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P15368

- FAS2_PENPA

UniProt

P15368 - FAS2_PENPA

Protein

Fatty acid synthase subunit alpha

Gene

FAS2

Organism
Penicillium patulum (Penicillium griseofulvum)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      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 alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase.

    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 sitei1275 – 12751For beta-ketoacyl synthase activityBy similarity
    Metal bindingi1743 – 17431MagnesiumBy similarity
    Metal bindingi1744 – 17441Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi1745 – 17451MagnesiumBy similarity
    Binding sitei1769 – 17691Acetyl-CoABy similarity
    Binding sitei1779 – 17791Acetyl-CoABy similarity
    Metal bindingi1843 – 18431MagnesiumBy similarity
    Metal bindingi1844 – 18441Magnesium; via carbonyl oxygenBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-KW
    2. macromolecule biosynthetic process Source: InterPro

    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)
    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
    OrganismiPenicillium patulum (Penicillium griseofulvum)
    Taxonomic identifieri5078 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18571857Fatty acid synthase subunit alphaPRO_0000180285Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei174 – 1741O-(pantetheine 4'-phosphoryl)serineBy similarity

    Keywords - PTMi

    Phosphopantetheine, Phosphoprotein

    Proteomic databases

    PRIDEiP15368.

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP15368.
    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? – 1857Beta-ketoacyl synthase
    Regioni648 – 845198Beta-ketoacyl reductaseAdd
    BLAST
    Regioni1743 – 17453Acetyl-CoA bindingBy similarity
    Regioni1788 – 180417Acetyl-CoA bindingBy similarityAdd
    BLAST
    Regioni1812 – 18154Acetyl-CoA bindingBy similarity
    Regioni1842 – 18443Acetyl-CoA bindingBy similarity

    Sequence similaritiesi

    Contains 1 acyl carrier domain.Curated

    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. 4 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.

    P15368-1 [UniParc]FASTAAdd to Basket

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    MRPEVEQELA HTLLVELLAY QFASPVRWIE TQDVILAEQR TERIVEIGPA     50
    DTLGGMARRT LASKYEAYDA ATSVQRQILC YNKDAKEIYY DVDPVEEEPE 100
    ATEPAPSATP AAPAAAPAAG APPPPPSAGP AASVEDIPVT AVDILRTLVA 150
    QKLKKSLADV PLSKAIKDLV GGKSTLQNEI LGDLGKEFGS TPEKPEDVPL 200
    DELGASMQAT FNGQLGKQSS SLIARMVSSK MPGGFNITSV RKYLETRWGL 250
    GSGRQDGVLL LALTMEPAAR LGSEVDAKAY LDDVTNKYAA SAGVNLSAPV 300
    AGGDSGGAGG GMVMDPAAID ALTKDQRALF KQQLEIIARY LKMDLRGGEK 350
    AHVISQETQK ALQAQLDLWQ AEHGDFYASG IEPSFDQLKA RVYDSSWNWA 400
    RQDALSMYYD IIFGRLQVVD REIVSQCIRI MNRSNPLLLD FMQYHIDNCP 450
    TERGETYQLA KELGQQLIEN CREVLEVAPV YKDVAVPTGP QTTIDARGNI 500
    SYKETPRTSA RKLEHYVKHM AEGGPISEYS NRTKVQNDLK SVYKLIRKQH 550
    RLSKSSQLQF DALYKDVVHA LGMNESQIIP QENGHSKKGG RSAAKRNTPT 600
    RPGKVETIPF LHLKKKTEHG WDYNKKLTGI YLNVTESAAK DGLSFQGKNV 650
    LMTGAGAGSI GAEVLQGLIS GGAQVIVTTS RFSREVTEYY QAMYARYGAR 700
    GSQLVVVPFN QGSKQDVEAL VEYIYDTKKG LGWDLDFVVP FAAIPENGRE 750
    IDSIDSKSEL AHRIMLTNLL RLLGSVKTQK QAHGFETRPA QVILPLSPNH 800
    GTFGNDGLYS ESKLALETLF NRWYSENWGH YLTICGAVIG WTRGTGLMSG 850
    NNMVAEGVEK LGVRTFSQQE MAFNLLGLMS PAIVNLCQLD PVFADLNGGL 900
    QFIPDLKGLM TKLRTDIMET SDVRQAVMKE TAIEHNIVNG EDSGVLYKKV 950
    IAEPRANIKF EFPNLPDWEK EVKPLNENLK GMVNLDKVVV VTGFSEVGPW 1000
    GNSRTRWEME SKGKFSLEGC VEMAWIMGLI KHHNGPLKGQ AYSGWVDAKT 1050
    GEPVDDKDVK PKYEKHILEH TGIRLIEPEL FKGYDPKKKQ LLQEIVIQED 1100
    LEPFEASKET AEEFKREHGD KVEIFEIPES GEYTVRLCKG ATMLIPKALQ 1150
    FDRLVAGQVP TGWDASRYGI PDDIISQVDP VTLFVLVCTA EAMLSAGVTD 1200
    PYEFYKYVHL SEVGNCIGSG IGGTHRLRGM YKDRFLDKPL QKDILQESFI 1250
    NTMSAWVNML LLSSTGPIKT PVGCCATAVE SVDIGYETIV EGKARVCFVG 1300
    GFDDFQEEGS YEFANMKATS NAEDEFAHGR TPQEMSRPTT TTRAGFMESQ 1350
    GCGMQLIMTA QLALDMGVPI HGIIALTTTA TDKIGRSVRS VPAPGQGVLT 1400
    TARENPGKFP SPLLDIKYRR RQLDLRKKQI NEWQEAELLY LQEEAEAMKA 1450
    QSDETFNEAE YMQERAQHIE REAIRQEKDA QYSLGNNFWK QDSRIAPLRG 1500
    AMATWGLTVD DIDVASFHGT STVANDKNES DVICQQMKHL GRSKGNAVMG 1550
    IFQKYLTGHP KGAAGAWMFN GCLQVLDSGL VPGNRNADNV DKVMEKFDYI 1600
    VYPSRSIQTD GVKAFSVTSF GFGQKGAQVI GIHPKYLYAT LDQAQYEAYK 1650
    TKVEARQKKA YRYFHNGLIN NSIFVAKSKA PYEDEQQSKV FLNPDYRVSV 1700
    DKKTSELKFS TTAPEAKQSE STRQTLESLA KANATENSKI GVDVEHIDSV 1750
    NIENETFVER NFTQSEQDYC RKAASPQSSF AGRWSAKEAV FKSLGVSSKG 1800
    AGAALKDIEI GVDANGAPVV NLHGAAAAAA KQAGVKQVSV SISHSDSQAV 1850
    AVAVSQF 1857
    Length:1,857
    Mass (Da):204,466
    Last modified:April 1, 1990 - v1
    Checksum:i34BAFD547D93FEE6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37461 Genomic DNA. Translation: AAA33695.1.
    PIRiS01787.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37461 Genomic DNA. Translation: AAA33695.1 .
    PIRi S01787.

    3D structure databases

    ProteinModelPortali P15368.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P15368.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. 4 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. "Isolation and sequence analysis of the fatty acid synthetase FAS2 gene from Penicillium patulum."
      Wiesner P., Beck J., Beck K.-F., Ripka S., Mueller G., Luecke S., Schweizer E.
      Eur. J. Biochem. 177:69-79(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiFAS2_PENPA
    AccessioniPrimary (citable) accession number: P15368
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 109 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

    Multifunctional enzyme

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3