Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P19097

- FAS2_YEAST

UniProt

P19097 - FAS2_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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

GO - Biological processi

  1. long-chain 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 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. 49 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 – 2018Combined sources
Turni21 – 233Combined sources
Helixi28 – 3710Combined sources
Beta strandi42 – 5110Combined sources
Helixi52 – 6413Combined sources
Helixi66 – 716Combined sources
Beta strandi77 – 804Combined sources
Turni81 – 833Combined sources
Helixi85 – 884Combined sources
Helixi147 – 15711Combined sources
Turni158 – 1603Combined sources
Turni163 – 1653Combined sources
Helixi172 – 1765Combined sources
Helixi180 – 19415Combined sources
Turni201 – 2033Combined sources
Helixi206 – 21611Combined sources
Helixi223 – 23614Combined sources
Helixi243 – 25210Combined sources
Turni258 – 2603Combined sources
Helixi261 – 27010Combined sources
Helixi280 – 29819Combined sources
Helixi329 – 35022Combined sources
Helixi356 – 38227Combined sources
Helixi384 – 3896Combined sources
Helixi396 – 3983Combined sources
Beta strandi400 – 4023Combined sources
Helixi405 – 42117Combined sources
Helixi430 – 44011Combined sources
Helixi445 – 45612Combined sources
Helixi460 – 4623Combined sources
Helixi464 – 48320Combined sources
Beta strandi497 – 5037Combined sources
Beta strandi509 – 5157Combined sources
Helixi522 – 53110Combined sources
Turni605 – 6073Combined sources
Helixi609 – 6157Combined sources
Helixi626 – 6294Combined sources
Beta strandi637 – 6437Combined sources
Beta strandi649 – 6513Combined sources
Helixi653 – 66816Combined sources
Beta strandi677 – 6826Combined sources
Beta strandi685 – 6873Combined sources
Helixi688 – 69811Combined sources
Beta strandi702 – 7098Combined sources
Helixi712 – 72514Combined sources
Beta strandi731 – 7366Combined sources
Helixi742 – 75312Combined sources
Turni756 – 7594Combined sources
Beta strandi766 – 7705Combined sources
Helixi781 – 7833Combined sources
Helixi786 – 79510Combined sources
Helixi797 – 81115Combined sources
Turni812 – 8143Combined sources
Beta strandi820 – 8267Combined sources
Helixi839 – 8457Combined sources
Helixi846 – 8483Combined sources
Helixi849 – 8557Combined sources
Turni859 – 8613Combined sources
Beta strandi862 – 8698Combined sources
Helixi885 – 8895Combined sources
Helixi898 – 9069Combined sources
Helixi907 – 9093Combined sources
Helixi911 – 9199Combined sources
Beta strandi922 – 9276Combined sources
Turni930 – 9323Combined sources
Beta strandi933 – 9353Combined sources
Helixi936 – 96833Combined sources
Turni971 – 9766Combined sources
Helixi998 – 10047Combined sources
Helixi1007 – 10093Combined sources
Turni1010 – 10123Combined sources
Helixi1015 – 10173Combined sources
Beta strandi1019 – 102810Combined sources
Helixi1033 – 104210Combined sources
Helixi1047 – 105610Combined sources
