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P19097

- FAS2_YEAST

UniProt

P19097 - FAS2_YEAST

Protein

Fatty acid synthase subunit alpha

Gene

FAS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (15 May 2002)
      Previous versions | rss
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    Functioni

    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. This subunit coordinates the binding of the six beta subunits to the enzyme complex.

    Catalytic activityi

    Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+.
    Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].
    (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.

    Enzyme regulationi

    Inhibited by cerulenin by covalent binding to active site of the ketoacyl synthase (KS) region.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei1305 – 13051For beta-ketoacyl synthase activity
    Metal bindingi1772 – 17721Magnesium
    Metal bindingi1773 – 17731Magnesium; via carbonyl oxygen
    Metal bindingi1774 – 17741Magnesium
    Binding sitei1798 – 17981Acetyl-CoA1 Publication
    Binding sitei1808 – 18081Acetyl-CoA1 Publication
    Metal bindingi1872 – 18721Magnesium
    Metal bindingi1873 – 18731Magnesium; via carbonyl oxygen

    GO - Molecular functioni

    1. 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: SGD
    2. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: SGD
    3. fatty-acyl-CoA synthase activity Source: UniProtKB-EC
    4. holo-[acyl-carrier-protein] synthase activity Source: SGD
    5. magnesium ion binding Source: InterPro
    6. protein binding Source: IntAct

    GO - Biological processi

    1. long-chain fatty acid biosynthetic process Source: SGD
    2. macromolecule biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase, Transferase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding, NAD, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:YPL231W-MONOMER.
    YEAST:YPL231W-MONOMER.
    SABIO-RKP19097.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fatty acid synthase subunit alpha (EC:2.3.1.86)
    Including the following 3 domains:
    Acyl carrier
    3-oxoacyl-[acyl-carrier-protein] reductase (EC:1.1.1.100)
    Alternative name(s):
    Beta-ketoacyl reductase
    3-oxoacyl-[acyl-carrier-protein] synthase (EC:2.3.1.41)
    Alternative name(s):
    Beta-ketoacyl synthase
    Gene namesi
    Name:FAS2
    Ordered Locus Names:YPL231W
    ORF Names:P1409
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XVI

    Organism-specific databases

    CYGDiYPL231w.
    SGDiS000006152. FAS2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. fatty acid synthase complex Source: SGD

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1250 – 12501G → S: Cerulenin-resistance. 1 Publication
    Mutagenesisi1769 – 17691V → D: Does not affect oligomerization; when associated with S-1771 and L-1773 or S-1771; L-1773; S-1879 and E-1881. 1 Publication
    Mutagenesisi1770 – 17701G → D: Loss of transferase activity. 1 Publication
    Mutagenesisi1771 – 17711V → S: Does not affect oligomerization but lacks transferase activity; when associated with D-1769 and L-1773 or D-1769; L-1773; S-1879 and E-1881. 1 Publication
    Mutagenesisi1772 – 17721D → S: Loss of transferase activity; when associated with S-1774. 1 Publication
    Mutagenesisi1773 – 17731V → L: Does not affect oligomerization but lacks transferase activity; when associated with D-1769 and S-1771 or D-1769; S-1771; S-1879 and E-1881. 1 Publication
    Mutagenesisi1774 – 17741E → S: Loss of transferase activity; when associated with S-1772. 1 Publication
    Mutagenesisi1841 – 18411R → A: Loss off transferase activity. 1 Publication
    Mutagenesisi1879 – 18791V → S: Does not affect oligomerization but lacks transferase activity; when associated with D-1769; S-1771; L-1773 and E-1881. 1 Publication
    Mutagenesisi1881 – 18811V → E: Does not affect oligomerization but lacks transferase activity; when associated with D-1769; S-1771; L-1773 and S-1879. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18871887Fatty acid synthase subunit alphaPRO_0000180287Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei50 – 501Phosphoserine1 Publication
    Modified residuei180 – 1801O-(pantetheine 4'-phosphoryl)serine1 Publication
    Modified residuei523 – 5231Phosphoserine1 Publication
    Modified residuei958 – 9581Phosphoserine1 Publication
    Modified residuei1440 – 14401Phosphoserine1 Publication

    Post-translational modificationi

    4'-phosphopantetheine is transferred from CoA to a specific serine of the Acyl carrier domain by the C-terminal PPT domain. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.

