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Q5B7V0

- FAS2_EMENI

UniProt

Q5B7V0 - FAS2_EMENI

Protein

Fatty acid synthase subunit alpha

Gene

fasA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (26 Apr 2005)
      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 By similarity.By similarity

    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 sitei1197 – 11971For beta-ketoacyl synthase activityPROSITE-ProRule annotation
    Metal bindingi1650 – 16501MagnesiumBy similarity
    Metal bindingi1651 – 16511Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi1652 – 16521MagnesiumBy similarity
    Binding sitei1676 – 16761Acetyl-CoABy similarity
    Binding sitei1686 – 16861Acetyl-CoABy similarity
    Metal bindingi1754 – 17541MagnesiumBy similarity
    Metal bindingi1755 – 17551Magnesium; 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 acid synthase activity Source: ASPGD
    4. fatty-acyl-CoA synthase activity Source: UniProtKB-EC
    5. holo-[acyl-carrier-protein] synthase activity Source: InterPro
    6. magnesium ion binding Source: InterPro

    GO - Biological processi

    1. fatty acid biosynthetic process Source: ASPGD
    2. macromolecule biosynthetic process Source: InterPro
    3. secondary metabolite biosynthetic process Source: ASPGD

    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)
    Gene namesi
    Name:fasA
    ORF Names:AN3380
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome VI

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17711771Fatty acid synthase subunit alphaPRO_0000419253Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei181 – 1811O-(pantetheine 4'-phosphoryl)serineBy similarity

    Keywords - PTMi

    Phosphopantetheine, Phosphoprotein

    Expressioni

    Inductioni

    Induced by oleic acid and stearic acid, but not by linoleic acid.1 Publication

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00009660.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5B7V0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini141 – 302162Acyl carrierAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni575 – 771197Beta-ketoacyl reductaseBy similarityAdd
    BLAST
    Regioni1041 – 1255215Beta-ketoacyl synthaseBy similarityAdd
    BLAST
    Regioni1650 – 16523Acetyl-CoA bindingBy similarity
    Regioni1695 – 171117Acetyl-CoA bindingBy similarityAdd
    BLAST
    Regioni1719 – 17224Acetyl-CoA bindingBy similarity
    Regioni1753 – 17553Acetyl-CoA bindingBy similarity

    Sequence similaritiesi

    Contains 1 acyl carrier domain.Curated

    Phylogenomic databases

    eggNOGiCOG4982.
    HOGENOMiHOG000177974.
    OMAiCCVSEAF.
    OrthoDBiEOG7BGHV1.

    Family and domain databases

    Gene3Di3.40.47.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.470.20. 1 hit.
    InterProiIPR008278. 4-PPantetheinyl_Trfase_SF.
    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]
    SUPFAMiSSF53901. 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.

    Q5B7V0-1 [UniParc]FASTAAdd to Basket

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    MAISSTADLA PSRKARGSES NDRALKLFIE LLSVETQQQL FRGEPCIQRF     50
    VEIGPRTILS TMAKRSASIQ KDQRSSASCY SPEFLSYHDN QPEILYQYQN 100
    DQAIYPLSQP TQPQFEPTSP SHLTKRSPSP SKALPMSAIP SAELTLQAGH 150
    VILAMTAQKL RRRFDQVPVE KTIRDLSGGK STLQNELTGD LVAEFGRVPE 200
    GVEDQPLSSL AESFQPEFSG IPGKAMSTLI SRFISGKMPA GFNQSAIQEY 250
    LNSRWGLTKS HATIPLCFAP TMEPARRLAN ADEARAYLDD LVEKHAAFQG 300
    ISLVPSNQVA DGHESLAPVV MNVADVDEMN KRTKLYRAQF DSLASYLGVD 350
    YFASEKAMSE SESRIAELEE TIRLLNTELD EQFIKGIKPS FNIKQVRKYD 400
    SWWNWSREEL IRLLNEICQD SSSACPPDME NRLQNLLNKW DANCSEIVRA 450
    HLIGLQSRSS APMNKLQLIL EEIFTLGNQT LSIDPLFVHN LPPMGPQTII 500
    TDAGCLEYHE LPRQISHYPE AMAYGPPWPQ GHTSAPFIHI KTREDGQDWM 550
    YDSKATSIYH AMLDVGVTTG LTFTHKAVLV TGAGPSSIAA SVIQGLLSGG 600
    ARIIVTTSRS ISQSADFYQQ MYRQYGAKGS SLSLFPFNQA SKQDCEQLVQ 650
    HIYGPDSPTD GDLDYILPFA AIPQVGEPDA FGGRQELALR AMLVNILRLI 700
    GFVRQEKERL RIENRPTMIV LPMSCNEGTF GGDGLYSEAK IGLKALFNRF 750
    YSENWSKYLT ICGAVIGWTR GTAIMQTSNA VAEEVEKLGV ITFTQAEMAF 800
    NILALMTPAL TALAEDTPIY ADLTGGLGSM WNIKQEISAA RKRISERQIL 850
    QIAIAEEDAR EQAMICSAST DVESGLPTTR HARLGLQFPP LPDVNEGYPN 900
    IEGMIDLTRI PVIVGYSELG PWGNARTRWE IEHRGDFSLE GYIEMAWIMG 950
    LIKHVDGHAK GRPYVGWVDA DTETPIQDYE VPHKYHKHIM AHAGLRLIKP 1000
    TKLDSYDPSR KELLHEVAVE EDLAPFETSK STAEAFKLRH GDCVTLLPIA 1050
    DSDNCRVYIK KGAVLMIPKA VPFDQVVAGR IPEGWDPARY GIPEEIVQQV 1100
    DVTTLYALCC VSEAFLSAGI KDPYEIYQYI HVSELANCLG SGGGPMKVIQ 1150
    NMYRDRFLDR QIRGDIILEH FVNTMGAWVN MLLLSATGPL KTPVGACATA 1200
    IESLDIGCEA IQNGRCKVAV VGGCDDYGEE LAFEFANIKA TANSTEELSK 1250
    GRTPADISRP TASSRSGFAE SAGCGVQILM SAALAIEMGL PIYGVVAYTH 1300
    MASDQIGRSI PAPGKGILTA ARENGQAKES PLLDLNFRRA VFDAEVALIN 1350
    KSHPKQATTL KPDHSETSNA ASLRIRDAQN RWANNIRLSD PSISPIRASL 1400
    ATWGLTVDDI KVVSMHGTST KANEVNEGNV INTQMRHLGR QMGNPLLAVC 1450
    QKSLTGHPKA GAGAWQLNGC LQMMQENIVP GNRNADNIDK QLREFEHIVY 1500
    PMESLRVPEI KATLLTSFGF GQKGAINIMV SPRYLFASLS NSDYEDYRSR 1550
    TTKRQRSATP TFVSRIMKNN LVQVKTRPPW NDPEAMQNFF LDPNSRVVDG 1600
    QITRAPRTAY KHQDISVPQS AAVSVNEALH AMLATTDHSS PAASASVGVD 1650
    VEEISSINVD NPIFISRNFT LLERDYCLSA PDPRASFAGR WVAKEAAFKS 1700
    LQTTSTGAGT AMDQIEILEV GGIPKVVRLT SQLHGHAHEV AFAQGITNIQ 1750
    ITISHCNNTA IAVALALRKN D 1771
    Length:1,771
    Mass (Da):194,939
    Last modified:April 26, 2005 - v1
    Checksum:iAFD90A5A2137EED1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACD01000055 Genomic DNA. Translation: EAA63348.1.
    BN001306 Genomic DNA. Translation: CBF82822.1.
    RefSeqiXP_660984.1. XM_655892.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00009660; CADANIAP00009660; CADANIAG00009660.
    GeneIDi2874362.
    KEGGiani:AN3380.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACD01000055 Genomic DNA. Translation: EAA63348.1 .
    BN001306 Genomic DNA. Translation: CBF82822.1 .
    RefSeqi XP_660984.1. XM_655892.1.

    3D structure databases

    ProteinModelPortali Q5B7V0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 162425.CADANIAP00009660.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00009660 ; CADANIAP00009660 ; CADANIAG00009660 .
    GeneIDi 2874362.
    KEGGi ani:AN3380.2.

    Phylogenomic databases

    eggNOGi COG4982.
    HOGENOMi HOG000177974.
    OMAi CCVSEAF.
    OrthoDBi EOG7BGHV1.

    Family and domain databases

    Gene3Di 3.40.47.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.470.20. 1 hit.
    InterProi IPR008278. 4-PPantetheinyl_Trfase_SF.
    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 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    2. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
      Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
      , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
      Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    3. "Two Delta9-stearic acid desaturases are required for Aspergillus nidulans growth and development."
      Wilson R.A., Chang P.K., Dobrzyn A., Ntambi J.M., Zarnowski R., Keller N.P.
      Fungal Genet. Biol. 41:501-509(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY FATTY ACIDS.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

    Entry informationi

    Entry nameiFAS2_EMENI
    AccessioniPrimary (citable) accession number: Q5B7V0
    Secondary accession number(s): C8VHP2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2012
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 69 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3