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Q10289 (FAS2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fatty acid synthase subunit alpha

EC=2.3.1.86
Alternative name(s):
p190/210

Including the following 3 domains:

  1. Acyl carrier
  2. 3-oxoacyl-[acyl-carrier-protein] reductase
    EC=1.1.1.100
    Alternative name(s):
    Beta-ketoacyl reductase
  3. 3-oxoacyl-[acyl-carrier-protein] synthase
    EC=2.3.1.41
    Alternative name(s):
    Beta-ketoacyl synthase
Gene names
Name:fas2
Synonyms:lsd1
ORF Names:SPAC4A8.11c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length1842 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00101

Catalytic activity

Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+. HAMAP-Rule MF_00101

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. HAMAP-Rule MF_00101

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH. HAMAP-Rule MF_00101

Subunit structure

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

Sequence similarities

Belongs to the fungal fatty acid synthetase subunit alpha family.

Contains 1 acyl carrier domain.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   LigandMagnesium
Metal-binding
NAD
NADP
   Molecular functionOxidoreductase
Transferase
   PTMPhosphopantetheine
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from direct assay PubMed 9693066. Source: PomBase

long-chain fatty acid biosynthetic process

Inferred from mutant phenotype Ref.2. Source: PomBase

macromolecule biosynthetic process

Inferred from electronic annotation. Source: InterPro

palmitic acid biosynthetic process

Inferred from mutant phenotype Ref.2. Source: PomBase

regulation of mitosis

Inferred from mutant phenotype Ref.1. Source: PomBase

   Cellular_componentcytosol

Inferred from direct assay PubMed 16823372. Source: PomBase

fatty acid synthase complex

Inferred from direct assay PubMed 9693066. Source: PomBase

   Molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity

Inferred from sequence orthology. Source: PomBase

3-oxoacyl-[acyl-carrier-protein] synthase activity

Inferred from sequence orthology. Source: PomBase

fatty acid synthase activity

Inferred from direct assay PubMed 9693066. Source: PomBase

fatty-acyl-CoA synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

holo-[acyl-carrier-protein] synthase activity

Inferred from sequence orthology. Source: PomBase

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18421842Fatty acid synthase subunit alpha HAMAP-Rule MF_00101
PRO_0000180286

Regions

Domain134 – 295162Acyl carrier
Region1728 – 17303Acetyl-CoA binding By similarity
Region1773 – 178917Acetyl-CoA binding By similarity
Region1797 – 18004Acetyl-CoA binding By similarity
Region1827 – 18293Acetyl-CoA binding By similarity
Region? – 1842Beta-ketoacyl synthase HAMAP-Rule MF_00101

Sites

Active site12621For beta-ketoacyl synthase activity By similarity
Metal binding17281Magnesium By similarity
Metal binding17291Magnesium; via carbonyl oxygen By similarity
Metal binding17301Magnesium By similarity
Metal binding18281Magnesium By similarity
Metal binding18291Magnesium; via carbonyl oxygen By similarity
Binding site17541Acetyl-CoA By similarity
Binding site17641Acetyl-CoA By similarity

Amino acid modifications

Modified residue1801O-(pantetheine 4'-phosphoryl)serine By similarity
Modified residue6041Phosphoserine Ref.8
Modified residue14121Phosphoserine Ref.8

Natural variations

Natural variant41E → V in strain: H265.
Natural variant6001I → N in strain: H518.
Natural variant12761I → T in strain: H201.

Experimental info

Sequence conflict1071S → A in AAB39943. Ref.4
Sequence conflict4221K → R in BAA11913. Ref.1
Sequence conflict15861P → S in BAA13877. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q10289 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: E4019F2D133EE571

FASTA1,842202,169
        10         20         30         40         50         60 
MRPEVEQELA HTLLLELLAY QFASPVRWIE TQDVILSPPV SAERIVEIGP SPTLAGMAKR 

        70         80         90        100        110        120 
TLKLKYENMD AALSINREVL CYSKDAREIY YNFEDEVADE PAEAPASTSS TPKVETAAAA 

       130        140        150        160        170        180 
APAATPAPAP AQTSAPAAAL PDEPPKALEV LHTLVAQKLK KSIEEVSPQK SIKDLVGGKS 

       190        200        210        220        230        240 
TLQNEILGDL QKEFGATPEK PEEVPLDELG AIMQSSFNGS LGKQSSSLIS RMISSKMPGG 

       250        260        270        280        290        300 
FNNSAVRGYL GNRYGLGPGR LESVLLLALT MEPASRLGSE ADAKAWLDSV AQKYAARNGV 

       310        320        330        340        350        360 
TLSSPTAEGG SSSGSAAVID EETFKKLTKN NTMLVTQQLE LFARYLNKDL RAGQKAQVAE 

       370        380        390        400        410        420 
KVISDTLRAQ LDLWNEEHGE FYASGIAPIF SPLKARVYDS DWNWARQDAL KMFFDIIFGR 

       430        440        450        460        470        480 
LKHVDTEIVA RCISVMNRSN PTLLEFMQYH IDHCPAEKGE TYQLAKTLGQ QLIDNCKSVI 

       490        500        510        520        530        540 
DAPPVFKNVN HPTAPSTTID ERGNLNYEEI PRPGVRKLTH YVTEMAKGGK LPTESKNKAK 

       550        560        570        580        590        600 
VQNDLARIYR IIKSQNKMSR SSKLQIKQLY GQVLHALSLP LPSSNDEQTP VKETIPFLHI 

       610        620        630        640        650        660 
RKKSVDGNWE FNKSLTGTYL DVLESGAKNG ITYQDKYALV TGAGAGSIGA QIVEGLLAGG 