    Keywords - PTMi

    Phosphopantetheine, Phosphoprotein

    Proteomic databases

    MaxQBiP19097.
    PaxDbiP19097.
    PeptideAtlasiP19097.

    Expressioni

    Gene expression databases

    GenevestigatoriP19097.

    Interactioni

    Subunit structurei

    [Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta).4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FAS1P071493EBI-6806,EBI-6795

    Protein-protein interaction databases

    BioGridi35931. 48 interactions.
    DIPiDIP-960N.
    IntActiP19097. 17 interactions.
    MINTiMINT-659193.
    STRINGi4932.YPL231W.

    Structurei

    Secondary structure

    1
    1887
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 2018
    Turni21 – 233
    Helixi28 – 3710
    Beta strandi42 – 5110
    Helixi52 – 6413
    Helixi66 – 716
    Beta strandi77 – 804
    Turni81 – 833
    Helixi85 – 884
    Helixi147 – 15711
    Turni158 – 1603
    Turni163 – 1653
    Helixi172 – 1765
    Helixi180 – 19415
    Turni201 – 2033
    Helixi206 – 21611
    Helixi223 – 23614
    Helixi243 – 25210
    Turni258 – 2603
    Helixi261 – 27010
    Helixi280 – 29819
    Helixi329 – 35022
    Helixi356 – 38227
    Helixi384 – 3896
    Helixi396 – 3983
    Beta strandi400 – 4023
    Helixi405 – 42117
    Helixi430 – 44011
    Helixi445 – 45612
    Helixi460 – 4623
    Helixi464 – 48320
    Beta strandi497 – 5037
    Beta strandi509 – 5157
    Helixi522 – 53110
    Turni605 – 6073
    Helixi609 – 6157
    Helixi626 – 6294
    Beta strandi637 – 6437
    Beta strandi649 – 6513
    Helixi653 – 66816
    Beta strandi677 – 6826
    Beta strandi685 – 6873
    Helixi688 – 69811
    Beta strandi702 – 7098
    Helixi712 – 72514
    Beta strandi731 – 7366
    Helixi742 – 75312
    Turni756 – 7594
    Beta strandi766 – 7705
    Helixi781 – 7833
    Helixi786 – 79510
    Helixi797 – 81115
    Turni812 – 8143
    Beta strandi820 – 8267
    Helixi839 – 8457
    Helixi846 – 8483
    Helixi849 – 8557
    Turni859 – 8613
    Beta strandi862 – 8698
    Helixi885 – 8895
    Helixi898 – 9069
    Helixi907 – 9093
    Helixi911 – 9199
    Beta strandi922 – 9276
    Turni930 – 9323
    Beta strandi933 – 9353
    Helixi936 – 96833
    Turni971 – 9766
    Helixi998 – 10047
    Helixi1007 – 10093
    Turni1010 – 10123
    Helixi1015 – 10173
    Beta strandi1019 – 102810
    Helixi1033 – 104210
    Helixi1047 – 105610
    Beta strandi1059 – 10679
    Beta strandi1070 – 10778
    Turni1078 – 10803
    Helixi1086 – 10883
    Helixi1089 – 109911
    Beta strandi1101 – 11055
    Helixi1108 – 11114
    Beta strandi1118 – 11269
    Beta strandi1134 – 11363
    Helixi1138 – 114811
    Helixi1149 – 11513
    Beta strandi1152 – 11565
    Turni1158 – 11603
    Beta strandi1163 – 11675
    Beta strandi1172 – 11798
    Beta strandi1185 – 11873
    Turni1195 – 11995
    Helixi1202 – 12076
    Helixi1210 – 122516
    Helixi1231 – 12333
    Helixi1234 – 12374
    Helixi1240 – 12423
    Beta strandi1243 – 12453
    Beta strandi1248 – 12514
    Helixi1254 – 12618
    Turni1262 – 12676
    Helixi1274 – 12785
    Helixi1282 – 12909
    Helixi1304 – 13063
    Helixi1307 – 132014
    Beta strandi1325 – 13339
    Helixi1337 – 13459
    Helixi1352 – 13576
    Helixi1362 – 13643
    Beta strandi1381 – 13899
    Helixi1390 – 13967
    Beta strandi1402 – 14109
    Helixi1424 – 14296
    Helixi1441 – 14433
    Helixi1445 – 147430
    Helixi1483 – 150826
    Turni1512 – 15154
    Beta strandi1517 – 15193
    Helixi1521 – 15277
    Turni1528 – 15303
    Helixi1533 – 15353
    Beta strandi1536 – 15405
    Helixi1547 – 156418
    Beta strandi1572 – 15754
    Helixi1578 – 15814
    Helixi1585 – 15873
    Helixi1588 – 160013
    Beta strandi1612 – 16143
    Helixi1616 – 16205
    Beta strandi1638 – 16458
    Turni1646 – 16483
    Beta strandi1649 – 16568
    Helixi1659 – 16624
    Helixi1667 – 169327
    Helixi1708 – 17103
    Helixi1711 – 17166
    Beta strandi1726 – 17283
    Beta strandi1730 – 17323
    Turni1735 – 17395
    Helixi1742 – 17454
    Beta strandi1769 – 17757
    Helixi1776 – 17783
    Helixi1784 – 17907
    Helixi1793 – 18008
    Beta strandi1802 – 18043
    Helixi1805 – 182319
    Beta strandi1837 – 18426
    Beta strandi1845 – 18517
    Helixi1853 – 18608
    Turni1861 – 18633
    Beta strandi1866 – 18738
    Beta strandi1875 – 188511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PFFX-ray4.00A/D/G671-1744[»]
    2UV8X-ray3.10A/B/C1-1887[»]
    2VKZX-ray4.00A/B/C1-1887[»]
    2WASX-ray1.90A/B/C/D/E/F1766-1887[»]
    2WATX-ray2.20A/B/C/D/E/F1766-1887[»]
    3HMJX-ray4.00A/B/C1-1887[»]
    ProteinModelPortaliP19097.
    SMRiP19097. Positions 1766-1886.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19097.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini140 – 301162Acyl carrierAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni675 – 874200Beta-ketoacyl reductaseAdd
    BLAST
    Regioni1149 – 1363215Beta-ketoacyl synthaseAdd
    BLAST
    Regioni1772 – 17743Acetyl-CoA binding
    Regioni1817 – 183317Acetyl-CoA bindingAdd
    BLAST
    Regioni1841 – 18444Acetyl-CoA binding
    Regioni1871 – 18733Acetyl-CoA binding

