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G8BAW7

- FAS2_CANPC

UniProt

G8BAW7 - FAS2_CANPC

Protein

Fatty acid synthase subunit alpha

Gene

FAS2

Organism
Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 17 (01 Oct 2014)
      Sequence version 1 (25 Jan 2012)
      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 sitei1303 – 13031For beta-ketoacyl synthase activityBy similarity
    Metal bindingi1770 – 17701MagnesiumBy similarity
    Metal bindingi1771 – 17711Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi1772 – 17721MagnesiumBy similarity
    Binding sitei1796 – 17961Acetyl-CoABy similarity
    Binding sitei1806 – 18061Acetyl-CoABy similarity
    Metal bindingi1870 – 18701MagnesiumBy similarity
    Metal bindingi1871 – 18711Magnesium; 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: CGD
    2. macromolecule biosynthetic process Source: InterPro
    3. pathogenesis Source: CGD
    4. single-species biofilm formation on inanimate substrate Source: CGD

    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
    ORF Names:CPAR2_807400
    OrganismiCandida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
    Taxonomic identifieri578454 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
    ProteomesiUP000005221: Chromosome 8

    Pathology & Biotechi

    Disruption phenotypei

    Essential for growth in fatty acid-free medium, but dispensable in medium with fatty acids. The growth in the presence of fatty acid depends on the type. Able to grow in a concentration-dependent manner in the presence of myristic acid, palmitic acid, or Tween 80 as the fatty acid sources, but unable to grow in the presence of unsaturated fatty like acids stearic acid or oleic acid. Intracellular survival in the murine macrophage line J774.16 is significantly reduced compared to wild type or heterozygous fungal cells. Required for systemic infection in mice. Impaired in its capacity to form biofilms on polysterene and silicone surfaces.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18841884Fatty acid synthase subunit alphaPRO_0000419251Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei182 – 1821O-(pantetheine 4'-phosphoryl)serineBy similarity

    Keywords - PTMi

    Phosphopantetheine, Phosphoprotein

    Expressioni

    Inductioni

    Expression significantly elevated by the presence of glucose. Down-regulated by unsaturated fatty acids oleic acid and Tween 80. Up-regulated during in vitro biofilm formation and hypoxic conditions.2 Publications

    Interactioni

    Subunit structurei

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

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini142 – 303162Acyl carrierAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni677 – 873197Beta-ketoacyl reductaseBy similarityAdd
    BLAST
    Regioni1147 – 1361215Beta-ketoacyl synthaseBy similarityAdd
    BLAST
    Regioni1770 – 17723Acetyl-CoA bindingBy similarity
    Regioni1815 – 183117Acetyl-CoA bindingBy similarityAdd
    BLAST
    Regioni1839 – 18424Acetyl-CoA bindingBy similarity
    Regioni1869 – 18713Acetyl-CoA bindingBy similarity

    Sequence similaritiesi

    Contains 1 acyl carrier domain.Curated

    Phylogenomic databases

    OrthoDBiEOG76QFRJ.

    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.

    G8BAW7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPEIEQELS HTLLTELLAY QFASPVRWIE TQDVFLKQHN TERVIEIGPS     50
    PTLAGMASRT IKAKYQSYDA ALSLQRQVLC YSKDAKEIYY TPDPAEPPAA 100
    EEPKAETGKE SAPAASAAAA AATQPAAAVA PPPQSAGPVE SIPDEPVKAS 150
    LLIHVLVAQK LKKPLDAVPM SKAIKDLVNG KSTVQNEILG DLGKEFGSTP 200
    EKPEETPLEE LAEQFQDTFS GSLGKTSTSL IGRLMSSKMP GGFSITNARK 250
    YLESRFGLGP GRQDSVLLTA LCNEPASRLG SEGDAKSFLD TMAQKYASHA 300
    GISLSSPSAG GASSGAGAAV VDSAALDALI AENKKLARQQ LETLARYLQV 350
    DLTKGEKAFI KEKEATTVLQ QELDLWEAEH GEFYAKGIKP VFSPLKSRTY 400
    DSYWNWARQD LLSMWFDILF GKLTSVDRET INQCIQIMNR ANPTLIKFMQ 450
    YHVELCPTYR GETYKLGKRL GEQLIENCKQ ILGQSPVYKD VSRITGPKTT 500
    VSAKGDIVYE EANKESVRKF EQYVFEMAQG GSMTKMKQSS IQEDLARVYK 550
    AISKQASRDS KLELQKVYDQ LLKVVEGSTE IETEQTTQDA LAIPTGSNTP 600
    TEEDELSTAS DDDEIASLPD KTSIAQPVSS TIPNKTIPFL HIQSKSESGN 650
    WEYDRKLSSI YLDGLESAAI NGLTFKDKYV LVTGAGAGSI GAEILQGLIS 700
    GGAKVIVTTS RYSKKVTEYY QNMYARYGAA GSTLIVVPFN QGSKQDVDAL 750
    VEYIYNDQKK GGLGWDLDVI IPFAAIPENG NGIDNIDSKS EFAHRIMLTN 800
    LLRLLGAVKA RKTTDTRPAQ CILPLSPNHG TFGFDGLYSE SKISLETLFN 850
    RWYSEDWGTK LTICGAIIGW TRGTGLMSAN NIIAEGIEKL GVRTFSQKEM 900
    AFNILGLLTP EIVNLCQEEP VMADLNGGLQ FIDNLKEFTS KLRNDLTETA 950
    DIRRAVSIES AIEQKVVNGD NVDSNYNKVT VRPRANMKFD FPTLKSYDEI 1000
    KQIAPDLEGM LDLENVVVVT GFAEVGPWGN ARTRWEMESK GEFSLEGAIE 1050
    MAWIMGMIKY HNGNLKGKPY SGWIDAKTQT PVDDKDIKAK YEEEILEHSG 1100
    IRLIEPELFN GYDPKKKQMI QEVVIQHDLE PFECSKETAE QYKHEHGDKC 1150
    EISEIEESGE YSVRILKGAT LFIPKALRFD RLVAGQIPTG WDARTYGIPE 1200
    DTINQVDPIT LYVLVATVEA LLSAGITDPY EFYKYVHVSE VGNCSGSGMG 1250
    GVSALRGMFK DRYADKPVQN DILQESFINT MSAWVNMLLL SASGPIKTPV 1300
    GACATAVESV DIGIETILSG KAKVVMVGGY DDFQEEGSYE FANMNATSSA 1350
    IDEFKHGRTP KEMSRPTTTT RNGFMEAQGS GIQVIMSADL ALKMGVPIHA 1400
    VLAMSATATD KIGRSVPAPG KGILTTAREH HGNLKYPSPL LNVKYRKRQL 1450
    SKRLDQIKSW ESSELNYLQE EAHLAKEEFG EEFSEAEFLR ERTEEIYRES 1500
    KRQVADAKKQ WGNAFYKSDP RIAPLRGALA TFNLTIDDIG VASFHGTSTV 1550
    ANDKNESATI DSMMKHLGRS EGNPVFGVFQ KYLTGHPKGA AGAWMLNGAI 1600
    QILESGIVPG NRNADNVDKV LEQYEYVLYP SRSIQTDGIK AVSVTSFGFG 1650
    QKGAQAVVVH PDYLYAVLDR STYEDYAKRV TARNKKTYRY MHNAITRNTM 1700
    FVAKDKAPYS DELTMDVYLD PLARVSKTKN EFVFTKKSVQ SDKSYVSNIA 1750
    NSTAKALSSL NKSSKGVGVD VELLSELNID NETFLERNFT PEEIKYCQNS 1800
    ANPQASFTGT WSAKEATFKA LGVSSQGGGA SLKEIEIVRD GNGAPQVVLN 1850
    DNAKAAAKAA GVKNVNVSIS HDDFQATAVA LSEF 1884
    Length:1,884
    Mass (Da):206,941
    Last modified:January 25, 2012 - v1
    Checksum:i33DCED9F65C58282
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    HE605205 Genomic DNA. Translation: CCE42191.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    HE605205 Genomic DNA. Translation: CCE42191.1 .

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    OrthoDBi EOG76QFRJ.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CDC 317 / ATCC MYA-4646.
    2. "Using RNA-seq to determine the transcriptional landscape and the hypoxic response of the pathogenic yeast Candida parapsilosis."
      Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J., Berriman M., Butler G.
      BMC Genomics 12:628-628(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: CDC 317 / ATCC MYA-4646.
    3. "Correlation between biofilm formation and the hypoxic response in Candida parapsilosis."
      Rossignol T., Ding C., Guida A., d'Enfert C., Higgins D.G., Butler G.
      Eukaryot. Cell 8:550-559(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY HYPOXIA AND BIOFILM FORMATION.
    4. "Fatty acid synthase impacts the pathobiology of Candida parapsilosis in vitro and during mammalian infection."
      Nguyen L.N., Trofa D., Nosanchuk J.D.
      PLoS ONE 4:E8421-E8421(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION BY CARBON SOURCES, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiFAS2_CANPC
    AccessioniPrimary (citable) accession number: G8BAW7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2012
    Last sequence update: January 25, 2012
    Last modified: October 1, 2014
    This is version 17 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    It can potentially be a fungicidal target. Inhibition of FAS2 by cerulenin impeds the growth of wild-type and heterozygous strains (PubMed:20027295).1 Publication

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3