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P07149

- FAS1_YEAST

UniProt

P07149 - FAS1_YEAST

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Protein

Fatty acid synthase subunit beta

Gene

FAS1

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 beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.

Catalytic activityi

Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+.
Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein].
A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.
An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.
Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei274 – 2741For acetyltransferase activityBy similarity
Active sitei1808 – 18081For malonyltransferase activityBy similarity

GO - Molecular functioni

  1. [acyl-carrier-protein] S-acetyltransferase activity Source: SGD
  2. [acyl-carrier-protein] S-malonyltransferase activity Source: SGD
  3. 3-hydroxyacyl-[acyl-carrier-protein] dehydratase activity Source: SGD
  4. 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
  5. enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: UniProtKB-EC
  6. enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity Source: SGD
  7. fatty-acyl-CoA synthase activity Source: UniProtKB-EC
  8. myristoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  9. oleoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  10. palmitoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  11. palmitoyltransferase activity Source: SGD

GO - Biological processi

  1. long-chain fatty acid biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Lyase, Oxidoreductase, Transferase

Keywords - Biological processi

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

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciMetaCyc:YKL182W-MONOMER.
YEAST:YKL182W-MONOMER.
SABIO-RKP07149.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid synthase subunit beta (EC:2.3.1.86)
Including the following 5 domains:
3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC:4.2.1.59)
Enoyl-[acyl-carrier-protein] reductase [NADH] (EC:1.3.1.9)
[Acyl-carrier-protein] acetyltransferase (EC:2.3.1.38)
[Acyl-carrier-protein] malonyltransferase (EC:2.3.1.39)
S-acyl fatty acid synthase thioesterase (EC:3.1.2.14)
Gene namesi
Name:FAS1
Ordered Locus Names:YKL182W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

CYGDiYKL182w.
SGDiS000001665. FAS1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: SGD
  2. fatty acid synthase complex Source: SGD
  3. lipid particle Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20512051Fatty acid synthase subunit betaPRO_0000180282Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei733 – 7331Phosphothreonine1 Publication
Modified residuei1121 – 11211Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP07149.
PaxDbiP07149.
PeptideAtlasiP07149.

Expressioni

Gene expression databases

GenevestigatoriP07149.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
FAS2P190973EBI-6795,EBI-6806

Protein-protein interaction databases

BioGridi33940. 67 interactions.
DIPiDIP-742N.
IntActiP07149. 77 interactions.
MINTiMINT-1325736.
STRINGi4932.YKL182W.