Beta strandi1059 – 10679Combined sources
Beta strandi1070 – 10778Combined sources
Turni1078 – 10803Combined sources
Helixi1086 – 10883Combined sources
Helixi1089 – 109911Combined sources
Beta strandi1101 – 11055Combined sources
Helixi1108 – 11114Combined sources
Beta strandi1118 – 11269Combined sources
Beta strandi1134 – 11363Combined sources
Helixi1138 – 114811Combined sources
Helixi1149 – 11513Combined sources
Beta strandi1152 – 11565Combined sources
Turni1158 – 11603Combined sources
Beta strandi1163 – 11675Combined sources
Beta strandi1172 – 11798Combined sources
Beta strandi1185 – 11873Combined sources
Turni1195 – 11995Combined sources
Helixi1202 – 12076Combined sources
Helixi1210 – 122516Combined sources
Helixi1231 – 12333Combined sources
Helixi1234 – 12374Combined sources
Helixi1240 – 12423Combined sources
Beta strandi1243 – 12453Combined sources
Beta strandi1248 – 12514Combined sources
Helixi1254 – 12618Combined sources
Turni1262 – 12676Combined sources
Helixi1274 – 12785Combined sources
Helixi1282 – 12909Combined sources
Helixi1304 – 13063Combined sources
Helixi1307 – 132014Combined sources
Beta strandi1325 – 13339Combined sources
Helixi1337 – 13459Combined sources
Helixi1352 – 13576Combined sources
Helixi1362 – 13643Combined sources
Beta strandi1381 – 13899Combined sources
Helixi1390 – 13967Combined sources
Beta strandi1402 – 14109Combined sources
Helixi1424 – 14296Combined sources
Helixi1441 – 14433Combined sources
Helixi1445 – 147430Combined sources
Helixi1483 – 150826Combined sources
Turni1512 – 15154Combined sources
Beta strandi1517 – 15193Combined sources
Helixi1521 – 15277Combined sources
Turni1528 – 15303Combined sources
Helixi1533 – 15353Combined sources
Beta strandi1536 – 15405Combined sources
Helixi1547 – 156418Combined sources
Beta strandi1572 – 15754Combined sources
Helixi1578 – 15814Combined sources
Helixi1585 – 15873Combined sources
Helixi1588 – 160013Combined sources
Beta strandi1612 – 16143Combined sources
Helixi1616 – 16205Combined sources
Beta strandi1638 – 16458Combined sources
Turni1646 – 16483Combined sources
Beta strandi1649 – 16568Combined sources
Helixi1659 – 16624Combined sources
Helixi1667 – 169327Combined sources
Helixi1708 – 17103Combined sources
Helixi1711 – 17166Combined sources
Beta strandi1726 – 17283Combined sources
Beta strandi1730 – 17323Combined sources
Turni1735 – 17395Combined sources
Helixi1742 – 17454Combined sources
Beta strandi1769 – 17757Combined sources
Helixi1776 – 17783Combined sources
Helixi1784 – 17907Combined sources
Helixi1793 – 18008Combined sources
Beta strandi1802 – 18043Combined sources
Helixi1805 – 182319Combined sources
Beta strandi1837 – 18426Combined sources
Beta strandi1845 – 18517Combined sources
Helixi1853 – 18608Combined sources
Turni1861 – 18633Combined sources
Beta strandi1866 – 18738Combined sources
Beta strandi1875 – 188511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP19097.
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

