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Protein

Lanosterol 14-alpha demethylase

Gene

ERG11

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: -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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

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 – 66Combined sources6
Helixi68 – 79Combined sources12
Beta strandi81 – 87Combined sources7
Beta strandi90 – 95Combined sources6
Helixi98 – 105Combined sources8
Turni109 – 111Combined sources3
Helixi114 – 126Combined sources13
Beta strandi128 – 130Combined sources3
Helixi136 – 147Combined sources12
Helixi152 – 172Combined sources21
Turni174 – 176Combined sources3
Turni178 – 180Combined sources3
Beta strandi182 – 187Combined sources6
Helixi188 – 205Combined sources18
Helixi207 – 212Combined sources6
Helixi215 – 225Combined sources11
Helixi231 – 234Combined sources4
Helixi241 – 266Combined sources26
Beta strandi272 – 274Combined sources3
Helixi276 – 282Combined sources7
Helixi294 – 325Combined sources32
Helixi327 – 344Combined sources18
Helixi348 – 350Combined sources3
Helixi353 – 356Combined sources4
Helixi360 – 372Combined sources13
Beta strandi379 – 383Combined sources5
Beta strandi387 – 389Combined sources3
Beta strandi392 – 396Combined sources5
Beta strandi401 – 404Combined sources4
Helixi406 – 410Combined sources5
Turni413 – 415Combined sources3
Beta strandi416 – 418Combined sources3
Helixi424 – 428Combined sources5
Helixi430 – 434Combined sources5
Beta strandi438 – 440Combined sources3
Beta strandi444 – 454Combined sources11
Helixi466 – 468Combined sources3
Helixi473 – 490Combined sources18
Beta strandi491 – 494Combined sources4
Beta strandi496 – 499Combined sources4
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

Gene3Di1.10.630.10, 1 hit
InterProiView protein in InterPro
IPR001128 Cyt_P450
IPR017972 Cyt_P450_CS
IPR002403 Cyt_P450_E_grp-IV
IPR036396 Cyt_P450_sf
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

EnsemblFungiiAOW29509; AOW29509; CAALFM_C500660CA
GeneIDi3641571
KEGGical:CAALFM_C500660CA

Similar proteinsi

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: May 23, 2018
This is version 140 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

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