Structurei

Secondary structure

1
2051
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 134Combined sources
Beta strandi16 – 194Combined sources
Turni24 – 263Combined sources
Helixi27 – 4014Combined sources
Turni46 – 483Combined sources
Beta strandi50 – 534Combined sources
Helixi57 – 6913Combined sources
Beta strandi74 – 763Combined sources
Helixi81 – 9515Combined sources
Helixi101 – 11010Combined sources
Helixi116 – 13217Combined sources
Helixi144 – 1518Combined sources
Beta strandi156 – 1605Combined sources
Helixi169 – 17911Combined sources
Helixi181 – 20121Combined sources
Beta strandi202 – 2043Combined sources
Helixi205 – 2084Combined sources
Helixi215 – 2206Combined sources
Helixi222 – 2243Combined sources
Helixi228 – 2325Combined sources
Helixi234 – 25623Combined sources
Helixi260 – 2656Combined sources
Beta strandi267 – 2737Combined sources
Helixi274 – 2763Combined sources
Helixi277 – 2848Combined sources
Helixi289 – 31325Combined sources
Helixi321 – 3299Combined sources
Beta strandi337 – 3448Combined sources
Helixi346 – 35813Combined sources
Helixi362 – 3643Combined sources
Beta strandi367 – 3704Combined sources
Beta strandi373 – 3753Combined sources
Beta strandi377 – 3815Combined sources
Helixi383 – 39614Combined sources
Helixi404 – 4063Combined sources
Helixi409 – 4113Combined sources
Beta strandi417 – 4204Combined sources
Turni430 – 4323Combined sources
Helixi433 – 44412Combined sources
Beta strandi445 – 4473Combined sources
Turni452 – 4543Combined sources
Turni462 – 4643Combined sources
Beta strandi466 – 4705Combined sources
Helixi475 – 48410Combined sources
Helixi490 – 4934Combined sources
Beta strandi499 – 5035Combined sources
Beta strandi505 – 5073Combined sources
Helixi508 – 5103Combined sources
Helixi512 – 5209Combined sources
Beta strandi526 – 5294Combined sources
Beta strandi540 – 5423Combined sources
Turni544 – 5485Combined sources
Helixi552 – 5543Combined sources
Helixi561 – 5644Combined sources
Beta strandi568 – 5714Combined sources
Beta strandi577 – 5804Combined sources
Helixi582 – 5876Combined sources
Beta strandi591 – 5944Combined sources
Helixi598 – 6014Combined sources
Helixi604 – 6129Combined sources
Beta strandi616 – 6205Combined sources
Helixi621 – 6233Combined sources
Helixi627 – 64014Combined sources
Beta strandi647 – 6526Combined sources
Helixi658 – 67114Combined sources
Beta strandi675 – 68410Combined sources
Helixi688 – 69710Combined sources
Beta strandi703 – 7053Combined sources
Helixi710 – 72213Combined sources
Beta strandi728 – 7325Combined sources
Beta strandi738 – 7403Combined sources
Helixi748 – 75710Combined sources
Beta strandi766 – 7705Combined sources
Helixi774 – 7774Combined sources
Helixi778 – 7803Combined sources
Turni781 – 7833Combined sources
Helixi785 – 7873Combined sources
Turni788 – 7903Combined sources
Helixi803 – 8053Combined sources
Helixi815 – 8228Combined sources
Helixi829 – 8368Combined sources
Beta strandi841 – 8477Combined sources
Beta strandi853 – 8575Combined sources
Helixi860 – 87011Combined sources
Turni871 – 8744Combined sources
Turni877 – 8793Combined sources
Helixi880 – 8856Combined sources
Helixi888 – 89811Combined sources
Helixi914 – 9163Combined sources
Helixi919 – 93012Combined sources
Turni933 – 9364Combined sources
Beta strandi937 – 9393Combined sources
Helixi941 – 95818Combined sources
Helixi970 – 9745Combined sources
Helixi976 – 98611Combined sources
Helixi988 – 9914Combined sources
Helixi997 – 100610Combined sources
Beta strandi1010 – 10123Combined sources
Beta strandi1016 – 10183Combined sources
Helixi1025 – 10306Combined sources
Helixi1035 – 10384Combined sources
Helixi1040 – 10423Combined sources
Helixi1048 – 10503Combined sources
