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P43098

- FAS2_CANAX

UniProt

P43098 - FAS2_CANAX

Protein

Fatty acid synthase subunit alpha

Gene

FAS2

Organism
Candida albicans (Yeast)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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 sitei1304 – 13041For beta-ketoacyl synthase activityBy similarity
    Metal bindingi1771 – 17711MagnesiumBy similarity
    Metal bindingi1772 – 17721Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi1773 – 17731MagnesiumBy similarity
    Binding sitei1797 – 17971Acetyl-CoABy similarity
    Binding sitei1807 – 18071Acetyl-CoABy similarity
    Metal bindingi1871 – 18711MagnesiumBy similarity
    Metal bindingi1872 – 18721Magnesium; 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
    OrganismiCandida albicans (Yeast)
    Taxonomic identifieri5476 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18851885Fatty acid synthase subunit alphaPRO_0000180284Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphopantetheine, Phosphoprotein

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP43098.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1157 – 1885729Beta-ketoacyl synthaseAdd
    BLAST
    Regioni1771 – 17733Acetyl-CoA bindingBy similarity
    Regioni1816 – 183217Acetyl-CoA bindingBy similarityAdd
    BLAST
    Regioni1840 – 18434Acetyl-CoA bindingBy similarity
    Regioni1870 – 18723Acetyl-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. 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.

    P43098-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPEIEQELS HTLLTELLAY QFASPVRWIE TQDVFLKQHN TERIIEIGPS     50
    PTLAGMANRT IKAKYESYDA ALSLQRQVLC YSKDAKEIYY KPDPADLAPK 100
    ETPKQEESTP SAPAAATPTP AAAAAPTPAP APASAGPVES IPDEPVKANL 150
    LIHVLVAQKL KKPLDAVPMT KAIKDLVNGK STVQNEILGD LGKEFGSTPE 200
    KPEDTPLEEL AEQFQDSFSG QLGKTSTSLI GRLMSSKMPG GFSITTARKY 250
    LESRFGLGAG RQDSVLLMAL TNEPANRLGS EADAKTFFDG IAQKYASSAG 300
    ISLSSGAGSG AGAANSGGAV VDSAALDALT AENKKLAKQQ LEVLARYLQS 350
    RLKQGSLKSF IKEKEASAVL QKELDLWEAE HGEFYAKGIQ PTFSALKSRT 400
    YDSYWNWARQ DVLSMYFDII FGKLTSVDRE TINQCIQIMN RANPTLIKFM 450
    QYHIDHCPEY KGETYKLAKR LGQQLIDNCK QVLTEDPVYK DVSRITGPKT 500
    KVSAKGNIEY EETQKDSVRK FEQYVYEMAQ GGAMTKVSQP TIQEDLARVY 550
    KAISKQASKD SKLELQRVYE DLLKVVESSK EIETEQLTKD ILQAATVPTT 600
    PTEEVDDPCT PSSDDEIASL PDKTSIIQPV SSTIPSQTIP FLHIQKKTKD 650
    GWEYNKKLSS LYLDGLESAA INGLTFKDKY VLVTGAGAGS IGAEILQGLI 700
    SGGAKVIVTT SRFSKKVTEY YQNMYARYGA AGSTLIVVPF NQGSKQDVDA 750
    LVQYIYDEPK KGGLGWDLDA IIPFAAIPEN GNGLDNIDSK SEFAHRIMLT 800
    NLLRLLGAVK SKKPTDTRPA QCILPLSPNH GTFGFDGLYS ESKISLETLF 850
    NRWYSEDWGS KLTVCGAVIG WTRGTGLMSA NNIIAEGIEK LGVRTFSQKE 900
    MAFNILGLLT PEIVQLCQEE PVMADLNGGL QFIDNLKDFT SKLRTDLLET 950
    ADIRRAVSIE SAIEQKVVNG DNVDANYSKV MVEPRANMKF DFPTLKSYDE 1000
    IKQIAPELEG MLDLENVVVV TGFAEVGPWG NSRTRWEMEA YGEFSLEGAI 1050
    EMAWIMGFIK YHNGNLQGKP YSGWVDAKTQ TPIDEKDIKS KYEEEILEHS 1100
    GIRLIEPELF NGYDPKKKQM IQEIVVQHDL EPFECSKETA EQYKHEHGEK 1150
    CEIFEIEESG EYTVRILKGA TLYVPKALRF DRLVAGQIPT GWDARTYGIP 1200
    EDTISQVDPI TLYVLVATVE ALLSAGITDP YEFYKYVHVS EVGNCSGSGM 1250
    GGVSALRGMF KDRYADKPVQ NDILQESFIN TMSAWVNMLL LSSSGPIKTP 1300
    VGACATAVES VDIGIETILS GKAKVVLVGG YDDFQEEGSY EFANMNATSN 1350
    SIEEFKHGRT PKEMSRPTTT TRNGFMEAQG SGIQVIMTAD LALKMGVPIH 1400
    AVLAMTATAT DKIGRSVPAP GKGILTTARE HHGNLKYPSP LLNIKYRKRQ 1450
    LNKRLEQIKS WEETELSYLQ EEAELAKEEF GDEFSMHEFL KERTEEVYRE 1500
    SKRQVSDAKK QWGNSFYKSD PRIAPLRGAL AAFNLTIDDI GVASFHGTST 1550
    VANDKNESAT INNMMKHLGR SEGNPVFGVF QKYLTGHPKG AAGAWMLNGA 1600
    IQILESGLVP GNRNADNVDK LLEQYEYVLY PSRSIQTDGI KAVSVTSFGF 1650
    GQKGAQAVVV HPDYLFAVLD RSTYEEYATK VSARNKKTYR YMHNAITRNT 1700
    MFVAKDKAPY SDELEQPVYL DPLARVEENK KKLVFSDKTI QSNQSYVGEV 1750
    AQKTAKALST LNKSSKGVGV DVELLSAINI DNETFIERNF TGNEVEYCLN 1800
    TAHPQASFTG TWSAKEAVFK ALGVESKGAG ASLIDIEITR DVNGAPKVIL 1850
    HGEAKKAAAK AGVKNVNISI SHDDFQATAV ALSEF 1885
    Length:1,885
    Mass (Da):207,589
    Last modified:November 1, 1995 - v1
    Checksum:i4835D57F362372E0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29063 Genomic DNA. Translation: AAA34345.1.
    PIRiJC4086.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29063 Genomic DNA. Translation: AAA34345.1 .
    PIRi JC4086.

    3D structure databases

    ProteinModelPortali P43098.
    ModBasei Search...
    MobiDBi Search...

    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. 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. "Analysis and expression of the Candida albicans FAS2 gene."
      Southard S.B., Cihlar R.L.
      Gene 156:133-138(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 4918.

    Entry informationi

    Entry nameiFAS2_CANAX
    AccessioniPrimary (citable) accession number: P43098
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 102 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