        10         20         30         40         50
MKPEVEQELA HILLTELLAY QFASPVRWIE TQDVFLKDFN TERVVEIGPS
60 70 80 90 100
PTLAGMAQRT LKNKYESYDA ALSLHREILC YSKDAKEIYY TPDPSELAAK
110 120 130 140 150
EEPAKEEAPA PTPAASAPAP AAAAPAPVAA AAPAAAAAEI ADEPVKASLL
160 170 180 190 200
LHVLVAHKLK KSLDSIPMSK TIKDLVGGKS TVQNEILGDL GKEFGTTPEK
210 220 230 240 250
PEETPLEELA ETFQDTFSGA LGKQSSSLLS RLISSKMPGG FTITVARKYL
260 270 280 290 300
QTRWGLPSGR QDGVLLVALS NEPAARLGSE ADAKAFLDSM AQKYASIVGV
310 320 330 340 350
DLSSAASASG AAGAGAAAGA AMIDAGALEE ITKDHKVLAR QQLQVLARYL
360 370 380 390 400
KMDLDNGERK FLKEKDTVAE LQAQLDYLNA ELGEFFVNGV ATSFSRKKAR
410 420 430 440 450
TFDSSWNWAK QSLLSLYFEI IHGVLKNVDR EVVSEAINIM NRSNDALIKF
460 470 480 490 500
MEYHISNTDE TKGENYQLVK TLGEQLIENC KQVLDVDPVY KDVAKPTGPK
510 520 530 540 550
TAIDKNGNIT YSEEPREKVR KLSQYVQEMA LGGPITKESQ PTIEEDLTRV
560 570 580 590 600
YKAISAQADK QDISSSTRVE FEKLYSDLMK FLESSKEIDP SQTTQLAGMD
610 620 630 640 650
VEDALDKDST KEVASLPNKS TISKTVSSTI PRETIPFLHL RKKTPAGDWK
660 670 680 690 700
YDRQLSSLFL DGLEKAAFNG VTFKDKYVLI TGAGKGSIGA EVLQGLLQGG
710 720 730 740 750
AKVVVTTSRF SKQVTDYYQS IYAKYGAKGS TLIVVPFNQG SKQDVEALIE
760 770 780 790 800
FIYDTEKNGG LGWDLDAIIP FAAIPEQGIE LEHIDSKSEF AHRIMLTNIL
810 820 830 840 850
RMMGCVKKQK SARGIETRPA QVILPMSPNH GTFGGDGMYS ESKLSLETLF
860 870 880 890 900
NRWHSESWAN QLTVCGAIIG WTRGTGLMSA NNIIAEGIEK MGVRTFSQKE
910 920 930 940 950
MAFNLLGLLT PEVVELCQKS PVMADLNGGL QFVPELKEFT AKLRKELVET
960 970 980 990 1000
SEVRKAVSIE TALEHKVVNG NSADAAYAQV EIQPRANIQL DFPELKPYKQ
1010 1020 1030 1040 1050
VKQIAPAELE GLLDLERVIV VTGFAEVGPW GSARTRWEME AFGEFSLEGC
1060 1070 1080 1090 1100
VEMAWIMGFI SYHNGNLKGR PYTGWVDSKT KEPVDDKDVK AKYETSILEH
1110 1120 1130 1140 1150
SGIRLIEPEL FNGYNPEKKE MIQEVIVEED LEPFEASKET AEQFKHQHGD
1160 1170 1180 1190 1200
KVDIFEIPET GEYSVKLLKG ATLYIPKALR FDRLVAGQIP TGWNAKTYGI
1210 1220 1230 1240 1250
SDDIISQVDP ITLFVLVSVV EAFIASGITD PYEMYKYVHV SEVGNCSGSG
1260 1270 1280 1290 1300
MGGVSALRGM FKDRFKDEPV QNDILQESFI NTMSAWVNML LISSSGPIKT
1310 1320 1330 1340 1350
PVGACATSVE SVDIGVETIL SGKARICIVG GYDDFQEEGS FEFGNMKATS
1360 1370 1380 1390 1400
NTLEEFEHGR TPAEMSRPAT TTRNGFMEAQ GAGIQIIMQA DLALKMGVPI
1410 1420 1430 1440 1450
YGIVAMAATA TDKIGRSVPA PGKGILTTAR EHHSSVKYAS PNLNMKYRKR
1460 1470 1480 1490 1500
QLVTREAQIK DWVENELEAL KLEAEEIPSE DQNEFLLERT REIHNEAESQ
1510 1520 1530 1540 1550
LRAAQQQWGN DFYKRDPRIA PLRGALATYG LTIDDLGVAS FHGTSTKAND
1560 1570 1580 1590 1600
KNESATINEM MKHLGRSEGN PVIGVFQKFL TGHPKGAAGA WMMNGALQIL
1610 1620 1630 1640 1650
NSGIIPGNRN ADNVDKILEQ FEYVLYPSKT LKTDGVRAVS ITSFGFGQKG
1660 1670 1680 1690 1700
GQAIVVHPDY LYGAITEDRY NEYVAKVSAR EKSAYKFFHN GMIYNKLFVS
1710 1720 1730 1740 1750
KEHAPYTDEL EEDVYLDPLA RVSKDKKSGS LTFNSKNIQS KDSYINANTI
1760 1770 1780 1790 1800
ETAKMIENMT KEKVSNGGVG VDVELITSIN VENDTFIERN FTPQEIEYCS
1810 1820 1830 1840 1850
AQPSVQSSFA GTWSAKEAVF KSLGVKSLGG GAALKDIEIV RVNKNAPAVE
1860 1870 1880
LHGNAKKAAE EAGVTDVKVS ISHDDLQAVA VAVSTKK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 49 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.
InParanoidi P19097.
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: November 26, 2014
This is version 161 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