Turni1057 – 10626Combined sources
Helixi1070 – 109021Combined sources
Helixi1094 – 10963Combined sources
Beta strandi1125 – 11284Combined sources
Helixi1135 – 11439Combined sources
Helixi1149 – 11557Combined sources
Beta strandi1158 – 11614Combined sources
Beta strandi1164 – 11674Combined sources
Helixi1169 – 11746Combined sources
Beta strandi1181 – 11866Combined sources
Helixi1190 – 11923Combined sources
Beta strandi1194 – 12018Combined sources
Beta strandi1204 – 121411Combined sources
Turni1215 – 12173Combined sources
Beta strandi1218 – 12258Combined sources
Beta strandi1229 – 12324Combined sources
Beta strandi1234 – 12418Combined sources
Helixi1258 – 127013Combined sources
Helixi1294 – 130411Combined sources
Helixi1323 – 13253Combined sources
Helixi1326 – 133510Combined sources
Helixi1336 – 13383Combined sources
Helixi1341 – 13433Combined sources
Helixi1347 – 13493Combined sources
Beta strandi1350 – 135910Combined sources
Beta strandi1367 – 13693Combined sources
Beta strandi1375 – 13839Combined sources
Beta strandi1385 – 139814Combined sources
Beta strandi1401 – 141414Combined sources
Helixi1419 – 14213Combined sources
Beta strandi1423 – 143412Combined sources
Helixi1438 – 14469Combined sources
Beta strandi1450 – 14545Combined sources
Beta strandi1463 – 147412Combined sources
Beta strandi1476 – 14783Combined sources
Beta strandi1480 – 149213Combined sources
Beta strandi1498 – 151013Combined sources
Helixi1515 – 15228Combined sources
Beta strandi1524 – 15274Combined sources
Beta strandi1529 – 154517Combined sources
Helixi1551 – 15577Combined sources
Helixi1562 – 15643Combined sources
Helixi1567 – 15726Combined sources
Beta strandi1576 – 15783Combined sources
Helixi1582 – 159716Combined sources
Helixi1602 – 16043Combined sources
Beta strandi1605 – 16128Combined sources
Beta strandi1621 – 163212Combined sources
Beta strandi1635 – 16439Combined sources
Beta strandi1649 – 165810Combined sources
Beta strandi1662 – 16665Combined sources
Turni1674 – 16774Combined sources
Helixi1678 – 16836Combined sources
Helixi1685 – 170218Combined sources
Helixi1706 – 17116Combined sources
Beta strandi1715 – 17206Combined sources
Helixi1724 – 173411Combined sources
Beta strandi1749 – 17546Combined sources
Beta strandi1761 – 17655Combined sources
Helixi1770 – 17723Combined sources
Helixi1774 – 179421Combined sources
Beta strandi1803 – 18064Combined sources
Helixi1810 – 181910Combined sources
Helixi1824 – 184017Combined sources
Beta strandi1850 – 18578Combined sources
Helixi1859 – 18624Combined sources
Helixi1868 – 188215Combined sources
Beta strandi1886 – 18938Combined sources
Turni1894 – 18963Combined sources
Beta strandi1897 – 19037Combined sources
Helixi1904 – 191916Combined sources
Helixi1924 – 19307Combined sources
Helixi1933 – 195220Combined sources
Beta strandi1964 – 19685Combined sources
Helixi1979 – 19813Combined sources
Helixi1988 – 19936Combined sources
Helixi1998 – 20003Combined sources
Helixi2003 – 20064Combined sources
Turni2007 – 20093Combined sources
Beta strandi2013 – 20153Combined sources
Helixi2023 – 203311Combined sources
Helixi2036 – 20438Combined sources
Turni2044 – 20485Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PFFX-ray4.00B/E/H1-545[»]
B/E/H1669-1940[»]
2UV8X-ray3.10G/H/I1-2051[»]
2VKZX-ray4.00G/H/I1-2051[»]
3HMJX-ray4.00G/H/I1-2051[»]
ProteinModelPortaliP07149.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07149.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1523 – 1648126MaoC-likeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 468468AcetyltransferaseAdd
BLAST
Regioni480 – 868389Enoyl reductaseAdd
BLAST
Regioni1144 – 1626483DehydrataseAdd
BLAST
Regioni1627 – 1845219Malonyl/palmitoyl transferaseAdd
BLAST