       670        680        690        700        710        720 
AKVVVTTSRF SRKVTEFYQS LYTRHGSRGS CLIVVPFNQG SKTDVEALID YIYDEKKGLG 

       730        740        750        760        770        780 
WNLDYIVPFA AIPENGREID GIDSRSEFAH RIMLTNILRL LGAVKSQKAS RGMDTRPAQV 

       790        800        810        820        830        840 
ILPLSPNHGT FGNDGLYSES KLGLETLFNR WYSESWANYL TICGAVIGWT RGTGLMAPNN 

       850        860        870        880        890        900 
IVSQGIEKYG VRTFSQSEMA FNILGLMSQK VVDLCQSEPI YANLNGGLEL LPDLKDLSTR 

       910        920        930        940        950        960 
LRTELLETAE IRRAVAAETA FDHSITNGPD SEAVFQKTAI QPRANLKFNF PKLKPYEALS 

       970        980        990       1000       1010       1020 
HLSDLRGMVD LEKVPVVTGF SEVGPWGNSR TRWDMECYGE FSLEGCVEIA WIMGLIKNFN 

      1030       1040       1050       1060       1070       1080 
GKGKDGKPYS GWVDTKTGEP VDDKDVKAKY EKYILEHCGI RIIEAELFHG YNPEKKELLQ 

      1090       1100       1110       1120       1130       1140 
EVVIDHDLEP FEASKEAAHE FKLRHGDQVE IFEIPDSTEW SVRFKRGTSM LIPKALRFDR 

      1150       1160       1170       1180       1190       1200 
FVAGQIPLGW DPKRYGIPDD IISQVDPTTL YVLVSTVEAL VASGITDPYE CYKYIHVSEL 

      1210       1220       1230       1240       1250       1260 
GNTVGSGIGG MSALRGMYKD RWTDKPVQKD ILQESFINTA NAWINMLLLS ASGPIKTPVG 

      1270       1280       1290       1300       1310       1320 
ACATAVESVD AAVDLITSGK ARICISGGYD DFSEEGSYEF ANMGATSNAA KETERGRTPQ 

      1330       1340       1350       1360       1370       1380 
EMSRPATSTR DGFMESQGAG VQIIMQAKLA IEMGVPIHGI VGYVSTAMDK QGRSVPAPGQ 

      1390       1400       1410       1420       1430       1440 
GILTGAREIA TKTPLPIVDL KFRSRQLQRR RSQIGEWAER EYLYLEEELD AMKVQNPDLD 

      1450       1460       1470       1480       1490       1500 
LEAYRIERIN VIKEEVVRQE KEALNTFGNE FWKRDPTIAP IRGALAVWGL TIDDLGVASF 

      1510       1520       1530       1540       1550       1560 
HGTSTKANEK NECDVIDSQL THLGRSKGNA VYGVFQKYLT GHSKGGAGAW MLNGALQILR 

      1570       1580       1590       1600       1610       1620 
SGFVPGNRNA DNIDEYLARF DRVMFPSEGI QTDGIKAASV TAFGFGQVGG QVIVIHPDYI 

      1630       1640       1650       1660       1670       1680 
YGVIDEATYN AYKAKTAARY KASYRYTHDA LVYNNLVRAK DSPPYTKEQE KAVYLNPLAR 

      1690       1700       1710       1720       1730       1740 
ASKSKAGTWT FPATLPAESD ISKTNETTRT LQSLTTSLTN SNENVGVDVE LVSAISIDNE 

      1750       1760       1770       1780       1790       1800 
TFIERNFTDT ERKYCFAAPN PQASFAGRWS AKEAVFKSLG ISGKGAAAPL KDIEIISSES 

      1810       1820       1830       1840 
GAPEVVLHGE AAKAATTAGV KSVSVSISHD DNQSVSVALA HK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604 AND SER-1412, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA54083.
T38781.
T43037.
T43409.
RefSeqNP_593823.1. NM_001019252.2.

3D structure databases

ProteinModelPortalQ10289.
SMRQ10289. Positions 1-94.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid280032. 6 interactions.
IntActQ10289. 1 interaction.
MINTMINT-4698444.
STRING4896.SPAC4A8.11c-1.

Proteomic databases

MaxQBQ10289.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC4A8.11c.1; SPAC4A8.11c.1:pep; SPAC4A8.11c.
GeneID2543618.
KEGGspo:SPAC4A8.11c.

Organism-specific databases

PomBaseSPAC4A8.11c.

Phylogenomic databases

HOGENOMHOG000177974.
KOK00667.
OMAQVIMNAD.
OrthoDBEOG76QFRJ.
PhylomeDBQ10289.

Family and domain databases

Gene3D3.40.366.10. 1 hit.
3.40.47.10. 3 hits.
3.40.50.720. 1 hit.
3.90.470.20. 1 hit.
HAMAPMF_00101. AcpS.
InterProIPR008278. 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]
PfamPF01648. ACPS. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
PIRSFPIRSF000454. FAS_yeast_alpha. 1 hit.
ProDomPD004282. PPantethiene-prot_Trfase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF52151. SSF52151. 1 hit.
SSF53901. SSF53901. 3 hits.
SSF56214. SSF56214. 1 hit.
TIGRFAMsTIGR00556. pantethn_trn. 1 hit.
PROSITEPS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20804624.

Entry information

Entry nameFAS2_SCHPO
AccessionPrimary (citable) accession number: Q10289
Secondary accession number(s): O14163 expand/collapse secondary AC list , P78866, P78973, Q96WT6, Q96WT7, Q96WT8, Q9URI5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: August 14, 2001
Last modified: May 14, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names