    Sequence similaritiesi

    Contains 1 acyl carrier domain.Curated

    Phylogenomic databases

    eggNOGiCOG4982.
    HOGENOMiHOG000177974.
    KOiK00667.
    OMAiIVIQEDL.
    OrthoDBiEOG76QFRJ.

    Family and domain databases

    Gene3Di3.40.366.10. 1 hit.
    3.40.47.10. 3 hits.
    3.40.50.720. 1 hit.
    3.90.470.20. 1 hit.
    HAMAPiMF_00101. AcpS.
    InterProiIPR008278. 4-PPantetheinyl_Trfase_SF.
    IPR001227. Ac_transferase_dom.
    IPR002582. ACPS.
    IPR016035. Acyl_Trfase/lysoPLipase.
    IPR026025. FAS_alpha_yeast.
    IPR018201. Ketoacyl_synth_AS.
    IPR014031. Ketoacyl_synth_C.
    IPR014030. Ketoacyl_synth_N.
    IPR016040. NAD(P)-bd_dom.
    IPR004568. PPantethiene-prot_Trfase_dom.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view]
    PfamiPF01648. ACPS. 1 hit.
    PF00109. ketoacyl-synt. 1 hit.
    PF02801. Ketoacyl-synt_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000454. FAS_yeast_alpha. 1 hit.
    ProDomiPD004282. PPantethiene-prot_Trfase. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF52151. SSF52151. 1 hit.
    SSF53901. SSF53901. 4 hits.
    SSF56214. SSF56214. 1 hit.
    TIGRFAMsiTIGR00556. pantethn_trn. 1 hit.
    PROSITEiPS00606. B_KETOACYL_SYNTHASE. 1 hit.
    PS00012. PHOSPHOPANTETHEINE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19097-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPEVEQELA HILLTELLAY QFASPVRWIE TQDVFLKDFN TERVVEIGPS     50
    PTLAGMAQRT LKNKYESYDA ALSLHREILC YSKDAKEIYY TPDPSELAAK 100
    EEPAKEEAPA PTPAASAPAP AAAAPAPVAA AAPAAAAAEI ADEPVKASLL 150
    LHVLVAHKLK KSLDSIPMSK TIKDLVGGKS TVQNEILGDL GKEFGTTPEK 200
    PEETPLEELA ETFQDTFSGA LGKQSSSLLS RLISSKMPGG FTITVARKYL 250
    QTRWGLPSGR QDGVLLVALS NEPAARLGSE ADAKAFLDSM AQKYASIVGV 300
    DLSSAASASG AAGAGAAAGA AMIDAGALEE ITKDHKVLAR QQLQVLARYL 350
    KMDLDNGERK FLKEKDTVAE LQAQLDYLNA ELGEFFVNGV ATSFSRKKAR 400
    TFDSSWNWAK QSLLSLYFEI IHGVLKNVDR EVVSEAINIM NRSNDALIKF 450
    MEYHISNTDE TKGENYQLVK TLGEQLIENC KQVLDVDPVY KDVAKPTGPK 500
    TAIDKNGNIT YSEEPREKVR KLSQYVQEMA LGGPITKESQ PTIEEDLTRV 550
    YKAISAQADK QDISSSTRVE FEKLYSDLMK FLESSKEIDP SQTTQLAGMD 600
    VEDALDKDST KEVASLPNKS TISKTVSSTI PRETIPFLHL RKKTPAGDWK 650
    YDRQLSSLFL DGLEKAAFNG VTFKDKYVLI TGAGKGSIGA EVLQGLLQGG 700
    AKVVVTTSRF SKQVTDYYQS IYAKYGAKGS TLIVVPFNQG SKQDVEALIE 750
    FIYDTEKNGG LGWDLDAIIP FAAIPEQGIE LEHIDSKSEF AHRIMLTNIL 800
    RMMGCVKKQK SARGIETRPA QVILPMSPNH GTFGGDGMYS ESKLSLETLF 850
