Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q10289

- FAS2_SCHPO

UniProt

Q10289 - FAS2_SCHPO

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (14 Aug 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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
    5. regulation of mitosis Source: PomBase

    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

    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.
    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.

    Q10289-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRPEVEQELA HTLLLELLAY QFASPVRWIE TQDVILSPPV SAERIVEIGP     50
    SPTLAGMAKR TLKLKYENMD AALSINREVL CYSKDAREIY YNFEDEVADE 100
    PAEAPASTSS TPKVETAAAA APAATPAPAP AQTSAPAAAL PDEPPKALEV 150
    LHTLVAQKLK KSIEEVSPQK SIKDLVGGKS TLQNEILGDL QKEFGATPEK 200
    PEEVPLDELG AIMQSSFNGS LGKQSSSLIS RMISSKMPGG FNNSAVRGYL 250
    GNRYGLGPGR LESVLLLALT MEPASRLGSE ADAKAWLDSV AQKYAARNGV 300
    TLSSPTAEGG SSSGSAAVID EETFKKLTKN NTMLVTQQLE LFARYLNKDL 350
    RAGQKAQVAE KVISDTLRAQ LDLWNEEHGE FYASGIAPIF SPLKARVYDS 400
    DWNWARQDAL KMFFDIIFGR LKHVDTEIVA RCISVMNRSN PTLLEFMQYH 450
    IDHCPAEKGE TYQLAKTLGQ QLIDNCKSVI DAPPVFKNVN HPTAPSTTID 500
    ERGNLNYEEI PRPGVRKLTH YVTEMAKGGK LPTESKNKAK VQNDLARIYR 550
    IIKSQNKMSR SSKLQIKQLY GQVLHALSLP LPSSNDEQTP VKETIPFLHI 600
    RKKSVDGNWE FNKSLTGTYL DVLESGAKNG ITYQDKYALV TGAGAGSIGA 650
    QIVEGLLAGG AKVVVTTSRF SRKVTEFYQS LYTRHGSRGS CLIVVPFNQG 700
    SKTDVEALID YIYDEKKGLG WNLDYIVPFA AIPENGREID GIDSRSEFAH 750
    RIMLTNILRL LGAVKSQKAS RGMDTRPAQV ILPLSPNHGT FGNDGLYSES 800
    KLGLETLFNR WYSESWANYL TICGAVIGWT RGTGLMAPNN IVSQGIEKYG 850
    VRTFSQSEMA FNILGLMSQK VVDLCQSEPI YANLNGGLEL LPDLKDLSTR 900
    LRTELLETAE IRRAVAAETA FDHSITNGPD SEAVFQKTAI QPRANLKFNF 950
    PKLKPYEALS HLSDLRGMVD LEKVPVVTGF SEVGPWGNSR TRWDMECYGE 1000
    FSLEGCVEIA WIMGLIKNFN GKGKDGKPYS GWVDTKTGEP VDDKDVKAKY 1050
    EKYILEHCGI RIIEAELFHG YNPEKKELLQ EVVIDHDLEP FEASKEAAHE 1100
    FKLRHGDQVE IFEIPDSTEW SVRFKRGTSM LIPKALRFDR FVAGQIPLGW 1150
    DPKRYGIPDD IISQVDPTTL YVLVSTVEAL VASGITDPYE CYKYIHVSEL 1200
    GNTVGSGIGG MSALRGMYKD RWTDKPVQKD ILQESFINTA NAWINMLLLS 1250
    ASGPIKTPVG ACATAVESVD AAVDLITSGK ARICISGGYD DFSEEGSYEF 1300
    ANMGATSNAA KETERGRTPQ EMSRPATSTR DGFMESQGAG VQIIMQAKLA 1350
    IEMGVPIHGI VGYVSTAMDK QGRSVPAPGQ GILTGAREIA TKTPLPIVDL 1400
    KFRSRQLQRR RSQIGEWAER EYLYLEEELD AMKVQNPDLD LEAYRIERIN 1450
    VIKEEVVRQE KEALNTFGNE FWKRDPTIAP IRGALAVWGL TIDDLGVASF 1500
    HGTSTKANEK NECDVIDSQL THLGRSKGNA VYGVFQKYLT GHSKGGAGAW 1550
    MLNGALQILR SGFVPGNRNA DNIDEYLARF DRVMFPSEGI QTDGIKAASV 1600
    TAFGFGQVGG QVIVIHPDYI YGVIDEATYN AYKAKTAARY KASYRYTHDA 1650
    LVYNNLVRAK DSPPYTKEQE KAVYLNPLAR ASKSKAGTWT FPATLPAESD 1700
    ISKTNETTRT LQSLTTSLTN SNENVGVDVE LVSAISIDNE TFIERNFTDT 1750
    ERKYCFAAPN PQASFAGRWS AKEAVFKSLG ISGKGAAAPL KDIEIISSES 1800
    GAPEVVLHGE AAKAATTAGV KSVSVSISHD DNQSVSVALA HK 1842
    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.
    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

    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 1, 2014
    This is version 130 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