primary accession number P07149
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on February 1, 1994 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 97)
Name and origin of the protein
Protein name Fatty acid synthase subunit beta
Synonym EC 2.3.1.86
Includes 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
     (EC 4.2.1.61)
Enoyl-[acyl-carrier-protein] reductase [NADH]
     (EC 1.3.1.9)
[Acyl-carrier-protein] acetyltransferase
     (EC 2.3.1.38)
[Acyl-carrier-protein] malonyltransferase
     (EC 2.3.1.39)
S-acyl fatty acid synthase thioesterase
     (EC 3.1.2.14)
Gene name
Name: FAS1
OrderedLocusNames: YKL182W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/BF00422073; PubMed=3528750 [NCBI, ExPASy, EBI, Israel, Japan]
Schweizer M., Roberts L.M., Hoeltke H.-J., Takabayashi K., Hoellerer E., Hoffmann B., Mueller G., Koettig H., Schweizer E.;
"The pentafunctional FAS1 gene of yeast: its nucleotide sequence and order of the catalytic domains.";
Mol. Gen. Genet. 203:479-486(1986).
[2]
SEQUENCE REVISION.
DOI=10.1007/BF00273618; PubMed=2034224 [NCBI, ExPASy, EBI, Israel, Japan]
Koettig H., Rottner G., Beck K.-F., Schweizer M., Schweizer E.;
"The pentafunctional FAS1 genes of Saccharomyces cerevisiae and Yarrowia lipolytica are co-linear and considerably longer than previously estimated.";
Mol. Gen. Genet. 226:310-314(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3031066 [NCBI, ExPASy, EBI, Israel, Japan]
Chirala S.S., Kuziora M.A., Spector D.M., Wakil S.J.;
"Complementation of mutations and nucleotide sequence of FAS1 gene encoding beta subunit of yeast fatty acid synthase.";
J. Biol. Chem. 262:4231-4240(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1002/yea.320091208; PubMed=8154185 [NCBI, ExPASy, EBI, Israel, Japan]
Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J., Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
"Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI from Saccharomyces cerevisiae reveals 23 open reading frames including the FAS1 gene.";
Yeast 9:1343-1348(1993).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1038/369371a0; PubMed=8196765 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1947-2051.
STRAIN=ATCC 26786 / X2180-1A;
PubMed=7992503 [NCBI, ExPASy, EBI, Israel, Japan]
Carter A.T., Narbad A., Pearson B.M., Beck K.-F., Logghe M., Contreras R., Schweizer M.;
"Phosphoribosylpyrophosphate synthetase (PRS): a new gene family in Saccharomyces cerevisiae.";
Yeast 10:1031-1044(1994).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1177; THR-1189; SER-1190 AND SER-1191, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1117; SER-1121 AND SER-1124, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
  • 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 + n malonyl-CoA + 2n NADH + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NAD+ + 2n NADP+.
  • CATALYTIC ACTIVITY: Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].
  • CATALYTIC ACTIVITY: Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein].
  • CATALYTIC ACTIVITY: (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] = hexadec-2-enoyl-[acyl-carrier-protein] + H2O.
  • CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH.
  • CATALYTIC ACTIVITY: Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.
  • SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits (alpha and beta).
  • INTERACTION:
    P19097:FAS2; NbExp=1; IntAct=EBI-6795, EBI-6806;
  • MISCELLANEOUS: Present with 91800 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X03977; CAA27616.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M30162; AAB59310.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X74151; CAA52256.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z28182; CAA82025.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X70069; CAA49673.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S34688; S34688.
RefSeq NP_012739.1; -.
3D structure databases
PDB
2PFF; X-ray; 4.00 A; B/E/H=1-545, B/E/H=1669-1941.[ExPASy / RCSB / EBI]
2UV8; X-ray; 3.10 A; G/H/I=5-2050.[ExPASy / RCSB / EBI]
2VKZ; X-ray; 4.00 A; G/H/I=1-2051.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2PFF; -.
2UV8; -.
2VKZ; -.
ModBase P07149.
Protein-protein interaction databases
DIP DIP:742N; -.
IntAct P07149; -.
Enzyme and pathway databases
BioCyc MetaCyc:YKL182W-MON; -.
Organism-specific databases
CYGD YKL182w; -.
SGD S000001665; FAS1.
Yeast-GFP YKL182W.
Gene expression databases
ArrayExpress P07149; -.
GermOnline YKL182W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from SGD).
GO:0005835; Cellular component: fatty acid synthase complex (inferred from direct assay from SGD).
GO:0005811; Cellular component: lipid particle (inferred from direct assay from SGD).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0004317; Molecular function: 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity (inferred from mutant phenotype from SGD).
GO:0004313; Molecular function: [acyl-carrier-protein] S-acetyltransferase activity (inferred from mutant phenotype from SGD).
GO:0004314; Molecular function: [acyl-carrier-protein] S-malonyltransferase activity (inferred from mutant phenotype from SGD).
GO:0004318; Molecular function: enoyl-[acyl-carrier-protein] reductase (NADH) activity (inferred from mutant phenotype from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006633; Biological process: fatty acid biosynthetic process (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR001227; Ac_transferase_reg.
IPR014043; Acyl_transferase.
IPR013565; DUF1729.
IPR003965; Fatty_acid_synthase.
