Lanosterol 14-alpha demethylase - Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

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P10613 (CP51_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names 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

Name:	ERG11
Synonyms:	CYP51, ERG16
ORF Names:	CaO19.922

Organism

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]

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	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 process	Lipid biosynthesis Lipid metabolism Steroid biosynthesis Steroid metabolism Sterol biosynthesis Sterol metabolism
Cellular component	Membrane
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell growth mode switching, budding to filamentous Inferred from mutant phenotype PubMed 16246085. Source: CGD cellular response to drug Inferred from mutant phenotype PubMed 15155210 PubMed 15611610 PubMed 17604452. Source: CGD ergosterol biosynthetic process Inferred from genetic interaction PubMed 7864896. Source: CGD membrane raft polarization Inferred from mutant phenotype PubMed 15189988. Source: CGD
Cellular_component	integral to membrane Inferred from direct assay PubMed 10393548. Source: CGD plasma membrane Inferred from direct assay PubMed 19824013. Source: CGD
Molecular_function	drug binding Inferred from direct assay PubMed 10448088 PubMed 20625155. Source: CGD electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro sterol 14-demethylase activity Inferred from direct assay PubMed 10448088 PubMed 10537192 PubMed 15314102 PubMed 20625155 PubMed 7864896 PubMed 8647850. 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

Iron (heme axial ligand) By similarity

Natural variations

Natural variant

105

F → L in fluconazole-resistant isolates.

Natural variant

266

E → D in strain: fluconazole-resistant isolates.

Natural variant

287

K → R in strain: fluconazole-resistant isolates.

Natural variant

450

G → E in strain: fluconazole-resistant isolates.

Natural variant

464

G → S in strain: fluconazole-resistant isolates.

Natural variant

467

R → K in strain: Isolate 13; azole-resistant. Ref.4

Natural variant

488

V → I in strain: fluconazole-resistant isolates.

Experimental info

Sequence conflict

V → D in AAB08099. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P10613 [UniParc].

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

FASTA

528

60,675

        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' referencesShow '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.
PIR	O4CK51. S02713.
RefSeq	XP_716761.1. XM_711668.1.
3D structure databases
ProteinModelPortal	P10613.
ModBase	Search...
Protein-protein interaction databases
STRING	5476.CAL0003627.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3641571.
KEGG	cal:CaO19.922.
Organism-specific databases
CGD	CAL0003627. ERG11.
Phylogenomic databases
eggNOG	COG2124.
KO	K05917.
Enzyme and pathway databases
BRENDA	1.14.13.70. 1096.
UniPathway	UPA00770; UER00754.
Family and domain databases
Gene3D	1.10.630.10. 1 hit.
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002403. Cyt_P450_E_grp-IV. [Graphical view]
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
ChEMBL	CHEMBL1780.
DrugBank	DB00646. Nystatin.

Entry information

Entry name

CP51_CANAL

Accession

Primary (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:	May 1, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]

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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents