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P10613

- CP51_CANAL

UniProt

P10613 - CP51_CANAL

Protein

Lanosterol 14-alpha demethylase

Gene

ERG11

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol.

    Catalytic activityi

    A 14-alpha-methylsteroid + 3 O2 + 3 NADPH = a Delta(14)-steroid + formate + 3 NADP+ + 4 H2O.

    Cofactori

    Heme group.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi470 – 4701Iron (heme axial ligand)By similarity

    GO - Molecular functioni

    1. alkane 1-monooxygenase activity Source: CGD
    2. C-22 sterol desaturase activity Source: CGD
    3. drug binding Source: CGD
    4. heme binding Source: CGD
    5. iron ion binding Source: InterPro
    6. oxidoreductase activity Source: CGD
    7. oxygen binding Source: CGD
    8. sterol 14-demethylase activity Source: CGD

    GO - Biological processi

    1. cell growth mode switching, budding to filamentous Source: CGD
    2. cellular response to drug Source: CGD
    3. cellular response to starvation Source: CGD
    4. chlamydospore formation Source: CGD
    5. demethylation Source: GOC
    6. ergosterol biosynthetic process Source: CGD
    7. fatty acid omega-oxidation Source: CGD
    8. filamentous growth Source: CGD
    9. filamentous growth of a population of unicellular organisms in response to biotic stimulus Source: CGD
    10. filamentous growth of a population of unicellular organisms in response to starvation Source: CGD
    11. lauric acid metabolic process Source: CGD
    12. membrane raft polarization Source: CGD

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

    Keywords - Ligandi

    Heme, Iron, Metal-binding, NADP

    Enzyme and pathway databases

    BRENDAi1.14.13.70. 1096.
    UniPathwayiUPA00770; UER00754.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lanosterol 14-alpha demethylase (EC:1.14.13.70)
    Alternative name(s):
    CYPLI
    Cytochrome P450 51
    Cytochrome P450-14DM
    Cytochrome P450-LIA1
    Sterol 14-alpha demethylase
    Gene namesi
    Name:ERG11
    Synonyms:CYP51, ERG16
    ORF Names:CaO19.922
    OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
    Taxonomic identifieri237561 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
    ProteomesiUP000000559: Unassembled WGS sequence

    Organism-specific databases

    CGDiCAL0003627. ERG11.

    Subcellular locationi

    Membrane Curated

    GO - Cellular componenti

    1. endoplasmic reticulum Source: CGD
    2. integral component of endoplasmic reticulum membrane Source: CGD
    3. integral component of membrane Source: CGD
    4. membrane Source: CGD
    5. plasma membrane Source: CGD

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 528528Lanosterol 14-alpha demethylasePRO_0000052003Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi5476.CAL0003627.

    Structurei

    3D structure databases

    ProteinModelPortaliP10613.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Phylogenomic databases

    eggNOGiCOG2124.
    KOiK05917.
    OrthoDBiEOG7712HB.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002403. Cyt_P450_E_grp-IV.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00465. EP450IV.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P10613-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAIVETVIDG INYFLSLSVT QQISILLGVP FVYNLVWQYL YSLRKDRAPL    50
    VFYWIPWFGS AASYGQQPYE FFESCRQKYG DVFSFMLLGK IMTVYLGPKG 100
    HEFVFNAKLS DVSAEDAYKH LTTPVFGKGV IYDCPNSRLM EQKKFAKFAL 150
    TTDSFKRYVP KIREEILNYF VTDESFKLKE KTHGVANVMK TQPEITIFTA 200
    SRSLFGDEMR RIFDRSFAQL YSDLDKGFTP INFVFPNLPL PHYWRRDAAQ 250
    KKISATYMKE IKSRRERGDI DPNRDLIDSL LIHSTYKDGV KMTDQEIANL 300
    LIGILMGGQH TSASTSAWFL LHLGEKPHLQ DVIYQEVVEL LKEKGGDLND 350
    LTYEDLQKLP SVNNTIKETL RMHMPLHSIF RKVTNPLRIP ETNYIVPKGH 400
    YVLVSPGYAH TSERYFDNPE DFDPTRWDTA AAKANSVSFN SSDEVDYGFG 450
    KVSKGVSSPY LPFGGGRHRC IGEQFAYVQL GTILTTFVYN LRWTIDGYKV 500
    PDPDYSSMVV LPTEPAEIIW EKRETCMF 528
    Length:528
    Mass (Da):60,675
    Last modified:November 1, 1995 - v2
    Checksum:i026948CEE4AF1B88
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 191V → D in AAB08099. (PubMed:9210671)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti105 – 1051F → L in fluconazole-resistant isolates.
    Natural varianti266 – 2661E → D in strain: fluconazole-resistant isolates.
    Natural varianti287 – 2871K → R in strain: fluconazole-resistant isolates.
    Natural varianti450 – 4501G → E in strain: fluconazole-resistant isolates.
    Natural varianti464 – 4641G → S in strain: fluconazole-resistant isolates.
    Natural varianti467 – 4671R → K in strain: Isolate 13; azole-resistant. 1 Publication
    Natural varianti488 – 4881V → I in strain: fluconazole-resistant isolates.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13296 Genomic DNA. Translation: CAA31658.1.
    EU819548 Genomic DNA. Translation: ACF34636.1.
    EU819551 Genomic DNA. Translation: ACF34639.1.
    FJ002303 Genomic DNA. Translation: ACH91036.1.
    FJ403378 Genomic DNA. Translation: ACJ23064.1.
    AACQ01000063 Genomic DNA. Translation: EAK97774.1.
    U67192 Genomic DNA. Translation: AAB08099.1.
    U67193 Genomic DNA. Translation: AAB08100.1.
    PIRiS02713. O4CK51.
    RefSeqiXP_716761.1. XM_711668.1.

    Genome annotation databases

    GeneIDi3641571.
    KEGGical:CaO19.922.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13296 Genomic DNA. Translation: CAA31658.1 .
    EU819548 Genomic DNA. Translation: ACF34636.1 .
    EU819551 Genomic DNA. Translation: ACF34639.1 .
    FJ002303 Genomic DNA. Translation: ACH91036.1 .
    FJ403378 Genomic DNA. Translation: ACJ23064.1 .
    AACQ01000063 Genomic DNA. Translation: EAK97774.1 .
    U67192 Genomic DNA. Translation: AAB08099.1 .
    U67193 Genomic DNA. Translation: AAB08100.1 .
    PIRi S02713. O4CK51.
    RefSeqi XP_716761.1. XM_711668.1.

    3D structure databases

    ProteinModelPortali P10613.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5476.CAL0003627.

    Chemistry

    ChEMBLi CHEMBL1780.
    DrugBanki DB00646. Nystatin.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3641571.
    KEGGi cal:CaO19.922.

    Organism-specific databases

    CGDi CAL0003627. ERG11.

    Phylogenomic databases

    eggNOGi COG2124.
    KOi K05917.
    OrthoDBi EOG7712HB.

    Enzyme and pathway databases

    UniPathwayi UPA00770 ; UER00754 .
    BRENDAi 1.14.13.70. 1096.

    Family and domain databases

    Gene3Di 1.10.630.10. 1 hit.
    InterProi IPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002403. Cyt_P450_E_grp-IV.
    [Graphical view ]
    Pfami PF00067. p450. 1 hit.
    [Graphical view ]
    PRINTSi PR00465. EP450IV.
    PR00385. P450.
    SUPFAMi SSF48264. SSF48264. 1 hit.
    PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of cytochrome P450 L1A1 (lanosterol 14 alpha-demethylase) from Candida albicans."
      Lai M.H., Kirsch D.R.
      Nucleic Acids Res. 17:804-804(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: SC5314 / ATCC MYA-2876.
    2. "ERG11 mutations in oral strains of Candida albicans isolated in Sardinia."
      Orru G., Ciusa M.L., Pilia F., Taccori F., Cosentino S., Pisano M.B., Meloni M., Fadda M.E.
      Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CA100, CA11, CA36 and CA95.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SC5314 / ATCC MYA-2876.
    4. "The presence of an R467K amino acid substitution and loss of allelic variation correlate with an azole-resistant lanosterol 14-alpha demethylase in Candida albicans."
      White T.C.
      Antimicrob. Agents Chemother. 41:1488-1494(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48 AND 467-528, VARIANT LYS-467.
      Strain: SS.
    5. "Modeling cytochrome P450 14-alpha demethylase (Candida albicans) from P450cam."
      Boscott P.E., Grant G.H.
      J. Mol. Graph. 12:185-192(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.
    6. "Molecular analysis of cyp51 from fluconazole-resistant Candida albicans strains."
      Loffler J., Kelly S.L., Hebart H., Schumacher U., Lass-Florl C., Einsele H.
      FEMS Microbiol. Lett. 151:263-268(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FLUCONAZOLE-RESISTANT.

    Entry informationi

    Entry nameiCP51_CANAL
    AccessioniPrimary (citable) accession number: P10613
    Secondary accession number(s): Q5A524, Q92208
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 114 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Candida albicans
      Candida albicans: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3