IPR016452; Fatty_acid_Synthase_bsu_fun.
IPR002539; MaoC_deHydtase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.366.10; Ac_transferase_reg; 1.
Pfam PF00698; Acyl_transf_1; 1.
PF08354; DUF1729; 1.
PF01575; MaoC_dehydratas; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF005562; FAS_yeast_beta; 1.
PRINTS PR01483; FASYNTHASE.
BLOCKS P07149.
ProtoNet P07149.
Proteomic databases
PeptideAtlas P07149; -.
Genome annotation databases
Ensembl YKL182W; Saccharomyces cerevisiae. [Contig view]
GeneID 853653; -.
GenomeReviews Y13137_GR; YKL182W.
KEGG sce:YKL182W; -.
NMPDR fig|4932.3.peg.3717; -.
Phylogenomic databases
HOGENOM P07149; -.
Other
LinkHub P07149; -.
NextBio 974569; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Fatty acid biosynthesis; Hydrolase; Lipid synthesis; Lyase; Multifunctional enzyme; NAD; NADP; Oxidoreductase; Phosphoprotein; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   2051  2051     Fatty acid synthase subunit beta. PRO_0000180282
REGION   1    468  468     Acetyltransferase. 
REGION   480    868  389     Enoyl reductase. 
REGION   1144   1626  483     Dehydratase. 
REGION   1627   1845  219     Malonyl/palmitoyl transferase. 
ACT_SITE   274    274        For acetyltransferase activity (By similarity). 
ACT_SITE   1808   1808        For malonyltransferase activity (By similarity). 
MOD_RES   1117   1117        Phosphoserine. 
MOD_RES   1121   1121        Phosphoserine. 
MOD_RES   1124   1124        Phosphoserine. 
MOD_RES   1177   1177        Phosphoserine. 
MOD_RES   1189   1189        Phosphothreonine. 
MOD_RES   1190   1190        Phosphoserine. 
MOD_RES   1191   1191        Phosphoserine. 
CONFLICT   191    191        S -> F (in Ref. 1; AAB59310). 
CONFLICT   212    212        G -> D (in Ref. 3). 
CONFLICT   403    403        D -> G (in Ref. 3). 
CONFLICT   1039   1039        H -> Q (in Ref. 1; AAB59310). 
CONFLICT   1149   1149        W -> R (in Ref. 3). 
CONFLICT   1184   1184        I -> F (in Ref. 1; AAB59310). 
CONFLICT   1290   1292        FEI -> SET (in Ref. 3). 
CONFLICT   1331   1333        WRA -> LRG (in Ref. 1; AAB59310). 
CONFLICT   1407   1411        TSSFF -> IFLFL (in Ref. 3). 
CONFLICT   1559   1559        D -> H (in Ref. 1; AAB59310). 
CONFLICT   1576   1576        P -> L (in Ref. 3). 
CONFLICT   1587   1587        A -> T (in Ref. 3). 
CONFLICT   1631   1631        M -> T (in Ref. 3). 
CONFLICT   1661   1661        V -> G (in Ref. 1; AAB59310). 
STRAND   10     13  4      
STRAND   16     19  4      
TURN   24     26  3      
HELIX   27     40  14      
TURN   46     48  3      
STRAND   50     53  4      
HELIX   57     69  13      
STRAND   74     76  3      
HELIX   81     95  15      
HELIX   101    110  10      
HELIX   116    132  17      
HELIX   144    151  8      
STRAND   156    160  5      
HELIX   169    179  11      
HELIX   181    201  21      
STRAND   202    204  3      
HELIX   205    208  4      
HELIX   215    220  6      
HELIX   222    224  3      
HELIX   228    232  5      
HELIX   234    256  23      
HELIX   260    265  6      
STRAND   267    273  7      
HELIX   274    276  3      
HELIX   277    284  8      
HELIX   289    313  25      
HELIX   321    329  9      
STRAND   337    344  8      
HELIX   346    358  13      
HELIX   362    364  3      
STRAND   367    370  4      
STRAND   373    375  3      
STRAND   377    381  5      
HELIX   383    396  14      
HELIX   404    406  3      
HELIX   409    411  3      
STRAND   417    420  4      
TURN   430    432  3      
HELIX   433    444  12      
STRAND   445    447  3      
TURN   452    454  3      
TURN   462    464  3      
STRAND   466    470  5      
HELIX   475    484  10      
HELIX   490    493  4      
STRAND   499    503  5      
STRAND   505    507  3      
HELIX   508    510  3      
HELIX   512    520  9      
STRAND   526    529  4      
STRAND   540    542  3      
TURN   544    548  5      
HELIX   552    554  3      
HELIX   561    564  4      
STRAND   568    571  4      
STRAND   577    580  4      
HELIX   582    587  6      
STRAND   591    594  4      
HELIX   598    601  4      
HELIX   604    612  9      
STRAND   616    620  5      
HELIX   621    623  3      
HELIX   627    640  14      
STRAND   647    652  6      
HELIX   658    671  14      
STRAND   675    684  10      
HELIX   688    697  10      
STRAND   703    705  3      
HELIX   710    722  13      
STRAND   728    732  5      
STRAND   738    740  3      
HELIX   748    757  10      
STRAND   766    770  5      
HELIX   774    777  4      
HELIX   778    780  3