Sequence similaritiesi

Contains 1 MaoC-like domain.Curated

Phylogenomic databases

eggNOGiCOG0331.
HOGENOMiHOG000177963.
InParanoidiP07149.
KOiK00668.
OMAiKLQHVGM.
OrthoDBiEOG76QFRJ.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.40.366.10. 5 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013565. DUF1729.
IPR003965. Fatty_acid_synthase.
IPR016452. Fatty_acid_Synthase_bsu_fun.
IPR029069. HotDog_dom.
IPR002539. MaoC_dom.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF08354. DUF1729. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
[Graphical view]
PIRSFiPIRSF005562. FAS_yeast_beta. 1 hit.
PRINTSiPR01483. FASYNTHASE.
SUPFAMiSSF52151. SSF52151. 5 hits.
SSF54637. SSF54637. 2 hits.

Sequencei

Sequence statusi: Complete.

P07149-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDAYSTRPLT LSHGSLEHVL LVPTASFFIA SQLQEQFNKI LPEPTEGFAA
60 70 80 90 100
DDEPTTPAEL VGKFLGYVSS LVEPSKVGQF DQVLNLCLTE FENCYLEGND
110 120 130 140 150
IHALAAKLLQ ENDTTLVKTK ELIKNYITAR IMAKRPFDKK SNSALFRAVG
160 170 180 190 200
EGNAQLVAIF GGQGNTDDYF EELRDLYQTY HVLVGDLIKF SAETLSELIR
210 220 230 240 250
TTLDAEKVFT QGLNILEWLE NPSNTPDKDY LLSIPISCPL IGVIQLAHYV
260 270 280 290 300
VTAKLLGFTP GELRSYLKGA TGHSQGLVTA VAIAETDSWE SFFVSVRKAI
310 320 330 340 350
TVLFFIGVRC YEAYPNTSLP PSILEDSLEN NEGVPSPMLS ISNLTQEQVQ
360 370 380 390 400
DYVNKTNSHL PAGKQVEISL VNGAKNLVVS GPPQSLYGLN LTLRKAKAPS
410 420 430 440 450
GLDQSRIPFS ERKLKFSNRF LPVASPFHSH LLVPASDLIN KDLVKNNVSF
460 470 480 490 500
NAKDIQIPVY DTFDGSDLRV LSGSISERIV DCIIRLPVKW ETTTQFKATH
510 520 530 540 550
ILDFGPGGAS GLGVLTHRNK DGTGVRVIVA GTLDINPDDD YGFKQEIFDV
560 570 580 590 600
TSNGLKKNPN WLEEYHPKLI KNKSGKIFVE TKFSKLIGRP PLLVPGMTPC
610 620 630 640 650
TVSPDFVAAT TNAGYTIELA GGGYFSAAGM TAAIDSVVSQ IEKGSTFGIN
660 670 680 690 700
LIYVNPFMLQ WGIPLIKELR SKGYPIQFLT IGAGVPSLEV ASEYIETLGL
710 720 730 740 750
KYLGLKPGSI DAISQVINIA KAHPNFPIAL QWTGGRGGGH HSFEDAHTPM
760 770 780 790 800
LQMYSKIRRH PNIMLIFGSG FGSADDTYPY LTGEWSTKFD YPPMPFDGFL
810 820 830 840 850
FGSRVMIAKE VKTSPDAKKC IAACTGVPDD KWEQTYKKPT GGIVTVRSEM
860 870 880 890 900
GEPIHKIATR GVMLWKEFDE TIFNLPKNKL VPTLEAKRDY IISRLNADFQ
910 920 930 940 950
KPWFATVNGQ ARDLATMTYE EVAKRLVELM FIRSTNSWFD VTWRTFTGDF
960 970 980 990 1000
LRRVEERFTK SKTLSLIQSY SLLDKPDEAI EKVFNAYPAA REQFLNAQDI
1010 1020 1030 1040 1050
DHFLSMCQNP MQKPVPFVPV LDRRFEIFFK KDSLWQSEHL EAVVDQDVQR
1060 1070 1080 1090 1100
TCILHGPVAA QFTKVIDEPI KSIMDGIHDG HIKKLLHQYY GDDESKIPAV
1110 1120 1130 1140 1150
EYFGGESPVD VQSQVDSSSV SEDSAVFKAT SSTDEESWFK ALAGSEINWR
1160 1170 1180 1190 1200
HASFLCSFIT QDKMFVSNPI RKVFKPSQGM VVEISNGNTS SKTVVTLSEP
1210 1220 1230 1240 1250
VQGELKPTVI LKLLKENIIQ MEMIENRTMD GKPVSLPLLY NFNPDNGFAP
1260 1270 1280 1290 1300
ISEVMEDRNQ RIKEMYWKLW IDEPFNLDFD PRDVIKGKDF EITAKEVYDF
1310 1320 1330 1340 1350
THAVGNNCED FVSRPDRTML APMDFAIVVG WRAIIKAIFP NTVDGDLLKL
1360 1370 1380 1390 1400
VHLSNGYKMI PGAKPLQVGD VVSTTAVIES VVNQPTGKIV DVVGTLSRNG
1410 1420 1430 1440 1450
KPVMEVTSSF FYRGNYTDFE NTFQKTVEPV YQMHIKTSKD IAVLRSKEWF
1460 1470 1480 1490 1500
QLDDEDFDLL NKTLTFETET EVTFKNANIF SSVKCFGPIK VELPTKETVE
1510 1520 1530 1540 1550
IGIVDYEAGA SHGNPVVDFL KRNGSTLEQK VNLENPIPIA VLDSYTPSTN
1560 1570 1580 1590 1600
EPYARVSGDL NPIHVSRHFA SYANLPGTIT HGMFSSASVR ALIENWAADS
1610 1620 1630 1640 1650
VSSRVRGYTC QFVDMVLPNT ALKTSIQHVG MINGRKLIKF ETRNEDDVVV
1660 1670 1680 1690 1700
LTGEAEIEQP VTTFVFTGQG SQEQGMGMDL YKTSKAAQDV WNRADNHFKD
1710 1720 1730 1740 1750
TYGFSILDIV INNPVNLTIH FGGEKGKRIR ENYSAMIFET IVDGKLKTEK
1760 1770 1780 1790 1800
IFKEINEHST SYTFRSEKGL LSATQFTQPA LTLMEKAAFE DLKSKGLIPA
1810 1820 1830 1840 1850
DATFAGHSLG EYAALASLAD VMSIESLVEV VFYRGMTMQV AVPRDELGRS
1860 1870 1880 1890 1900
NYGMIAINPG RVAASFSQEA LQYVVERVGK RTGWLVEIVN YNVENQQYVA
1910 1920 1930 1940 1950
AGDLRALDTV TNVLNFIKLQ KIDIIELQKS LSLEEVEGHL FEIIDEASKK
1960 1970 1980 1990 2000
SAVKPRPLKL ERGFACIPLV GISVPFHSTY LMNGVKPFKS FLKKNIIKEN
2010 2020 2030 2040 2050
VKVARLAGKY IPNLTAKPFQ VTKEYFQDVY DLTGSEPIKE IIDNWEKYEQ

