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Q10289

- FAS2_SCHPO

UniProt

Q10289 - FAS2_SCHPO

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Protein

Fatty acid synthase subunit alpha

Gene

fas2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1262 – 12621For beta-ketoacyl synthase activityBy similarity
Metal bindingi1728 – 17281MagnesiumBy similarity
Metal bindingi1729 – 17291Magnesium; via carbonyl oxygenBy similarity
Metal bindingi1730 – 17301MagnesiumBy similarity
Binding sitei1754 – 17541Acetyl-CoABy similarity
Binding sitei1764 – 17641Acetyl-CoABy similarity
Metal bindingi1828 – 18281MagnesiumBy similarity
Metal bindingi1829 – 18291Magnesium; via carbonyl oxygenBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. fatty acid biosynthetic process Source: PomBase
  2. long-chain fatty acid biosynthetic process Source: PomBase
  3. macromolecule biosynthetic process Source: InterPro
  4. palmitic acid biosynthetic process Source: PomBase
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

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid synthase subunit alpha (EC:2.3.1.86)
Alternative name(s):
p190/210
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
Synonyms:lsd1
ORF Names:SPAC4A8.11c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC4A8.11c.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: PomBase
  2. fatty acid synthase complex Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18421842Fatty acid synthase subunit alphaPRO_0000180286Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei180 – 1801O-(pantetheine 4'-phosphoryl)serineBy similarity
Modified residuei604 – 6041Phosphoserine1 Publication
Modified residuei1412 – 14121Phosphoserine1 Publication

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

MaxQBiQ10289.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi280032. 6 interactions.
IntActiQ10289. 1 interaction.
MINTiMINT-4698444.
STRINGi4896.SPAC4A8.11c-1.

Structurei

3D structure databases

ProteinModelPortaliQ10289.
SMRiQ10289. Positions 1-94.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini134 – 295162Acyl carrierAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni? – 1842Beta-ketoacyl synthase
Regioni1728 – 17303Acetyl-CoA bindingBy similarity
Regioni1773 – 178917Acetyl-CoA bindingBy similarityAdd
BLAST
Regioni1797 – 18004Acetyl-CoA bindingBy similarity
Regioni1827 – 18293Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Contains 1 acyl carrier domain.Curated

Phylogenomic databases

HOGENOMiHOG000177974.
InParanoidiQ10289.
KOiK00667.
OMAiQVIMNAD.
OrthoDBiEOG76QFRJ.
PhylomeDBiQ10289.

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. 3 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.

Q10289 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRPEVEQELA HTLLLELLAY QFASPVRWIE TQDVILSPPV SAERIVEIGP
60 70 80 90 100
SPTLAGMAKR TLKLKYENMD AALSINREVL CYSKDAREIY YNFEDEVADE
110 120 130 140 150
PAEAPASTSS TPKVETAAAA APAATPAPAP AQTSAPAAAL PDEPPKALEV
160 170 180 190 200
LHTLVAQKLK KSIEEVSPQK SIKDLVGGKS TLQNEILGDL QKEFGATPEK
210 220 230 240 250
PEEVPLDELG AIMQSSFNGS LGKQSSSLIS RMISSKMPGG FNNSAVRGYL
260 270 280 290 300
GNRYGLGPGR LESVLLLALT MEPASRLGSE ADAKAWLDSV AQKYAARNGV
310 320 330 340 350
TLSSPTAEGG SSSGSAAVID EETFKKLTKN NTMLVTQQLE LFARYLNKDL
360 370 380 390 400
RAGQKAQVAE KVISDTLRAQ LDLWNEEHGE FYASGIAPIF SPLKARVYDS
410 420 430 440 450
DWNWARQDAL KMFFDIIFGR LKHVDTEIVA RCISVMNRSN PTLLEFMQYH
460 470 480 490 500
IDHCPAEKGE TYQLAKTLGQ QLIDNCKSVI DAPPVFKNVN HPTAPSTTID
510 520 530 540 550
ERGNLNYEEI PRPGVRKLTH YVTEMAKGGK LPTESKNKAK VQNDLARIYR
560 570 580 590 600
IIKSQNKMSR SSKLQIKQLY GQVLHALSLP LPSSNDEQTP VKETIPFLHI
610 620 630 640 650
RKKSVDGNWE FNKSLTGTYL DVLESGAKNG ITYQDKYALV TGAGAGSIGA
660 670 680 690 700
QIVEGLLAGG AKVVVTTSRF SRKVTEFYQS LYTRHGSRGS CLIVVPFNQG
710 720 730 740 750
SKTDVEALID YIYDEKKGLG WNLDYIVPFA AIPENGREID GIDSRSEFAH
760 770 780 790 800
RIMLTNILRL LGAVKSQKAS RGMDTRPAQV ILPLSPNHGT FGNDGLYSES
810 820 830 840 850
KLGLETLFNR WYSESWANYL TICGAVIGWT RGTGLMAPNN IVSQGIEKYG
860 870 880 890 900
VRTFSQSEMA FNILGLMSQK VVDLCQSEPI YANLNGGLEL LPDLKDLSTR
910 920 930 940 950
LRTELLETAE IRRAVAAETA FDHSITNGPD SEAVFQKTAI QPRANLKFNF
960 970 980 990 1000
PKLKPYEALS HLSDLRGMVD LEKVPVVTGF SEVGPWGNSR TRWDMECYGE
1010 1020 1030 1040 1050
FSLEGCVEIA WIMGLIKNFN GKGKDGKPYS GWVDTKTGEP VDDKDVKAKY
1060 1070 1080 1090 1100
EKYILEHCGI RIIEAELFHG YNPEKKELLQ EVVIDHDLEP FEASKEAAHE
1110 1120 1130 1140 1150
FKLRHGDQVE IFEIPDSTEW SVRFKRGTSM LIPKALRFDR FVAGQIPLGW
1160 1170 1180 1190 1200
DPKRYGIPDD IISQVDPTTL YVLVSTVEAL VASGITDPYE CYKYIHVSEL
1210 1220 1230 1240 1250
GNTVGSGIGG MSALRGMYKD RWTDKPVQKD ILQESFINTA NAWINMLLLS
1260 1270 1280 1290 1300
ASGPIKTPVG ACATAVESVD AAVDLITSGK ARICISGGYD DFSEEGSYEF
1310 1320 1330 1340 1350
ANMGATSNAA KETERGRTPQ EMSRPATSTR DGFMESQGAG VQIIMQAKLA
1360 1370 1380 1390 1400
IEMGVPIHGI VGYVSTAMDK QGRSVPAPGQ GILTGAREIA TKTPLPIVDL
1410 1420 1430 1440 1450
KFRSRQLQRR RSQIGEWAER EYLYLEEELD AMKVQNPDLD LEAYRIERIN
1460 1470 1480 1490 1500
VIKEEVVRQE KEALNTFGNE FWKRDPTIAP IRGALAVWGL TIDDLGVASF
1510 1520 1530 1540 1550
HGTSTKANEK NECDVIDSQL THLGRSKGNA VYGVFQKYLT GHSKGGAGAW
1560 1570 1580 1590 1600
MLNGALQILR SGFVPGNRNA DNIDEYLARF DRVMFPSEGI QTDGIKAASV
1610 1620 1630 1640 1650
TAFGFGQVGG QVIVIHPDYI YGVIDEATYN AYKAKTAARY KASYRYTHDA
1660 1670 1680 1690 1700
LVYNNLVRAK DSPPYTKEQE KAVYLNPLAR ASKSKAGTWT FPATLPAESD
1710 1720 1730 1740 1750
ISKTNETTRT LQSLTTSLTN SNENVGVDVE LVSAISIDNE TFIERNFTDT
1760 1770 1780 1790 1800
ERKYCFAAPN PQASFAGRWS AKEAVFKSLG ISGKGAAAPL KDIEIISSES
1810 1820 1830 1840
GAPEVVLHGE AAKAATTAGV KSVSVSISHD DNQSVSVALA HK
Length:1,842
Mass (Da):202,169
Last modified:August 14, 2001 - v2
Checksum:iE4019F2D133EE571
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071S → A in AAB39943. 1 PublicationCurated
Sequence conflicti422 – 4221K → R in BAA11913. (PubMed:8769419)Curated
Sequence conflicti1586 – 15861P → S in BAA13877. (PubMed:9501991)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41E → V in strain: H265.
Natural varianti600 – 6001I → N in strain: H518.
Natural varianti1276 – 12761I → T in strain: H201.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D83412 Genomic DNA. Translation: BAA11913.1.
AB013747 Genomic DNA. Translation: BAB62029.1.
AB013748 Genomic DNA. Translation: BAB62030.1.
AB013749 Genomic DNA. Translation: BAB62031.1.
AB013750 Genomic DNA. Translation: BAB62032.1.
CU329670 Genomic DNA. Translation: CAB11481.1.
U82216 Genomic DNA. Translation: AAB39943.1.
D89216 mRNA. Translation: BAA13877.1.
U97396 mRNA. Translation: AAB63888.1.
PIRiA54083.
T38781.
T43037.
T43409.
RefSeqiNP_593823.1. NM_001019252.2.

Genome annotation databases

EnsemblFungiiSPAC4A8.11c.1; SPAC4A8.11c.1:pep; SPAC4A8.11c.
GeneIDi2543618.
KEGGispo:SPAC4A8.11c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D83412 Genomic DNA. Translation: BAA11913.1 .
AB013747 Genomic DNA. Translation: BAB62029.1 .
AB013748 Genomic DNA. Translation: BAB62030.1 .
AB013749 Genomic DNA. Translation: BAB62031.1 .
AB013750 Genomic DNA. Translation: BAB62032.1 .
CU329670 Genomic DNA. Translation: CAB11481.1 .
U82216 Genomic DNA. Translation: AAB39943.1 .
D89216 mRNA. Translation: BAA13877.1 .
U97396 mRNA. Translation: AAB63888.1 .
PIRi A54083.
T38781.
T43037.
T43409.
RefSeqi NP_593823.1. NM_001019252.2.

3D structure databases

ProteinModelPortali Q10289.
SMRi Q10289. Positions 1-94.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 280032. 6 interactions.
IntActi Q10289. 1 interaction.
MINTi MINT-4698444.
STRINGi 4896.SPAC4A8.11c-1.

Proteomic databases

MaxQBi Q10289.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPAC4A8.11c.1 ; SPAC4A8.11c.1:pep ; SPAC4A8.11c .
GeneIDi 2543618.
KEGGi spo:SPAC4A8.11c.

Organism-specific databases

PomBasei SPAC4A8.11c.

Phylogenomic databases

HOGENOMi HOG000177974.
InParanoidi Q10289.
KOi K00667.
OMAi QVIMNAD.
OrthoDBi EOG76QFRJ.
PhylomeDBi Q10289.

Miscellaneous databases

NextBioi 20804624.

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. 3 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. "Aberrant mitosis in fission yeast mutants defective in fatty acid synthetase and acetyl CoA carboxylase."
    Saitoh S., Takahashi K., Nabeshima K., Yamashita Y., Nakaseko Y., Hirata A., Yanagida M.
    J. Cell Biol. 134:949-961(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Very long-chain fatty-acid-containing phospholipids accumulate in fatty acid synthase temperature-sensitive mutant strains of the fission yeast Schizosaccharomyces pombe fas2/lsd1."
    Yokoyama K., Saitoh S., Ishida M., Yamakawa Y., Nakamura K., Inoue K., Taguchi R., Tokumura A., Nishijima M., Yanagida M., Setaka M.
    Biochim. Biophys. Acta 1532:223-233(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 972 / ATCC 24843, H201, H265 and H518.
  3. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  4. Koken M.H.M., de Rooij J.
    Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-215.
  5. "Schizosaccharomyces pombe fatty acid synthase mediates DNA strand exchange in vitro."
    Kaeslin E., Heyer W.-D.
    J. Biol. Chem. 269:14103-14110(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20.
  6. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1466-1842.
    Strain: PR745.
  7. Jang Y.-J., Yoo H.-S.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1505-1564.
    Strain: 972 / ATCC 24843.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604 AND SER-1412, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiFAS2_SCHPO
AccessioniPrimary (citable) accession number: Q10289
Secondary accession number(s): O14163
, P78866, P78973, Q96WT6, Q96WT7, Q96WT8, Q9URI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: August 14, 2001
Last modified: October 29, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3