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Protein

Lanosterol 14-alpha demethylase

Gene

ERG11

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

hemeBy similarity

Pathwayi: zymosterol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes zymosterol from lanosterol.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Lanosterol 14-alpha demethylase (ERG11)
  2. no protein annotated in this organism
  3. Methylsterol monooxygenase (ERG25)
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. no protein annotated in this organism
This subpathway is part of the pathway zymosterol biosynthesis, which is itself part of Steroid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes zymosterol from lanosterol, the pathway zymosterol biosynthesis and in Steroid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi470Iron (heme axial ligand)By similarity1

GO - Molecular functioni

  • drug binding Source: CGD
  • heme binding Source: InterPro
  • iron ion binding Source: InterPro
  • sterol 14-demethylase activity Source: CGD

GO - Biological processi

  • cell growth mode switching, budding to filamentous Source: CGD
  • cellular response to drug Source: CGD
  • ergosterol biosynthetic process Source: CGD
  • membrane raft polarization Source: CGD

Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
Biological processLipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
LigandHeme, 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
Ordered Locus Names:CAALFM_C500660CA
ORF Names:CaO19.922
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Chromosome 5

Organism-specific databases

CGDiCAL0000176310. ERG11.
EuPathDBiFungiDB:C5_00660C_A.

Subcellular locationi

GO - Cellular componenti

  • integral component of membrane Source: CGD
  • membrane Source: CGD
  • plasma membrane Source: CGD

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1780.
DrugBankiDB04794. Bifonazole.
DB00257. Clotrimazole.
DB01127. Econazole.
DB00196. Fluconazole.
DB01026. Ketoconazole.
DB08933. Luliconazole.
DB01110. Miconazole.
DB00239. Oxiconazole.
DB01263. Posaconazole.
DB01153. Sertaconazole.
DB00251. Terconazole.
DB01007. Tioconazole.
DB00582. Voriconazole.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000520031 – 528Lanosterol 14-alpha demethylaseAdd BLAST528

Proteomic databases

PRIDEiP10613.

Structurei

Secondary structure

1528
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi28 – 40Combined sources13
Turni56 – 58Combined sources3
Helixi61 – 64Combined sources4
Helixi68 – 79Combined sources12
Beta strandi82 – 84Combined sources3
Beta strandi90 – 95Combined sources6
Helixi97 – 104Combined sources8
Turni109 – 111Combined sources3
Beta strandi112 – 114Combined sources3
Helixi115 – 126Combined sources12
Helixi136 – 146Combined sources11
Helixi147 – 149Combined sources3
Helixi152 – 172Combined sources21
Turni174 – 176Combined sources3
Turni178 – 180Combined sources3
Beta strandi182 – 187Combined sources6
Helixi188 – 204Combined sources17
Helixi207 – 211Combined sources5
Helixi218 – 225Combined sources8
Helixi230 – 233Combined sources4
Helixi241 – 265Combined sources25
Turni266 – 268Combined sources3
Beta strandi272 – 274Combined sources3
Helixi276 – 282Combined sources7
Helixi294 – 325Combined sources32
Helixi328 – 344Combined sources17
Helixi348 – 350Combined sources3
Helixi353 – 356Combined sources4
Helixi360 – 372Combined sources13
Beta strandi379 – 385Combined sources7
Beta strandi401 – 404Combined sources4
Helixi406 – 410Combined sources5
Turni413 – 415Combined sources3
Helixi424 – 427Combined sources4
Beta strandi447 – 450Combined sources4
Beta strandi452 – 454Combined sources3
Helixi466 – 468Combined sources3
Helixi473 – 490Combined sources18
Beta strandi491 – 494Combined sources4
Beta strandi496 – 498Combined sources3
Beta strandi506 – 509Combined sources4
Beta strandi517 – 522Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5FSAX-ray2.86A/B49-528[»]
5TZ1X-ray2.00A/B48-528[»]
5V5ZX-ray2.90A1-528[»]
ProteinModelPortaliP10613.
SMRiP10613.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Phylogenomic databases

InParanoidiP10613.
KOiK05917.
OrthoDBiEOG092C1MV8.

Family and domain databases

InterProiView protein in InterPro
IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002403. Cyt_P450_E_grp-IV.
PfamiView protein in Pfam
PF00067. p450. 1 hit.
PRINTSiPR00465. EP450IV.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiView protein in PROSITE
PS00086. CYTOCHROME_P450. 1 hit.

Sequencei

Sequence statusi: Complete.

P10613-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIVETVIDG INYFLSLSVT QQISILLGVP FVYNLVWQYL YSLRKDRAPL
60 70 80 90 100
VFYWIPWFGS AASYGQQPYE FFESCRQKYG DVFSFMLLGK IMTVYLGPKG
110 120 130 140 150
HEFVFNAKLS DVSAEDAYKH LTTPVFGKGV IYDCPNSRLM EQKKFAKFAL
160 170 180 190 200
TTDSFKRYVP KIREEILNYF VTDESFKLKE KTHGVANVMK TQPEITIFTA
210 220 230 240 250
SRSLFGDEMR RIFDRSFAQL YSDLDKGFTP INFVFPNLPL PHYWRRDAAQ
260 270 280 290 300
KKISATYMKE IKSRRERGDI DPNRDLIDSL LIHSTYKDGV KMTDQEIANL
310 320 330 340 350
LIGILMGGQH TSASTSAWFL LHLGEKPHLQ DVIYQEVVEL LKEKGGDLND
360 370 380 390 400
LTYEDLQKLP SVNNTIKETL RMHMPLHSIF RKVTNPLRIP ETNYIVPKGH
410 420 430 440 450
YVLVSPGYAH TSERYFDNPE DFDPTRWDTA AAKANSVSFN SSDEVDYGFG
460 470 480 490 500
KVSKGVSSPY LPFGGGRHRC IGEQFAYVQL GTILTTFVYN LRWTIDGYKV
510 520
PDPDYSSMVV LPTEPAEIIW EKRETCMF
Length:528
Mass (Da):60,675
Last modified:November 1, 1995 - v2
Checksum:i026948CEE4AF1B88
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti19V → D in AAB08099 (PubMed:9210671).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti105F → L in fluconazole-resistant isolates. 1
Natural varianti266E → D in strain: fluconazole-resistant isolates. 1
Natural varianti287K → R in strain: fluconazole-resistant isolates. 1
Natural varianti450G → E in strain: fluconazole-resistant isolates. 1
Natural varianti464G → S in strain: fluconazole-resistant isolates. 1
Natural varianti467R → K in strain: Isolate 13; azole-resistant. 1 Publication1
Natural varianti488V → I in strain: fluconazole-resistant isolates. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
CP017627 Genomic DNA. Translation: AOW29509.1.
U67192 Genomic DNA. Translation: AAB08099.1.
U67193 Genomic DNA. Translation: AAB08100.1.
PIRiS02713. O4CK51.
RefSeqiXP_716761.1. XM_711668.2.

Genome annotation databases

GeneIDi3641571.
KEGGical:CAALFM_C500660CA.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiCP51_CANAL
AccessioniPrimary (citable) accession number: P10613
Secondary accession number(s): A0A1D8PMZ1, Q5A524, Q92208
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1995
Last modified: July 5, 2017
This is version 137 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families