S
Length:2,051
Mass (Da):228,691
Last modified:February 1, 1994 - v2
Checksum:i43AA85A6071D8EAA
GO

Sequence cautioni

The sequence CAA27616.1 differs from that shown. Reason: Frameshift at positions 1845, 1948 and 2017. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911S → F in AAB59310. (PubMed:2034224)Curated
Sequence conflicti191 – 1911S → F in CAA27616. (PubMed:3528750)Curated
Sequence conflicti212 – 2121G → D in AAA34602. (PubMed:3031066)Curated
Sequence conflicti403 – 4031D → G in AAA34602. (PubMed:3031066)Curated
Sequence conflicti1039 – 10391H → Q in AAB59310. (PubMed:2034224)Curated
Sequence conflicti1039 – 10391H → Q in CAA27616. (PubMed:3528750)Curated
Sequence conflicti1149 – 11491W → R in AAA34602. (PubMed:3031066)Curated
Sequence conflicti1184 – 11841I → F in AAB59310. (PubMed:2034224)Curated
Sequence conflicti1184 – 11841I → F in CAA27616. (PubMed:3528750)Curated
Sequence conflicti1290 – 12923FEI → SET in AAA34602. (PubMed:3031066)Curated
Sequence conflicti1331 – 13333WRA → LRG in AAB59310. (PubMed:2034224)Curated
Sequence conflicti1331 – 13333WRA → LRG in CAA27616. (PubMed:3528750)Curated
Sequence conflicti1407 – 14115TSSFF → IFLFL in AAA34602. (PubMed:3031066)Curated
Sequence conflicti1559 – 15591D → H in AAB59310. (PubMed:2034224)Curated
Sequence conflicti1559 – 15591D → H in CAA27616. (PubMed:3528750)Curated
Sequence conflicti1576 – 15761P → L in AAA34602. (PubMed:3031066)Curated
Sequence conflicti1587 – 15871A → T in AAA34602. (PubMed:3031066)Curated
Sequence conflicti1631 – 16311M → T in AAA34602. (PubMed:3031066)Curated
Sequence conflicti1647 – 16471D → H in CAA27616. (PubMed:3528750)Curated
Sequence conflicti1661 – 16611V → G in AAB59310. (PubMed:2034224)Curated
Sequence conflicti1661 – 16611V → G in CAA27616. (PubMed:3528750)Curated
Sequence conflicti1876 – 18761E → K in AAA34602. (PubMed:3031066)Curated
Sequence conflicti1980 – 19801Y → T in AAA34602. (PubMed:3031066)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30162 Genomic DNA. Translation: AAB59310.1.
X74151 Genomic DNA. Translation: CAA52256.1.
Z28182 Genomic DNA. Translation: CAA82025.1.
X03977 Genomic DNA. Translation: CAA27616.1. Frameshift.
M31034 Genomic DNA. Translation: AAA34602.1.
X70069 Genomic DNA. Translation: CAA49673.1.
BK006944 Genomic DNA. Translation: DAA08985.1.
PIRiS34688.
RefSeqiNP_012739.1. NM_001179748.1.

