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Q9UUG0

- FAS1_SCHPO

UniProt

Q9UUG0 - FAS1_SCHPO

Protein

Fatty acid synthase subunit beta

Gene

fas1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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 sitei270 – 2701For acetyltransferase activityBy similarity
    Active sitei1361 – 13611For dehydratase activitySequence Analysis
    Active sitei1828 – 18281For malonyltransferase activityBy similarity

    GO - Molecular functioni

    1. [acyl-carrier-protein] S-acetyltransferase activity Source: PomBase
    2. [acyl-carrier-protein] S-malonyltransferase activity Source: PomBase
    3. 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
    4. 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity Source: PomBase
    5. enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: PomBase
    6. fatty acid synthase activity Source: PomBase
    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

    GO - Biological processi

    1. fatty acid biosynthetic process Source: PomBase

    Keywords - Molecular functioni

    Hydrolase, Lyase, Oxidoreductase, Transferase

    Keywords - Biological processi

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

    Keywords - Ligandi

    NAD, NADP

    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
    ORF Names:SPAC926.09c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC926.09c.

    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 – 20732073Fatty acid synthase subunit betaPRO_0000180281Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1122 – 11221Phosphoserine1 Publication
    Modified residuei2073 – 20731Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UUG0.
    PaxDbiQ9UUG0.

    Interactioni

    Subunit structurei

    [Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta).1 Publication

    Protein-protein interaction databases

    BioGridi279916. 17 interactions.
    MINTiMINT-4713190.
    STRINGi4896.SPAC926.09c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UUG0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1558 – 1667110MaoC-likeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 459459AcetyltransferaseAdd
    BLAST
    Regioni470 – 858389Enoyl reductaseAdd
    BLAST
    Regioni1155 – 1644490DehydrataseAdd
    BLAST
    Regioni1645 – 2073429Malonyl/palmitoyl transferaseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 MaoC-like domain.Curated

    Phylogenomic databases

    eggNOGiCOG0331.
    HOGENOMiHOG000177963.
    KOiK00668.
    OMAiKLQHVGM.
    OrthoDBiEOG76QFRJ.
    PhylomeDBiQ9UUG0.

    Family and domain databases

    Gene3Di3.10.129.10. 2 hits.
    3.20.20.70. 1 hit.
    3.40.366.10. 5 hits.
    InterProiIPR001227. Ac_transferase_dom.
    IPR014043. Acyl_transferase.
    IPR016035. Acyl_Trfase/lysoPLipase.
    IPR013785. Aldolase_TIM.
    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.

    Q9UUG0-1 [UniParc]FASTAAdd to Basket

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    MVEAEQVHQS LRSLVLSYAH FSPSILIPAS QYLLAAQLRD EFLSLHPAPS     50
    AESVEKEGAE LEFEHELHLL AGFLGLIAAK EEETPGQYTQ LLRIITLEFE 100
    RTFLAGNEVH AVVHSLGLNI PAQKDVVRFY YHSCALIGQT TKFHGSALLD 150
    ESSVKLAAIF GGQGYEDYFD ELIELYEVYA PFAAELIQVL SKHLFTLSQN 200
    EQASKVYSKG LNVLDWLAGE RPERDYLVSA PVSLPLVGLT QLVHFSVTAQ 250
    ILGLNPGELA SRFSAASGHS QGIVVAAAVS ASTDSASFME NAKVALTTLF 300
    WIGVRSQQTF PTTTLPPSVV ADSLASSEGN PTPMLAVRDL PIETLNKHIE 350
    TTNTHLPEDR KVSLSLVNGP RSFVVSGPAR SLYGLNLSLR KEKADGQNQS 400
    RIPHSKRKLR FINRFLSISV PFHSPYLAPV RSLLEKDLQG LQFSALKVPV 450
    YSTDDAGDLR FEQPSKLLLA LAVMITEKVV HWEEACGFPD VTHIIDFGPG 500
    GISGVGSLTR ANKDGQGVRV IVADSFESLD MGAKFEIFDR DAKSIEFAPN 550
    WVKLYSPKLV KNKLGRVYVD TRLSRMLGLP PLWVAGMTPT SVPWQFCSAI 600
    AKAGFTYELA GGGYFDPKMM REAIHKLSLN IPPGAGICVN VIYINPRTYA 650
    WQIPLIRDMV AEGYPIRGVT IAAGIPSLEV ANELISTLGV QYLCLKPGSV 700
    EAVNAVISIA KANPTFPIVL QWTGGRAGGH HSFEDFHSPI LLTYSAIRRC 750
    DNIVLIAGSG FGGADDTEPY LTGEWSAAFK LPPMPFDGIL FGSRLMVAKE 800
    AHTSLAAKEA IVAAKGVDDS EWEKTYDGPT GGIVTVLSEL GEPIHKLATR 850
    GIMFWKELDD TIFSLPRPKR LPALLAKKQY IIKRLNDDFQ KVYFPAHIVE 900
    QVSPEKFKFE AVDSVEDMTY AELLYRAIDL MYVTKEKRWI DVTLRTFTGK 950
    LMRRIEERFT QDVGKTTLIE NFEDLNDPYP VAARFLDAYP EASTQDLNTQ 1000
    DAQFFYSLCS NPFQKPVPFI PAIDDTFEFY FKKDSLWQSE DLAAVVGEDV 1050
    GRVAILQGPM AAKHSTKVNE PAKELLDGIN ETHIQHFIKK FYAGDEKKIP 1100
    IVEYFGGVPP VNVSHKSLES VSVTEEAGSK VYKLPEIGSN SALPSKKLWF 1150
    ELLAGPEYTW FRAIFTTQRV AKGWKLEHNP VRRIFAPRYG QRAVVKGKDN 1200
    DTVVELYETQ SGNYVLAARL SYDGETIVVS MFENRNALKK EVHLDFLFKY 1250
    EPSAGYSPVS EILDGRNDRI KHFYWALWFG EEPYPENASI TDTFTGPEVT 1300
    VTGNMIEDFC RTVGNHNEAY TKRAIRKRMA PMDFAIVVGW QAITKAIFPK 1350
    AIDGDLLRLV HLSNSFRMVG SHSLMEGDKV TTSASIIAIL NNDSGKTVTV 1400
    KGTVYRDGKE VIEVISRFLY RGTFTDFENT FEHTQETPMQ LTLATPKDVA 1450
    VLQSKSWFQL LDPSQDLSGS ILTFRLNSYV RFKDQKVKSS VETKGIVLSE 1500
    LPSKAIIQVA SVDFQSVDCH GNPVIEFLKR NGKPIEQPVE FENGGYSVIQ 1550
    VMDEGYSPVF VTPPTNSPYA EVSGDYNPIH VSPTFAAFVE LPGTHGITHG 1600
    MYTSAAARRF VETYAAQNVP ERVKHYEVTF VNMVLPNTEL ITKLSHTGMI 1650
    NGRKIIKVEV LNQETSEPVL VGTAEVEQPV SAYVFTGQGS QEQGMGMDLY 1700
    ASSPVARKIW DSADKHFLTN YGFSIIDIVK HNPHSITIHF GGSKGKKIRD 1750
    NYMAMAYEKL MEDGTSKVVP VFETITKDST SFSFTHPSGL LSATQFTQPA 1800
    LTLMEKSAFE DMRSKGLVQN DCAFAGHSLG EYSALSAMGD VLSIEALVDL 1850
    VFLRGLTMQN AVHRDELGRS DYGMVAANPS RVSASFTDAA LRFIVDHIGQ 1900
    QTNLLLEIVN YNVENQQYVV SGNLLSLSTL GHVLNFLKVQ KIDFEKLKET 1950
    LTIEQLKEQL TDIVEACHAK TLEQQKKTGR IELERGYATI PLKIDVPFHS 2000
    SFLRGGVRMF REYLVKKIFP HQINVAKLRG KYIPNLTAKP FEISKEYFQN 2050
    VYDLTGSQRI KKILQNWDEY ESS 2073
    Length:2,073
    Mass (Da):230,561
    Last modified:May 1, 2000 - v1
    Checksum:iD928270838E7C7C4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti222 – 2221P → R in BAA36384. (PubMed:9693066)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB010274 Genomic DNA. Translation: BAA36384.1.
    CU329670 Genomic DNA. Translation: CAB54157.1.
    D89148 mRNA. Translation: BAA13810.1.
    PIRiT39207.
    T42424.
    T43311.
    RefSeqiNP_594370.1. NM_001019791.2.

    Genome annotation databases

    EnsemblFungiiSPAC926.09c.1; SPAC926.09c.1:pep; SPAC926.09c.
    GeneIDi2543497.
    KEGGispo:SPAC926.09c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB010274 Genomic DNA. Translation: BAA36384.1 .
    CU329670 Genomic DNA. Translation: CAB54157.1 .
    D89148 mRNA. Translation: BAA13810.1 .
    PIRi T39207.
    T42424.
    T43311.
    RefSeqi NP_594370.1. NM_001019791.2.

    3D structure databases

    ProteinModelPortali Q9UUG0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 279916. 17 interactions.
    MINTi MINT-4713190.
    STRINGi 4896.SPAC926.09c-1.

    Proteomic databases

    MaxQBi Q9UUG0.
    PaxDbi Q9UUG0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC926.09c.1 ; SPAC926.09c.1:pep ; SPAC926.09c .
    GeneIDi 2543497.
    KEGGi spo:SPAC926.09c.

    Organism-specific databases

    PomBasei SPAC926.09c.

    Phylogenomic databases

    eggNOGi COG0331.
    HOGENOMi HOG000177963.
    KOi K00668.
    OMAi KLQHVGM.
    OrthoDBi EOG76QFRJ.
    PhylomeDBi Q9UUG0.

    Miscellaneous databases

    NextBioi 20804508.

    Family and domain databases

    Gene3Di 3.10.129.10. 2 hits.
    3.20.20.70. 1 hit.
    3.40.366.10. 5 hits.
    InterProi IPR001227. Ac_transferase_dom.
    IPR014043. Acyl_transferase.
    IPR016035. Acyl_Trfase/lysoPLipase.
    IPR013785. Aldolase_TIM.
    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

    1. "Cloning of the fatty acid synthetase beta subunit from fission yeast, coexpression with the alpha subunit, and purification of the intact multifunctional enzyme complex."
      Niwa H., Katayama E., Yanagida M., Morikawa K.
      Protein Expr. Purif. 13:403-413(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT.
    2. "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.
    3. "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 1725-2073.
      Strain: PR745.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1122 AND SER-2073, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiFAS1_SCHPO
    AccessioniPrimary (citable) accession number: Q9UUG0
    Secondary accession number(s): P78799
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 14, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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