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P78615

- FAS2_EMEND

UniProt

P78615 - FAS2_EMEND

Protein

Fatty acid synthase subunit alpha

Gene

fasA

Organism
Emericella nidulans (Aspergillus nidulans)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      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.1 Publication

    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 sitei1279 – 12791For beta-ketoacyl synthase activityBy similarity
    Metal bindingi1746 – 17461MagnesiumBy similarity
    Metal bindingi1747 – 17471Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi1748 – 17481MagnesiumBy similarity
    Binding sitei1772 – 17721Acetyl-CoABy similarity
    Binding sitei1782 – 17821Acetyl-CoABy similarity
    Metal bindingi1844 – 18441MagnesiumBy similarity
    Metal bindingi1845 – 18451Magnesium; 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:fasA
    OrganismiEmericella nidulans (Aspergillus nidulans)
    Taxonomic identifieri162425 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Pathology & Biotechi

    Disruption phenotypei

    Unable to grow on minimal medium unless supplemented with myristic acid.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18581858Fatty acid synthase subunit alphaPRO_0000419254Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei178 – 1781O-(pantetheine 4'-phosphoryl)serineBy similarity

    Keywords - PTMi

    Phosphopantetheine, Phosphoprotein

    Interactioni

    Subunit structurei

    Fatty acid synthase is composed of alpha and beta subunits.By similarity

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00001194.

    Structurei

    3D structure databases

    ProteinModelPortaliP78615.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini138 – 299162Acyl carrierAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni651 – 848198Beta-ketoacyl reductaseBy similarityAdd
    BLAST
    Regioni1123 – 1337215Beta-ketoacyl synthaseBy similarityAdd
    BLAST
    Regioni1746 – 17483Acetyl-CoA bindingBy similarity
    Regioni1791 – 180717Acetyl-CoA bindingBy similarityAdd
    BLAST
    Regioni1815 – 18184Acetyl-CoA bindingBy similarity
    Regioni1843 – 18453Acetyl-CoA bindingBy similarity

    Sequence similaritiesi

    Contains 1 acyl carrier domain.Curated

    Phylogenomic databases

    eggNOGiCOG4982.

    Family and domain databases

    Gene3Di3.40.366.10. 1 hit.
    3.40.47.10. 2 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.

    P78615-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRPEIEQELA HTLLVELLAY QFASPVRWIE TQDVILAEKR TERIVEIGPA     50
    DTLGGMARRT LASKYEAYDA ATSVQRQILC YNKDAKEIYY DVDPVEEETE 100
    SAPEAAAAPP TSAAPAAAVV AAPAPAASAP SAGPAAPVED APVTALDIVR 150
    TLVAQKLKKA LSDVPLNKAI KDLVGGKSTL QNEILGDLGK EFGSTPEKPE 200
    DTPLDELGAS MQATFNGQLG KQSSSLIARL VSSKMPGGFN ITAVRKYLET 250
    RWGLGPGRQD GVLLLALTME PASRIGSEPD AKVFLDDVAN KYAANSGISL 300
    NVPTASGDGG ASAGGMLMDP AAIDALTKDQ RALFKQQLEI IARYLKMDLR 350
    DGQKAFVASQ ETQKTLQAQL DLWQAEHGDF YASGIEPSFD PLKARVYDSS 400
    WNWARQDALS MYYDIIFGRL KVVDREIVSQ CIRIMNRSNP LLLEFMQYHI 450
    DNCPTERGET YQLAKELGEQ LIENCKEVLG VSPVYKDVAV PTGPQTTIDA 500
    RGNIEYQEVP RASARKLEHY VKQMAEGGPI SEYSNRAKVQ NDLRSVYKLI 550
    RRQHRLSKSS QLQFNALYKD VVRALSMNEN QIMPQENGST KKPGRNGSVR 600
    NGSPRAGKVE TIPFLHLKKK NEHGWDYSKK LTGIYLDVLE SAARSGLTFQ 650
    GKNVLMTGAG AGSIGAEVLQ GLISGGAKVI VTTSRYSREV TEYYQAMYAR 700
    YGARGSQLVV VPFNQGSKQD VEALVDYIYD TKKGLGWDLD FIVPFAAIPE 750
    NGREIDSIDS KSELAHRIML TNLLRLLGSV KAQKQANGFE TRPAQVILPL 800
    SPNHGTFGND GLYSESKLAL ETLFNRWYSE NWSNYLTICG AVIGWTRGTG 850
    LMSGNNMVAE GVEKLGVRTF SQQEMAFNLL GLMAPAIVNL CQLDPVWADL 900
    NGGLQFIPDL KDLMTRLRTE IMETSDVRRA VIKETAIENK VVNGEDSEVL 950
    YKKVIAEPRA NIKFQFPNLP TWDEDIKPLN ENLKGMVNLD KVVVVTGFSE 1000
    VGPWGNSRTR WEMEASGKFS LEGCVEMAWI MGLIRHHNGP IKGKTYSGWV 1050
    DSKTGEPVDD KDVKAKYEKY ILEHSGIRLI EPELFKGYDP KKKQLLQEIV 1100
    IEEDLEPFEA SKETAEEFKR EHGEKVEIFE VLESGEYTVR LKKGATLLIP 1150
    KALQFDRLVA GQVPTGWDAR RYGIPEDIIE QVDPVTLFVL VCTAEAMLSA 1200
    GVTDPYEFYK YVHLSEVGNC IGSGIGGTHA LRGMYKDRYL DKPLQKDILQ 1250
    ESFINTMSAW VNMLLLSSTG PIKTPVGACA TAVESVDIGY ETIVEGKARV 1300
    CFVGGFDDFQ EEGSYEFANM KATSNAEDEF AHGRTPQEMS RPTTTTRAGF 1350
    MESQGCGMQL IMSAQLALDM GVPIYGIIAL TTTATDKIGR SVPAPGQGVL 1400
    TTARENPGKF PSPLLDIKYR RRQLELRKRQ IREWQESELL YLQEEAEAIK 1450
    AQNPADFVVE EYLQERAQHI NREAIRQEKD AQFSLGNNFW KQDSRIAPLR 1500
    GALATWGLTV DEIGVASFHG TSTVANDKNE SDVICQQMKH LGRKKGNALL 1550
    GIFQKYLTGH PKGAAGAWMF NGCLQVLDSG LVPGNRNADN VDKVMEKFDY 1600
    IVYPSRSIQT DGIKAFSVTS FGFGQKGAQV IGIHPKYLYA TLDRAQFEAY 1650
    RAKVETRQKK AYRYFHNGLV NNSIFVAKNK APYEDELQSK VFLNPDYRVA 1700
    ADKKTSELKY PPKPPVATDA GSESTKAVIE SLAKAHATEN SKIGVDVESI 1750
    DSINISNETF IERILPASEQ QYCQNAPSPQ SSFAGRWSAK EAVFKSLGVC 1800
    SKGAGAPLKD IEIENDSNGA PTLHGVAAEA AKEAGVKHIS VSISHSDMQA 1850
    VAVAISQF 1858
    Length:1,858
    Mass (Da):204,732
    Last modified:May 1, 1997 - v1
    Checksum:i3D961E8716C9E24D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U75347 Genomic DNA. Translation: AAB41493.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U75347 Genomic DNA. Translation: AAB41493.1 .

    3D structure databases

    ProteinModelPortali P78615.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 162425.CADANIAP00001194.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG4982.

    Family and domain databases

    Gene3Di 3.40.366.10. 1 hit.
    3.40.47.10. 2 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. "Aspergillus has distinct fatty acid synthases for primary and secondary metabolism."
      Brown D.W., Adams T.H., Keller N.P.
      Proc. Natl. Acad. Sci. U.S.A. 93:14873-14877(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE.
      Strain: FGSC 89.

    Entry informationi

    Entry nameiFAS2_EMEND
    AccessioniPrimary (citable) accession number: P78615
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2012
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 86 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