Genome annotation databases

EnsemblFungiiYKL182W; YKL182W; YKL182W.
GeneIDi853653.
KEGGisce:YKL182W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30162 Genomic DNA. Translation: AAB59310.1 .
X74151 Genomic DNA. Translation: CAA52256.1 .
Z28182 Genomic DNA. Translation: CAA82025.1 .
X03977 Genomic DNA. Translation: CAA27616.1 . Frameshift.
M31034 Genomic DNA. Translation: AAA34602.1 .
X70069 Genomic DNA. Translation: CAA49673.1 .
BK006944 Genomic DNA. Translation: DAA08985.1 .
PIRi S34688.
RefSeqi NP_012739.1. NM_001179748.1.

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 B/E/H 1-545 [» ]
B/E/H 1669-1940 [» ]
2UV8 X-ray 3.10 G/H/I 1-2051 [» ]
2VKZ X-ray 4.00 G/H/I 1-2051 [» ]
3HMJ X-ray 4.00 G/H/I 1-2051 [» ]
ProteinModelPortali P07149.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33940. 67 interactions.
DIPi DIP-742N.
IntActi P07149. 77 interactions.
MINTi MINT-1325736.
STRINGi 4932.YKL182W.

Proteomic databases

MaxQBi P07149.
PaxDbi P07149.
PeptideAtlasi P07149.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKL182W ; YKL182W ; YKL182W .
GeneIDi 853653.
KEGGi sce:YKL182W.

Organism-specific databases

CYGDi YKL182w.
SGDi S000001665. FAS1.

Phylogenomic databases

eggNOGi COG0331.
HOGENOMi HOG000177963.
InParanoidi P07149.
KOi K00668.
OMAi KLQHVGM.
OrthoDBi EOG76QFRJ.

Enzyme and pathway databases

BioCyci MetaCyc:YKL182W-MONOMER.
YEAST:YKL182W-MONOMER.
SABIO-RK P07149.

Miscellaneous databases

EvolutionaryTracei P07149.
NextBioi 974569.

Gene expression databases

Genevestigatori P07149.

Family and domain databases

Gene3Di 3.10.129.10. 2 hits.
3.40.366.10. 5 hits.
InterProi IPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013565. DUF1729.
IPR003965. Fatty_acid_synthase.
IPR016452. Fatty_acid_Synthase_bsu_fun.
IPR029069. HotDog_dom.
IPR002539. MaoC_dom.
[Graphical view ]
Pfami PF00698. Acyl_transf_1. 1 hit.
PF08354. DUF1729. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
[Graphical view ]
PIRSFi PIRSF005562. FAS_yeast_beta. 1 hit.
PRINTSi PR01483. FASYNTHASE.
SUPFAMi SSF52151. SSF52151. 5 hits.
SSF54637. SSF54637. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The pentafunctional FAS1 genes of Saccharomyces cerevisiae and Yarrowia lipolytica are co-linear and considerably longer than previously estimated."
    Koettig H., Rottner G., Beck K.-F., Schweizer M., Schweizer E.
    Mol. Gen. Genet. 226:310-314(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI from Saccharomyces cerevisiae reveals 23 open reading frames including the FAS1 gene."
    Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J., Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.
    Yeast 9:1343-1348(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [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. "The pentafunctional FAS1 gene of yeast: its nucleotide sequence and order of the catalytic domains."
    Schweizer M., Roberts L.M., Hoeltke H.-J., Takabayashi K., Hoellerer E., Hoffmann B., Mueller G., Koettig H., Schweizer E.
    Mol. Gen. Genet. 203:479-486(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2025.
  6. "Complementation of mutations and nucleotide sequence of FAS1 gene encoding beta subunit of yeast fatty acid synthase."
    Chirala S.S., Kuziora M.A., Spector D.M., Wakil S.J.
    J. Biol. Chem. 262:4231-4240(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1980.
    Strain: ATCC 26787 / X2180-1B.
  7. "Phosphoribosylpyrophosphate synthetase (PRS): a new gene family in Saccharomyces cerevisiae."
    Carter A.T., Narbad A., Pearson B.M., Beck K.-F., Logghe M., Contreras R., Schweizer M.
    Yeast 10:1031-1044(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1947-2051.
    Strain: ATCC 26786 / X2180-1A.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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 THR-733 AND SER-1121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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].

Entry informationi

Entry nameiFAS1_YEAST
AccessioniPrimary (citable) accession number: P07149
Secondary accession number(s): D6VX19, Q05747
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1994
Last modified: November 26, 2014
This is version 155 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 91800 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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

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