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P50859 (CP51_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:CAGL0E04334g
OrganismCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier284593 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length533 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 By similarity.

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 processLipid synthesis
Steroid biosynthesis
Sterol biosynthesis
   Cellular componentMembrane
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processsterol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmembrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

sterol 14-demethylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 533533Lanosterol 14-alpha demethylase
PRO_0000052004

Sites

Metal binding4721Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict641I → M in AAB32679. Ref.3
Sequence conflict4731I → T in AAB32679. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P50859 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: A0506C17507E6EF7

FASTA53361,305
        10         20         30         40         50         60 
MSTENTSLVV ELLEYVKLGL SYFQALPLAQ RVSIMVALPF VYTITWQLLY SLRKDRPPLV 

        70         80         90        100        110        120 
FYWIPWVGSA IPYGTKPYEF FEDCQKKYGD IFSFMLLGRI MTVYLGPKGH EFIFNAKLAD 

       130        140        150        160        170        180 
VSAEAAYSHL TTPVFGKGVI YDCPNHRLME QKKFVKGALT KEAFVRYVPL IAEEIYKYFR 

       190        200        210        220        230        240 
NSKNFKINEN NSGIVDVMVS QPEMTIFTAS RSLLGKEMRD KLDTDFAYLY SDLDKGFTPI 

       250        260        270        280        290        300 
NFVFPNLPLE HYRKRDHAQQ AISGTYMSLI KERREKNDIQ NRDLIDELMK NSTYKDGTKM 

       310        320        330        340        350        360 
TDQEIANLLI GVLMGGQHTS AATSAWCLLH LAERPDVQEE LYQEQMRVLN NDTKELTYDD 

       370        380        390        400        410        420 
LQNMPLLNQM IKETLRLHHP LHSLFRKVMR DVAIPNTSYV VPRDYHVLVS PGYTHLQEEF 

       430        440        450        460        470        480 
FPKPNEFNIH RWDGDAASSS AAGGDEVDYG FGAISKGVSS PYLPFGGGRH RCIGELFAYC 

       490        500        510        520        530 
QLGVLMSIFI RTMKWRYPTE GETVPPSDFT SMVTLPTAPA KIYWEKRHPE QKY

« Hide

References

« Hide 'large scale' references
[1]"Deletion of the Candida glabrata ERG3 and ERG11 genes: effect on cell viability, cell growth, sterol composition, and antifungal susceptibility."
Geber A., Hitchcock C.A., Swartz J.E., Pullen F.S., Marsden K.E., Kwon-Chung K.J., Bennett J.E.
Antimicrob. Agents Chemother. 39:2708-2717(1995) [PubMed: 8593007] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 2001-L5.
[2]"Genome evolution in yeasts."
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. expand/collapse author list , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
Nature 430:35-44(2004) [PubMed: 15229592] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.
[3]"Rapid detection and identification of Candida albicans and Torulopsis (Candida) glabrata in clinical specimens by species-specific nested PCR amplification of a cytochrome P-450 lanosterol-alpha-demethylase (L1A1) gene fragment."
Burgener-Kairuz P., Zuber J.P., Jaunin P., Buchman T.G., Bille J., Rossier M.
J. Clin. Microbiol. 32:1902-1907(1994) [PubMed: 7989540] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-473.
Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L40389 Genomic DNA. Translation: AAB02329.1.
CR380951 Genomic DNA. Translation: CAG58795.1.
S75389 Genomic DNA. Translation: AAB32679.1.
RefSeqXP_445876.1. XM_445876.1.

3D structure databases

ProteinModelPortalP50859.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2887532.
GenomeReviewsGene locus CAGL0E04334g in contig CR380951_GR.
KEGGcgr:CAGL0E04334g.

Phylogenomic databases

eggNOGfuNOG06039.
HOGENOMHBG566517.
OMASSISAWI.
OrthoDBEOG4QJVWH.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
KOK05917.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00465. EP450IV.
PR00385. P450.
SUPFAMSSF48264. Cytochrome_P450. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00639. Butoconazole.
DB01167. Itraconazole.
DB01110. Miconazole.

Entry information

Entry nameCP51_CANGA
AccessionPrimary (citable) accession number: P50859
Secondary accession number(s): Q02312
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 14, 2011
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents