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P19097

- FAS2_YEAST

UniProt

P19097 - FAS2_YEAST

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Protein
Fatty acid synthase subunit alpha
Gene
FAS2, YPL231W, P1409
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.UniRule annotation

Catalytic activityi

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

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-CoA
Binding sitei1808 – 18081Acetyl-CoA
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. fatty acid biosynthetic process Source: SGD
  2. macromolecule biosynthetic process Source: InterPro
Complete GO annotation...

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
Complete GO annotation...

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 alphaUniRule annotation
PRO_0000180287Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501Phosphoserine1 Publication
Modified residuei180 – 1801O-(pantetheine 4'-phosphoryl)serineUniRule annotation
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.UniRule annotation

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).2 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

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.

Miscellaneous databases

EvolutionaryTraceiP19097.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni675 – 874200Beta-ketoacyl reductaseUniRule annotation
Add
BLAST
Regioni1149 – 1363215Beta-ketoacyl synthaseUniRule annotation
Add
BLAST
Regioni1772 – 17743Acetyl-CoA bindingUniRule annotation
Regioni1817 – 183317Acetyl-CoA bindingUniRule annotation
Add
BLAST
Regioni1841 – 18444Acetyl-CoA bindingUniRule annotation
Regioni1871 – 18733Acetyl-CoA bindingUniRule annotation

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti310 – 3101G → GTTGTGG in AAA34601. 1 Publication
Sequence conflicti594 – 5941T → I in AAA34601. 1 Publication
Sequence conflicti941 – 101979AKLRK…LERVI → CLNCVKSWLKLLKLERQFPS KLLWSIRLSMAIALMLHMLK SKFNQELTFNWTSQNRNHTN RLNKLLPLSLRVCWIWKELF in AAA34601. 1 Publication
Add
BLAST
Sequence conflicti1036 – 10416RWEMEA → KMGNGS in AAA34601. 1 Publication
Sequence conflicti1408 – 14081A → S in AAA34601. 1 Publication
Sequence conflicti1671 – 16711N → T in AAA34601. 1 Publication

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 158 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.

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

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