    NRWHSESWAN QLTVCGAIIG WTRGTGLMSA NNIIAEGIEK MGVRTFSQKE 900
    MAFNLLGLLT PEVVELCQKS PVMADLNGGL QFVPELKEFT AKLRKELVET 950
    SEVRKAVSIE TALEHKVVNG NSADAAYAQV EIQPRANIQL DFPELKPYKQ 1000
    VKQIAPAELE GLLDLERVIV VTGFAEVGPW GSARTRWEME AFGEFSLEGC 1050
    VEMAWIMGFI SYHNGNLKGR PYTGWVDSKT KEPVDDKDVK AKYETSILEH 1100
    SGIRLIEPEL FNGYNPEKKE MIQEVIVEED LEPFEASKET AEQFKHQHGD 1150
    KVDIFEIPET GEYSVKLLKG ATLYIPKALR FDRLVAGQIP TGWNAKTYGI 1200
    SDDIISQVDP ITLFVLVSVV EAFIASGITD PYEMYKYVHV SEVGNCSGSG 1250
    MGGVSALRGM FKDRFKDEPV QNDILQESFI NTMSAWVNML LISSSGPIKT 1300
    PVGACATSVE SVDIGVETIL SGKARICIVG GYDDFQEEGS FEFGNMKATS 1350
    NTLEEFEHGR TPAEMSRPAT TTRNGFMEAQ GAGIQIIMQA DLALKMGVPI 1400
    YGIVAMAATA TDKIGRSVPA PGKGILTTAR EHHSSVKYAS PNLNMKYRKR 1450
    QLVTREAQIK DWVENELEAL KLEAEEIPSE DQNEFLLERT REIHNEAESQ 1500
    LRAAQQQWGN DFYKRDPRIA PLRGALATYG LTIDDLGVAS FHGTSTKAND 1550
    KNESATINEM MKHLGRSEGN PVIGVFQKFL TGHPKGAAGA WMMNGALQIL 1600
    NSGIIPGNRN ADNVDKILEQ FEYVLYPSKT LKTDGVRAVS ITSFGFGQKG 1650
    GQAIVVHPDY LYGAITEDRY NEYVAKVSAR EKSAYKFFHN GMIYNKLFVS 1700
    KEHAPYTDEL EEDVYLDPLA RVSKDKKSGS LTFNSKNIQS KDSYINANTI 1750
    ETAKMIENMT KEKVSNGGVG VDVELITSIN VENDTFIERN FTPQEIEYCS 1800
    AQPSVQSSFA GTWSAKEAVF KSLGVKSLGG GAALKDIEIV RVNKNAPAVE 1850
    LHGNAKKAAE EAGVTDVKVS ISHDDLQAVA VAVSTKK 1887
    Length:1,887
    Mass (Da):206,947
    Last modified:May 15, 2002 - v2
    Checksum:i08B872734CF3AEEA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti310 – 3101G → GTTGTGG in AAA34601. (PubMed:2900835)Curated
    Sequence conflicti594 – 5941T → I in AAA34601. (PubMed:2900835)Curated
    Sequence conflicti941 – 101979AKLRK…LERVI → CLNCVKSWLKLLKLERQFPS KLLWSIRLSMAIALMLHMLK SKFNQELTFNWTSQNRNHTN RLNKLLPLSLRVCWIWKELF in AAA34601. (PubMed:2900835)CuratedAdd
    BLAST
    Sequence conflicti1036 – 10416RWEMEA → KMGNGS in AAA34601. (PubMed:2900835)Curated
    Sequence conflicti1408 – 14081A → S in AAA34601. (PubMed:2900835)Curated
    Sequence conflicti1671 – 16711N → T in AAA34601. (PubMed:2900835)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03936 Genomic DNA. Translation: AAA34601.1.
    X76890 Genomic DNA. Translation: CAA54218.1.
    X94561 Genomic DNA. Translation: CAA64256.1.
    Z73586 Genomic DNA. Translation: CAA97947.1.
    Z73587 Genomic DNA. Translation: CAA97948.1.
    BK006949 Genomic DNA. Translation: DAA11205.1.
    PIRiS61703.
    RefSeqiNP_015093.1. NM_001184045.1.

    Genome annotation databases

    EnsemblFungiiYPL231W; YPL231W; YPL231W.
    GeneIDi855845.
    KEGGisce:YPL231W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03936 Genomic DNA. Translation: AAA34601.1 .
    X76890 Genomic DNA. Translation: CAA54218.1 .
    X94561 Genomic DNA. Translation: CAA64256.1 .
    Z73586 Genomic DNA. Translation: CAA97947.1 .
    Z73587 Genomic DNA. Translation: CAA97948.1 .
    BK006949 Genomic DNA. Translation: DAA11205.1 .
    PIRi S61703.
    RefSeqi NP_015093.1. NM_001184045.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PFF X-ray 4.00 A/D/G 671-1744 [» ]
    2UV8 X-ray 3.10 A/B/C 1-1887 [» ]
    2VKZ X-ray 4.00 A/B/C 1-1887 [» ]
    2WAS X-ray 1.90 A/B/C/D/E/F 1766-1887 [» ]
    2WAT X-ray 2.20 A/B/C/D/E/F 1766-1887 [» ]
    3HMJ X-ray 4.00 A/B/C 1-1887 [» ]
    ProteinModelPortali P19097.
    SMRi P19097. Positions 1766-1886.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35931. 48 interactions.
    DIPi DIP-960N.
    IntActi P19097. 17 interactions.
    MINTi MINT-659193.
    STRINGi 4932.YPL231W.

    Proteomic databases

    MaxQBi P19097.
    PaxDbi P19097.
    PeptideAtlasi P19097.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YPL231W ; YPL231W ; YPL231W .
    GeneIDi 855845.
    KEGGi sce:YPL231W.

    Organism-specific databases

    CYGDi YPL231w.
    SGDi S000006152. FAS2.

    Phylogenomic databases

    eggNOGi COG4982.
    HOGENOMi HOG000177974.
    KOi K00667.
    OMAi IVIQEDL.
    OrthoDBi EOG76QFRJ.

    Enzyme and pathway databases

    BioCyci MetaCyc:YPL231W-MONOMER.
    YEAST:YPL231W-MONOMER.
    SABIO-RK P19097.

    Miscellaneous databases

    EvolutionaryTracei P19097.
    NextBioi 980431.

    Gene expression databases

    Genevestigatori P19097.

    Family and domain databases

    Gene3Di 3.40.366.10. 1 hit.
    3.40.47.10. 3 hits.
    3.40.50.720. 1 hit.
    3.90.470.20. 1 hit.
    HAMAPi MF_00101. AcpS.
    InterProi IPR008278. 4-PPantetheinyl_Trfase_SF.
    IPR001227. Ac_transferase_dom.
    IPR002582. ACPS.
    IPR016035. Acyl_Trfase/lysoPLipase.
    IPR026025. FAS_alpha_yeast.
    IPR018201. Ketoacyl_synth_AS.
    IPR014031. Ketoacyl_synth_C.
    IPR014030. Ketoacyl_synth_N.
    IPR016040. NAD(P)-bd_dom.
    IPR004568. PPantethiene-prot_Trfase_dom.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view ]
    Pfami PF01648. ACPS. 1 hit.
    PF00109. ketoacyl-synt. 1 hit.
    PF02801. Ketoacyl-synt_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000454. FAS_yeast_alpha. 1 hit.
    ProDomi PD004282. PPantethiene-prot_Trfase. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF52151. SSF52151. 1 hit.
    SSF53901. SSF53901. 4 hits.
    SSF56214. SSF56214. 1 hit.
    TIGRFAMsi TIGR00556. pantethn_trn. 1 hit.
    PROSITEi PS00606. B_KETOACYL_SYNTHASE. 1 hit.
    PS00012. PHOSPHOPANTETHEINE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of the multifunctional alpha subunit protein of yeast fatty acid synthase derived from FAS2 gene sequence."
      Mohamed A.H., Chirala S.S., Mody N.H., Huang W.Y., Wakil S.J.
      J. Biol. Chem. 263:12315-12325(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Schueller H.-J.
      Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 26786 / X2180-1A.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
      Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
      , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
      Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Cerulenin-resistant mutants of Saccharomyces cerevisiae with an altered fatty acid synthase gene."
      Inokoshi J., Tomoda H., Hashimoto H., Watanabe A., Takeshima H., Omura S.
      Mol. Gen. Genet. 244:90-96(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-1250.
      Strain: ATCC 204508 / S288c.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-958 AND SER-1440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    9. "Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
      Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
      Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    10. "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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together."
      Lomakin I.B., Xiong Y., Steitz T.A.
      Cell 129:319-332(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 671-1744 IN COMPLEX WITH FAS1, SUBUNIT.
    14. "Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase."
      Leibundgut M., Jenni S., Frick C., Ban N.
      Science 316:288-290(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH FAS1, SUBUNIT, PHOSPHOPANTETHEINYLATION AT SER-180.
    15. Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) IN COMPLEX WITH FAS1 AND THE INHIBITOR CERULENIN, ENZYME REGULATION.
    16. "Multimeric options for the auto-activation of the Saccharomyces cerevisiae FAS type I megasynthase."
      Johansson P., Mulinacci B., Koestler C., Vollrath R., Oesterhelt D., Grininger M.
      Structure 17:1063-1074(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1766-1887 IN COMPLEX WITH FAS1 AND ACETYL-COA, MUTAGENESIS OF VAL-1769; GLY-1770; VAL-1771; ASP-1772; VAL-1773; GLU-1774; ARG-1841; VAL-1879 AND VAL-1881, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiFAS2_YEAST
    AccessioniPrimary (citable) accession number: P19097
    Secondary accession number(s): D6W3D9, Q12533
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: May 15, 2002
    Last modified: October 1, 2014
    This is version 159 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 17000 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

    External Data

    Dasty 3