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P10613 (CP51_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ERG11
Synonyms:CYP51, ERG16
ORF Names:CaO19.922
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

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

Cofactor

Heme group By similarity.

Pathway

Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6.

Subcellular location

Membrane Potential.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Biological processLipid biosynthesis
Lipid metabolism
Steroid biosynthesis
Steroid metabolism
Sterol biosynthesis
Sterol metabolism
   Cellular componentMembrane
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell growth mode switching, budding to filamentous

Inferred from mutant phenotype PubMed 16246085. Source: CGD

cellular response to drug

Inferred from mutant phenotype PubMed 15155210PubMed 15611610PubMed 17604452. Source: CGD

cellular response to starvation

Inferred from mutant phenotype PubMed 12773383. Source: CGD

chlamydospore formation

Inferred from mutant phenotype PubMed 18663031. Source: CGD

demethylation

Inferred from direct assay PubMed 10448088PubMed 10537192PubMed 15314102PubMed 20625155PubMed 7864896PubMed 8647850. Source: GOC

ergosterol biosynthetic process

Inferred from genetic interaction PubMed 7864896. Source: CGD

fatty acid omega-oxidation

Inferred from direct assay PubMed 17400174. Source: CGD

filamentous growth

Inferred from mutant phenotype PubMed 12773383. Source: CGD

filamentous growth of a population of unicellular organisms in response to biotic stimulus

Inferred from mutant phenotype PubMed 12773383. Source: CGD

filamentous growth of a population of unicellular organisms in response to starvation

Inferred from mutant phenotype PubMed 12773383. Source: CGD

lauric acid metabolic process

Inferred from mutant phenotype PubMed 11536334. Source: CGD

membrane raft polarization

Inferred from mutant phenotype PubMed 15189988. Source: CGD

   Cellular_componentendoplasmic reticulum

Inferred from sequence or structural similarity PubMed 10390230. Source: CGD

integral component of endoplasmic reticulum membrane

Inferred from sequence or structural similarity PubMed 11536334. Source: CGD

integral component of membrane

Inferred from direct assay PubMed 10393548. Source: CGD

membrane

Inferred from direct assay PubMed 16534748. Source: CGD

plasma membrane

Inferred from direct assay PubMed 19824013. Source: CGD

   Molecular_functionC-22 sterol desaturase activity

Inferred from sequence or structural similarity PubMed 10390230. Source: CGD

alkane 1-monooxygenase activity

Inferred from direct assay PubMed 17400174. Source: CGD

drug binding

Inferred from direct assay PubMed 10448088PubMed 20625155. Source: CGD

heme binding

Inferred from sequence or structural similarity PubMed 11536334. Source: CGD

iron ion binding

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity

Inferred from direct assay PubMed 18663031. Source: CGD

oxygen binding

Inferred from direct assay PubMed 18663031. Source: CGD

sterol 14-demethylase activity

Inferred from direct assay PubMed 10448088PubMed 10537192PubMed 15314102PubMed 20625155PubMed 7864896PubMed 8647850. Source: CGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 528528Lanosterol 14-alpha demethylase
PRO_0000052003

Sites

Metal binding4701Iron (heme axial ligand) By similarity

Natural variations

Natural variant1051F → L in fluconazole-resistant isolates.
Natural variant2661E → D in strain: fluconazole-resistant isolates.
Natural variant2871K → R in strain: fluconazole-resistant isolates.
Natural variant4501G → E in strain: fluconazole-resistant isolates.
Natural variant4641G → S in strain: fluconazole-resistant isolates.
Natural variant4671R → K in strain: Isolate 13; azole-resistant. Ref.4
Natural variant4881V → I in strain: fluconazole-resistant isolates.

Experimental info

Sequence conflict191V → D in AAB08099. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P10613 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 026948CEE4AF1B88

FASTA52860,675
        10         20         30         40         50         60 
MAIVETVIDG INYFLSLSVT QQISILLGVP FVYNLVWQYL YSLRKDRAPL VFYWIPWFGS 

        70         80         90        100        110        120 
AASYGQQPYE FFESCRQKYG DVFSFMLLGK IMTVYLGPKG HEFVFNAKLS DVSAEDAYKH 

       130        140        150        160        170        180 
LTTPVFGKGV IYDCPNSRLM EQKKFAKFAL TTDSFKRYVP KIREEILNYF VTDESFKLKE 

       190        200        210        220        230        240 
KTHGVANVMK TQPEITIFTA SRSLFGDEMR RIFDRSFAQL YSDLDKGFTP INFVFPNLPL 

       250        260        270        280        290        300 
PHYWRRDAAQ KKISATYMKE IKSRRERGDI DPNRDLIDSL LIHSTYKDGV KMTDQEIANL 

       310        320        330        340        350        360 
LIGILMGGQH TSASTSAWFL LHLGEKPHLQ DVIYQEVVEL LKEKGGDLND LTYEDLQKLP 

       370        380        390        400        410        420 
SVNNTIKETL RMHMPLHSIF RKVTNPLRIP ETNYIVPKGH YVLVSPGYAH TSERYFDNPE 

       430        440        450        460        470        480 
DFDPTRWDTA AAKANSVSFN SSDEVDYGFG KVSKGVSSPY LPFGGGRHRC IGEQFAYVQL 

       490        500        510        520 
GTILTTFVYN LRWTIDGYKV PDPDYSSMVV LPTEPAEIIW EKRETCMF 

« Hide

References

« Hide 'large scale' references
[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]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRO4CK51. S02713.
RefSeqXP_716761.1. XM_711668.1.

3D structure databases

ProteinModelPortalP10613.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5476.CAL0003627.

Chemistry

ChEMBLCHEMBL1780.
DrugBankDB00646. Nystatin.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3641571.
KEGGcal:CaO19.922.

Organism-specific databases

CGDCAL0003627. ERG11.

Phylogenomic databases

eggNOGCOG2124.
KOK05917.
OrthoDBEOG7712HB.

Enzyme and pathway databases

BRENDA1.14.13.70. 1096.
UniPathwayUPA00770; UER00754.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00465. EP450IV.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCP51_CANAL
AccessionPrimary (citable) accession number: P10613
Secondary accession number(s): Q5A524, Q92208
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Candida albicans

Candida albicans: entries and gene names