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Protein

Fatty acid synthase subunit alpha

Gene

FAS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei1305For beta-ketoacyl synthase activity1
Metal bindingi1772Magnesium1
Metal bindingi1773Magnesium; via carbonyl oxygen1
Metal bindingi1774Magnesium1
Binding sitei1798Acetyl-CoA1 Publication1
Binding sitei1808Acetyl-CoA1 Publication1
Metal bindingi1872Magnesium1
Metal bindingi1873Magnesium; via carbonyl oxygen1

GO - Molecular functioni

  • 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: SGD
  • 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: SGD
  • 3-oxo-pimeloyl-[acp] methyl ester reductase activity Source: UniProtKB-EC
  • fatty-acyl-CoA synthase activity Source: UniProtKB-EC
  • holo-[acyl-carrier-protein] synthase activity Source: SGD
  • magnesium ion binding Source: InterPro

GO - Biological processi

  • long-chain fatty acid biosynthetic process Source: SGD
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
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL231W.
SGDiS000006152. FAS2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • fatty acid synthase complex Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1250G → S: Cerulenin-resistance. 1 Publication1
Mutagenesisi1769V → D: Does not affect oligomerization; when associated with S-1771 and L-1773 or S-1771; L-1773; S-1879 and E-1881. 1 Publication1
Mutagenesisi1770G → D: Loss of transferase activity. 1 Publication1
Mutagenesisi1771V → 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 Publication1
Mutagenesisi1772D → S: Loss of transferase activity; when associated with S-1774. 1 Publication1
Mutagenesisi1773V → 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 Publication1
Mutagenesisi1774E → S: Loss of transferase activity; when associated with S-1772. 1 Publication1
Mutagenesisi1841R → A: Loss off transferase activity. 1 Publication1
Mutagenesisi1879V → S: Does not affect oligomerization but lacks transferase activity; when associated with D-1769; S-1771; L-1773 and E-1881. 1 Publication1
Mutagenesisi1881V → E: Does not affect oligomerization but lacks transferase activity; when associated with D-1769; S-1771; L-1773 and S-1879. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001802871 – 1887Fatty acid synthase subunit alphaAdd BLAST1887

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei50PhosphoserineCombined sources1
Modified residuei180O-(pantetheine 4'-phosphoryl)serine1 Publication1
Modified residuei523PhosphoserineCombined sources1
Modified residuei958PhosphoserineCombined sources1
Modified residuei1440PhosphoserineCombined sources1

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

Isopeptide bond, Phosphopantetheine, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP19097.
PRIDEiP19097.
TopDownProteomicsiP19097.

PTM databases

iPTMnetiP19097.

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. 55 interactors.
DIPiDIP-960N.
IntActiP19097. 19 interactors.
MINTiMINT-659193.

Structurei

Secondary structure

11887
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 20Combined sources18
Turni21 – 23Combined sources3
Helixi28 – 37Combined sources10
Beta strandi42 – 51Combined sources10
Helixi52 – 64Combined sources13
Helixi66 – 71Combined sources6
Beta strandi77 – 80Combined sources4
Turni81 – 83Combined sources3
Helixi85 – 88Combined sources4
Helixi147 – 157Combined sources11
Turni158 – 160Combined sources3
Turni163 – 165Combined sources3
Helixi172 – 176Combined sources5
Helixi180 – 194Combined sources15
Turni201 – 203Combined sources3
Helixi206 – 216Combined sources11
Helixi223 – 236Combined sources14
Helixi243 – 252Combined sources10
Turni258 – 260Combined sources3
Helixi261 – 270Combined sources10
Beta strandi274 – 276Combined sources3
Helixi280 – 298Combined sources19
Helixi329 – 350Combined sources22
Helixi356 – 382Combined sources27
Helixi384 – 389Combined sources6
Helixi396 – 398Combined sources3
Beta strandi400 – 402Combined sources3
Helixi405 – 421Combined sources17
Helixi430 – 440Combined sources11
Helixi445 – 456Combined sources12
Helixi460 – 462Combined sources3
Helixi464 – 483Combined sources20
Beta strandi497 – 503Combined sources7
Beta strandi509 – 515Combined sources7
Helixi522 – 531Combined sources10
Turni605 – 607Combined sources3
Helixi609 – 615Combined sources7
Helixi626 – 629Combined sources4
Beta strandi637 – 643Combined sources7
Beta strandi649 – 651Combined sources3
Helixi653 – 668Combined sources16
Beta strandi677 – 682Combined sources6
Beta strandi685 – 687Combined sources3
Helixi688 – 698Combined sources11
Beta strandi702 – 709Combined sources8
Helixi712 – 725Combined sources14
Beta strandi731 – 736Combined sources6
Helixi742 – 753Combined sources12
Turni756 – 759Combined sources4
Beta strandi766 – 770Combined sources5
Helixi781 – 783Combined sources3
Helixi786 – 795Combined sources10
Helixi797 – 811Combined sources15
Turni812 – 814Combined sources3
Beta strandi820 – 826Combined sources7
Helixi839 – 845Combined sources7
Helixi846 – 848Combined sources3
Helixi849 – 855Combined sources7
Turni859 – 861Combined sources3
Beta strandi862 – 869Combined sources8
Helixi885 – 889Combined sources5
Helixi898 – 906Combined sources9
Helixi907 – 909Combined sources3
Helixi911 – 919Combined sources9
Beta strandi922 – 927Combined sources6
Turni930 – 932Combined sources3
Beta strandi933 – 935Combined sources3
Helixi936 – 968Combined sources33
Turni971 – 976Combined sources6
Helixi998 – 1004Combined sources7
Helixi1007 – 1009Combined sources3
Turni1010 – 1012Combined sources3
Helixi1015 – 1017Combined sources3
Beta strandi1019 – 1028Combined sources10
Helixi1033 – 1042Combined sources10
Helixi1047 – 1056Combined sources10
Beta strandi1059 – 1067Combined sources9
Beta strandi1070 – 1077Combined sources8
Turni1078 – 1080Combined sources3
Helixi1086 – 1088Combined sources3
Helixi1089 – 1099Combined sources11
Beta strandi1101 – 1105Combined sources5
Helixi1108 – 1111Combined sources4
Beta strandi1118 – 1126Combined sources9
Beta strandi1134 – 1136Combined sources3
Helixi1138 – 1148Combined sources11
Helixi1149 – 1151Combined sources3
Beta strandi1152 – 1156Combined sources5
Turni1158 – 1160Combined sources3
Beta strandi1163 – 1167Combined sources5
Beta strandi1172 – 1179Combined sources8
Beta strandi1185 – 1187Combined sources3
Turni1195 – 1199Combined sources5
Helixi1202 – 1207Combined sources6
Helixi1210 – 1225Combined sources16
Helixi1231 – 1233Combined sources3
Helixi1234 – 1237Combined sources4
Helixi1240 – 1242Combined sources3
Beta strandi1243 – 1245Combined sources3
Beta strandi1248 – 1251Combined sources4
Helixi1254 – 1261Combined sources8
Turni1262 – 1267Combined sources6
Helixi1274 – 1278Combined sources5
Helixi1282 – 1290Combined sources9
Helixi1304 – 1306Combined sources3
Helixi1307 – 1320Combined sources14
Beta strandi1325 – 1333Combined sources9
Helixi1337 – 1345Combined sources9
Helixi1352 – 1357Combined sources6
Helixi1362 – 1364Combined sources3
Beta strandi1381 – 1389Combined sources9
Helixi1390 – 1396Combined sources7
Beta strandi1402 – 1410Combined sources9
Helixi1424 – 1429Combined sources6
Helixi1441 – 1443Combined sources3
Helixi1445 – 1474Combined sources30
Helixi1483 – 1508Combined sources26
Turni1512 – 1515Combined sources4
Beta strandi1517 – 1519Combined sources3
Helixi1521 – 1527Combined sources7
Turni1528 – 1530Combined sources3
Helixi1533 – 1535Combined sources3
Beta strandi1536 – 1540Combined sources5
Helixi1547 – 1564Combined sources18
Beta strandi1572 – 1575Combined sources4
Helixi1578 – 1581Combined sources4
Helixi1585 – 1587Combined sources3
Helixi1588 – 1600Combined sources13
Beta strandi1612 – 1614Combined sources3
Helixi1616 – 1620Combined sources5
Beta strandi1638 – 1645Combined sources8
Turni1646 – 1648Combined sources3
Beta strandi1649 – 1656Combined sources8
Helixi1659 – 1662Combined sources4
Helixi1667 – 1693Combined sources27
Helixi1708 – 1710Combined sources3
Helixi1711 – 1716Combined sources6
Beta strandi1726 – 1728Combined sources3
Beta strandi1730 – 1732Combined sources3
Turni1735 – 1739Combined sources5
Helixi1742 – 1745Combined sources4
Beta strandi1769 – 1775Combined sources7
Helixi1776 – 1778Combined sources3
Helixi1784 – 1790Combined sources7
Helixi1793 – 1800Combined sources8
Beta strandi1802 – 1804Combined sources3
Helixi1805 – 1823Combined sources19
Beta strandi1837 – 1842Combined sources6
Beta strandi1845 – 1851Combined sources7
Helixi1853 – 1860Combined sources8
Turni1861 – 1863Combined sources3
Beta strandi1866 – 1873Combined sources8
Beta strandi1875 – 1885Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ML8NMR-A138-302[»]
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19097.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini140 – 301Acyl carrierAdd BLAST162

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni675 – 874Beta-ketoacyl reductaseAdd BLAST200
Regioni1149 – 1363Beta-ketoacyl synthaseAdd BLAST215
Regioni1772 – 1774Acetyl-CoA binding3
Regioni1817 – 1833Acetyl-CoA bindingAdd BLAST17
Regioni1841 – 1844Acetyl-CoA binding4
Regioni1871 – 1873Acetyl-CoA binding3

Sequence similaritiesi

Contains 1 acyl carrier domain.Curated

Phylogenomic databases

HOGENOMiHOG000177974.
InParanoidiP19097.
KOiK00667.
OMAiMGIFQKY.
OrthoDBiEOG092C010Q.

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. 1 hit.
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. Ppantetheine-prot_Trfase_dom.
IPR016039. Thiolase-like.
[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]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52151. 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)DescriptionActionsGraphical viewLength
Sequence conflicti310G → GTTGTGG in AAA34601 (PubMed:2900835).Curated1
Sequence conflicti594T → I in AAA34601 (PubMed:2900835).Curated1
Sequence conflicti941 – 1019AKLRK…LERVI → CLNCVKSWLKLLKLERQFPS KLLWSIRLSMAIALMLHMLK SKFNQELTFNWTSQNRNHTN RLNKLLPLSLRVCWIWKELF in AAA34601 (PubMed:2900835).CuratedAdd BLAST79
Sequence conflicti1036 – 1041RWEMEA → KMGNGS in AAA34601 (PubMed:2900835).Curated6
Sequence conflicti1408A → S in AAA34601 (PubMed:2900835).Curated1
Sequence conflicti1671N → T in AAA34601 (PubMed:2900835).Curated1

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.
PIRiS61703.
RefSeqiNP_015093.1. NM_001184045.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ML8NMR-A138-302[»]
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35931. 55 interactors.
DIPiDIP-960N.
IntActiP19097. 19 interactors.
MINTiMINT-659193.

PTM databases

iPTMnetiP19097.

Proteomic databases

MaxQBiP19097.
PRIDEiP19097.
TopDownProteomicsiP19097.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YPL231W.
SGDiS000006152. FAS2.

Phylogenomic databases

HOGENOMiHOG000177974.
InParanoidiP19097.
KOiK00667.
OMAiMGIFQKY.
OrthoDBiEOG092C010Q.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP19097.
PROiP19097.

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. 1 hit.
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. Ppantetheine-prot_Trfase_dom.
IPR016039. Thiolase-like.
[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]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52151. 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]
ProtoNetiSearch...

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 2, 2016
This is version 182 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.