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Reviewed, UniProtKB/Swiss-Prot P07149 (FAS1_YEAST)

Last modified June 16, 2009. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Fatty acid synthase subunit beta
    EC=2.3.1.86
Including the following 5 domains:
    1- Recommended name:
            3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
              EC=4.2.1.61
    2- Recommended name:
            Enoyl-[acyl-carrier-protein] reductase [NADH]
              EC=1.3.1.9
    3- Recommended name:
            [Acyl-carrier-protein] acetyltransferase
              EC=2.3.1.38
    4- Recommended name:
            [Acyl-carrier-protein] malonyltransferase
              EC=2.3.1.39
    5- Recommended name:
            S-acyl fatty acid synthase thioesterase
              EC=3.1.2.14
Gene names
Name: FAS1
Ordered Locus Names: YKL182W
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length2051 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (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+.

Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].

Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein].

(3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] = hexadec-2-enoyl-[acyl-carrier-protein] + H2O.

Acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH.

Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.

Subunit structure

[Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta).

Miscellaneous

Present with 91800 molecules/cell in log phase SD medium. Ref.7

Sequence similarities

Belongs to the fungal fatty acid synthetase subunit beta family.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

FAS2P190971EBI-6795,EBI-6806

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20512051Fatty acid synthase subunit beta
PRO_0000180282

Regions

Region1 – 468468Acetyltransferase
Region480 – 868389Enoyl reductase
Region1144 – 1626483Dehydratase
Region1627 – 1845219Malonyl/palmitoyl transferase

Sites

Active site2741For acetyltransferase activity By similarity
Active site18081For malonyltransferase activity By similarity

Amino acid modifications

Modified residue11171Phosphoserine Ref.9
Modified residue11211Phosphoserine Ref.9
Modified residue11241Phosphoserine Ref.9
Modified residue11771Phosphoserine Ref.8
Modified residue11891Phosphothreonine Ref.8
Modified residue11901Phosphoserine Ref.8
Modified residue11911Phosphoserine Ref.8

Experimental info

Sequence conflict1911S → F in AAB59310. Ref.1
Sequence conflict2121G → D Ref.3
Sequence conflict4031D → G Ref.3
Sequence conflict10391H → Q in AAB59310. Ref.1
Sequence conflict11491W → R Ref.3
Sequence conflict11841I → F in AAB59310. Ref.1
Sequence conflict1290 – 12923FEI → SET Ref.3
Sequence conflict1331 – 13333WRA → LRG in AAB59310. Ref.1
Sequence conflict1407 – 14115TSSFF → IFLFL Ref.3
Sequence conflict15591D → H in AAB59310. Ref.1
Sequence conflict15761P → L Ref.3
Sequence conflict15871A → T Ref.3
Sequence conflict16311M → T Ref.3
Sequence conflict16611V → G in AAB59310. Ref.1

Secondary structure

1 .......................................................................................................................................................................................................................................................................................................................................................... 2051
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P07149-1 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 43AA85A6071D8EAA

FASTA2,051228,691
        10         20         30         40         50         60 
MDAYSTRPLT LSHGSLEHVL LVPTASFFIA SQLQEQFNKI LPEPTEGFAA DDEPTTPAEL 

        70         80         90        100        110        120 
VGKFLGYVSS LVEPSKVGQF DQVLNLCLTE FENCYLEGND IHALAAKLLQ ENDTTLVKTK 

       130        140        150        160        170        180 
ELIKNYITAR IMAKRPFDKK SNSALFRAVG EGNAQLVAIF GGQGNTDDYF EELRDLYQTY 

       190        200        210        220        230        240 
HVLVGDLIKF SAETLSELIR TTLDAEKVFT QGLNILEWLE NPSNTPDKDY LLSIPISCPL 

       250        260        270        280        290        300 
IGVIQLAHYV VTAKLLGFTP GELRSYLKGA TGHSQGLVTA VAIAETDSWE SFFVSVRKAI 

       310        320        330        340        350        360 
TVLFFIGVRC YEAYPNTSLP PSILEDSLEN NEGVPSPMLS ISNLTQEQVQ DYVNKTNSHL 

       370        380        390        400        410        420 
PAGKQVEISL VNGAKNLVVS GPPQSLYGLN LTLRKAKAPS GLDQSRIPFS ERKLKFSNRF 

       430        440        450        460        470        480 
LPVASPFHSH LLVPASDLIN KDLVKNNVSF NAKDIQIPVY DTFDGSDLRV LSGSISERIV 

       490        500        510        520        530        540 
DCIIRLPVKW ETTTQFKATH ILDFGPGGAS GLGVLTHRNK DGTGVRVIVA GTLDINPDDD 

       550        560        570        580        590        600 
YGFKQEIFDV TSNGLKKNPN WLEEYHPKLI KNKSGKIFVE TKFSKLIGRP PLLVPGMTPC 

       610        620        630        640        650        660 
TVSPDFVAAT TNAGYTIELA GGGYFSAAGM TAAIDSVVSQ IEKGSTFGIN LIYVNPFMLQ 

       670        680        690        700        710        720 
WGIPLIKELR SKGYPIQFLT IGAGVPSLEV ASEYIETLGL KYLGLKPGSI DAISQVINIA 

       730        740        750        760        770        780 
KAHPNFPIAL QWTGGRGGGH HSFEDAHTPM LQMYSKIRRH PNIMLIFGSG FGSADDTYPY 

       790        800        810        820        830        840 
LTGEWSTKFD YPPMPFDGFL FGSRVMIAKE VKTSPDAKKC IAACTGVPDD KWEQTYKKPT 

       850        860        870        880        890        900 
GGIVTVRSEM GEPIHKIATR GVMLWKEFDE TIFNLPKNKL VPTLEAKRDY IISRLNADFQ 

       910        920        930        940        950        960 
KPWFATVNGQ ARDLATMTYE EVAKRLVELM FIRSTNSWFD VTWRTFTGDF LRRVEERFTK 

       970        980        990       1000       1010       1020 
SKTLSLIQSY SLLDKPDEAI EKVFNAYPAA REQFLNAQDI DHFLSMCQNP MQKPVPFVPV 

      1030       1040       1050       1060       1070       1080 
LDRRFEIFFK KDSLWQSEHL EAVVDQDVQR TCILHGPVAA QFTKVIDEPI KSIMDGIHDG 

      1090       1100       1110       1120       1130       1140 
HIKKLLHQYY GDDESKIPAV EYFGGESPVD VQSQVDSSSV SEDSAVFKAT SSTDEESWFK 

      1150       1160       1170       1180       1190       1200 
ALAGSEINWR HASFLCSFIT QDKMFVSNPI RKVFKPSQGM VVEISNGNTS SKTVVTLSEP 

      1210       1220       1230       1240       1250       1260 
VQGELKPTVI LKLLKENIIQ MEMIENRTMD GKPVSLPLLY NFNPDNGFAP ISEVMEDRNQ 

      1270       1280       1290       1300       1310       1320 
RIKEMYWKLW IDEPFNLDFD PRDVIKGKDF EITAKEVYDF THAVGNNCED FVSRPDRTML 

      1330       1340       1350       1360       1370       1380 
APMDFAIVVG WRAIIKAIFP NTVDGDLLKL VHLSNGYKMI PGAKPLQVGD VVSTTAVIES 

      1390       1400       1410       1420       1430       1440 
VVNQPTGKIV DVVGTLSRNG KPVMEVTSSF FYRGNYTDFE NTFQKTVEPV YQMHIKTSKD 

      1450       1460       1470       1480       1490       1500 
IAVLRSKEWF QLDDEDFDLL NKTLTFETET EVTFKNANIF SSVKCFGPIK VELPTKETVE 

      1510       1520       1530       1540       1550       1560 
IGIVDYEAGA SHGNPVVDFL KRNGSTLEQK VNLENPIPIA VLDSYTPSTN EPYARVSGDL 

      1570       1580       1590       1600       1610       1620 
NPIHVSRHFA SYANLPGTIT HGMFSSASVR ALIENWAADS VSSRVRGYTC QFVDMVLPNT 

      1630       1640       1650       1660       1670       1680 
ALKTSIQHVG MINGRKLIKF ETRNEDDVVV LTGEAEIEQP VTTFVFTGQG SQEQGMGMDL 

      1690       1700       1710       1720       1730       1740 
YKTSKAAQDV WNRADNHFKD TYGFSILDIV INNPVNLTIH FGGEKGKRIR ENYSAMIFET 

      1750       1760       1770       1780       1790       1800 
IVDGKLKTEK IFKEINEHST SYTFRSEKGL LSATQFTQPA LTLMEKAAFE DLKSKGLIPA 

      1810       1820       1830       1840       1850       1860 
DATFAGHSLG EYAALASLAD VMSIESLVEV VFYRGMTMQV AVPRDELGRS NYGMIAINPG 

      1870       1880       1890       1900       1910       1920 
RVAASFSQEA LQYVVERVGK RTGWLVEIVN YNVENQQYVA AGDLRALDTV TNVLNFIKLQ 

      1930       1940       1950       1960       1970       1980 
KIDIIELQKS LSLEEVEGHL FEIIDEASKK SAVKPRPLKL ERGFACIPLV GISVPFHSTY 

      1990       2000       2010       2020       2030       2040 
LMNGVKPFKS FLKKNIIKEN VKVARLAGKY IPNLTAKPFQ VTKEYFQDVY DLTGSEPIKE 

      2050 
IIDNWEKYEQ S

« Hide

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References

« Hide 'large scale' references
[1]"The pentafunctional FAS1 gene of yeast: its nucleotide sequence and order of the catalytic domains."
Schweizer M., Roberts L.M., Hoeltke H.-J., Takabayashi K., Hoellerer E., Hoffmann B., Mueller G., Koettig H., Schweizer E.
Mol. Gen. Genet. 203:479-486(1986) [PubMed: 3528750] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The pentafunctional FAS1 genes of Saccharomyces cerevisiae and Yarrowia lipolytica are co-linear and considerably longer than previously estimated."
Koettig H., Rottner G., Beck K.-F., Schweizer M., Schweizer E.
Mol. Gen. Genet. 226:310-314(1991) [PubMed: 2034224] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"Complementation of mutations and nucleotide sequence of FAS1 gene encoding beta subunit of yeast fatty acid synthase."
Chirala S.S., Kuziora M.A., Spector D.M., Wakil S.J.
J. Biol. Chem. 262:4231-4240(1987) [PubMed: 3031066] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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."
Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J., Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.
Yeast 9:1343-1348(1993) [PubMed: 8154185] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Complete DNA sequence of yeast chromosome XI."
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. expand/collapse author list , 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.
Nature 369:371-378(1994) [PubMed: 8196765] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"Phosphoribosylpyrophosphate synthetase (PRS): a new gene family in Saccharomyces cerevisiae."
Carter A.T., Narbad A., Pearson B.M., Beck K.-F., Logghe M., Contreras R., Schweizer M.
Yeast 10:1031-1044(1994) [PubMed: 7992503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1947-2051.
Strain: ATCC 26786 / X2180-1A.
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
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.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1177; THR-1189; SER-1190 AND SER-1191, MASS SPECTROMETRY.
[9]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1117; SER-1121 AND SER-1124, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X03977 Genomic DNA. Translation: CAA27616.1. Sequence problems.
M30162 Genomic DNA. Translation: AAB59310.1.
X74151 Genomic DNA. Translation: CAA52256.1.
Z28182 Genomic DNA. Translation: CAA82025.1.
X70069 Genomic DNA. Translation: CAA49673.1.
PIRS34688.
RefSeqNP_012739.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2PFFX-ray4.00B/E/H1-1940[»]
2UV8X-ray3.10G/H/I1-2051[»]
2VKZX-ray4.00G/H/I1-2051[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:742N.
IntActP07149. 77 interactions.

Proteomic databases

PeptideAtlasP07149.
PRIDEP07149.

Genome annotation databases

EnsemblYKL182W. Saccharomyces cerevisiae. [Contig view]
GeneID853653.
GenomeReviewsGene locus YKL182W in contig Y13137_GR.
KEGGsce:YKL182W.
NMPDRfig|4932.3.peg.3717.

Organism-specific databases

CYGDYKL182w.
SGDS000001665. FAS1.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP07149.
OMAP07149. SATQFTQ.

Enzyme and pathway databases

BioCycMetaCyc:YKL182W-MON.
BRENDA1.3.1.9. 250.
2.3.1.38. 250.
2.3.1.39. 250.
2.3.1.86. 250.
3.1.2.14. 250.
4.2.1.61. 250.

Gene expression databases

ArrayExpressP07149.
GermOnlineYKL182W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001227. Ac_transferase_reg.
IPR014043. Acyl_transferase.
IPR013565. DUF1729.
IPR003965. Fatty_acid_synthase.
IPR016452. Fatty_acid_Synthase_bsu_fun.
IPR002539. MaoC_deHydtase.
[Graphical view]
Gene3DG3DSA:3.40.366.10. Ac_transferase_reg. 1 hit.
PfamPF00698. Acyl_transf_1. 1 hit.
PF08354. DUF1729. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
[Graphical view]
PIRSFPIRSF005562. FAS_yeast_beta. 1 hit.
PRINTSPR01483. FASYNTHASE.
ProtoNetSearch...

Other Resources

NextBio974569.

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Entry information

Entry nameFAS1_YEAST
AccessionPrimary (citable) accession number: P07149
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents