P10613 (CP51_CANAL) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 94.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | 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 names |
| ||||||
| Organism | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) | ||||||
| Taxonomic identifier | 237561 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida |
Protein attributes
| Sequence length | 528 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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 | Obtusifoliol + 3 O2 + 3 NADPH = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + 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 process | Lipid synthesis Steroid biosynthesis Sterol biosynthesis |
| Cellular component | Membrane |
| Ligand | Heme Iron Metal-binding NADP |
| Molecular function | Monooxygenase Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | cellular response to drug Inferred from mutant phenotype. Source: CGD ergosterol biosynthetic processInferred from genetic interaction. Source: CGD membrane raft polarizationInferred from mutant phenotype. Source: CGD |
| Cellular component | integral to membrane Inferred from direct assay. Source: CGD membrane fractionInferred from direct assay. Source: CGD plasma membraneInferred from direct assay. Source: CGD |
| Molecular function | drug binding Inferred from direct assay. Source: CGD electron carrier activityInferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro sterol 14-demethylase activityInferred from direct assay. Source: CGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 528 | 528 | Lanosterol 14-alpha demethylase | PRO_0000052003 | |||||
Sites | |||||||||
| Metal binding | 470 | 1 | Iron (heme axial ligand) By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 105 | 1 | F → L in fluconazole-resistant isolates. | ||||||
| Natural variant | 266 | 1 | E → D in strain: fluconazole-resistant isolates. | ||||||
| Natural variant | 287 | 1 | K → R in strain: fluconazole-resistant isolates. | ||||||
| Natural variant | 450 | 1 | G → E in strain: fluconazole-resistant isolates. | ||||||
| Natural variant | 464 | 1 | G → S in strain: fluconazole-resistant isolates. | ||||||
| Natural variant | 467 | 1 | R → K in strain: Isolate 13; azole-resistant. Ref.4 | ||||||
| Natural variant | 488 | 1 | V → I in strain: fluconazole-resistant isolates. | ||||||
Experimental info | |||||||||
| Sequence conflict | 19 | 1 | V → D in AAB08099. Ref.4 | ||||||
Sequences
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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: 2644625] [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: 15123810] [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: 9210671] [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: 7819160] [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: 9228762] [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. |
| PIR | O4CK51. S02713. |
| RefSeq | XP_716761.1. XM_711668.1. |
3D structure databases | |
| ProteinModelPortal | P10613. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P10613. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 3641571. |
| KEGG | cal:CaO19.922. |
Organism-specific databases | |
| CGD | CAL0003627. ERG11. |
Phylogenomic databases | |
| PhylomeDB | P10613. |
Enzyme and pathway databases | |
| BRENDA | 1.14.13.70. 1096. |
Family and domain databases | |
| InterPro | IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002403. Cyt_P450_E_grp-IV. [Graphical view] |
| Gene3D | G3DSA:1.10.630.10. Cyt_P450. 1 hit. |
| KO | K05917. |
| Pfam | PF00067. p450. 1 hit. [Graphical view] |
| PRINTS | PR00465. EP450IV. PR00385. P450. |
| SUPFAM | SSF48264. Cytochrome_P450. 1 hit. |
| PROSITE | PS00086. CYTOCHROME_P450. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| DrugBank | DB00646. Nystatin. |
Entry information
| Entry name | CP51_CANAL | ||||||||
| Accession | Primary (citable) accession number: P10613 Secondary accession number(s): Q5A524, Q92208 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Candida albicans Candida albicans: entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with