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UniProtKB - P50859 (CP51_CANGA)
Protein
Lanosterol 14-alpha demethylase
Gene
ERG11
Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Status
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 (By similarity).
By similarityCatalytic activityi
- a 14α-methyl steroid + 3 O2 + 3 reduced [NADPH—hemoprotein reductase] = a Δ14 steroid + formate + 4 H+ + 4 H2O + 3 oxidized [NADPH—hemoprotein reductase]EC:1.14.14.154
Cofactori
hemeBy similarity
: zymosterol biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes zymosterol from lanosterol. 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 472 | Iron (heme axial ligand)By similarity | 1 |
GO - Molecular functioni
- heme binding Source: InterPro
- iron ion binding Source: InterPro
- sterol 14-demethylase activity Source: EnsemblFungi
GO - Biological processi
- ergosterol biosynthetic process Source: CGD
Keywordsi
Molecular function | Monooxygenase, Oxidoreductase |
Biological process | Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism |
Ligand | Heme, Iron, Metal-binding |
Enzyme and pathway databases
UniPathwayi | UPA00770;UER00754 |
Names & Taxonomyi
Protein namesi | Recommended name: Lanosterol 14-alpha demethylase (EC:1.14.14.154)Alternative name(s): CYPLI Cytochrome P450 51 Cytochrome P450-14DM Cytochrome P450-LIA1 Sterol 14-alpha demethylase |
Gene namesi | Name:ERG11 Synonyms:CYP51 Ordered Locus Names:CAGL0E04334g |
Organismi | Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
Taxonomic identifieri | 284593 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › Nakaseomyces/Candida clade › |
Proteomesi |
|
Organism-specific databases
CGDi | CAL0128884, ERG11 |
VEuPathDBi | FungiDB:CAGL0E04334g |
Subcellular locationi
Other locations
- Membrane Curated
Endoplasmic reticulum
- endoplasmic reticulum Source: EnsemblFungi
Other locations
- membrane Source: UniProtKB-SubCell
Keywords - Cellular componenti
MembranePathology & Biotechi
Chemistry databases
DrugBanki | DB09040, Efinaconazole DB11633, Isavuconazole DB01167, Itraconazole DB01026, Ketoconazole |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000052004 | 1 – 533 | Lanosterol 14-alpha demethylaseAdd BLAST | 533 |
Proteomic databases
PRIDEi | P50859 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P50859 |
SMRi | P50859 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the cytochrome P450 family.Curated
Phylogenomic databases
eggNOGi | KOG0684, Eukaryota |
HOGENOMi | CLU_001570_15_0_1 |
InParanoidi | P50859 |
OMAi | AWTLIEL |
Family and domain databases
Gene3Di | 1.10.630.10, 1 hit |
InterProi | View protein in InterPro IPR001128, Cyt_P450 IPR017972, Cyt_P450_CS IPR002403, Cyt_P450_E_grp-IV IPR036396, Cyt_P450_sf |
Pfami | View protein in Pfam PF00067, p450, 1 hit |
PRINTSi | PR00465, EP450IV PR00385, P450 |
SUPFAMi | SSF48264, SSF48264, 1 hit |
PROSITEi | View protein in PROSITE PS00086, CYTOCHROME_P450, 1 hit |
i Sequence
Sequence statusi: Complete.
P50859-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSTENTSLVV ELLEYVKLGL SYFQALPLAQ RVSIMVALPF VYTITWQLLY
60 70 80 90 100
SLRKDRPPLV FYWIPWVGSA IPYGTKPYEF FEDCQKKYGD IFSFMLLGRI
110 120 130 140 150
MTVYLGPKGH EFIFNAKLAD VSAEAAYSHL TTPVFGKGVI YDCPNHRLME
160 170 180 190 200
QKKFVKGALT KEAFVRYVPL IAEEIYKYFR NSKNFKINEN NSGIVDVMVS
210 220 230 240 250
QPEMTIFTAS RSLLGKEMRD KLDTDFAYLY SDLDKGFTPI NFVFPNLPLE
260 270 280 290 300
HYRKRDHAQQ AISGTYMSLI KERREKNDIQ NRDLIDELMK NSTYKDGTKM
310 320 330 340 350
TDQEIANLLI GVLMGGQHTS AATSAWCLLH LAERPDVQEE LYQEQMRVLN
360 370 380 390 400
NDTKELTYDD LQNMPLLNQM IKETLRLHHP LHSLFRKVMR DVAIPNTSYV
410 420 430 440 450
VPRDYHVLVS PGYTHLQEEF FPKPNEFNIH RWDGDAASSS AAGGDEVDYG
460 470 480 490 500
FGAISKGVSS PYLPFGGGRH RCIGELFAYC QLGVLMSIFI RTMKWRYPTE
510 520 530
GETVPPSDFT SMVTLPTAPA KIYWEKRHPE QKY
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 64 | I → M in AAB32679 (PubMed:7989540).Curated | 1 | |
Sequence conflicti | 473 | I → T in AAB32679 (PubMed:7989540).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L40389 Genomic DNA Translation: AAB02329.1 CR380951 Genomic DNA Translation: CAG58795.1 S75389 Genomic DNA Translation: AAB32679.1 |
RefSeqi | XP_445876.1, XM_445876.1 |
Genome annotation databases
EnsemblFungii | CAG58795; CAG58795; CAGL0E04334g |
GeneIDi | 2887532 |
KEGGi | cgr:CAGL0E04334g |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L40389 Genomic DNA Translation: AAB02329.1 CR380951 Genomic DNA Translation: CAG58795.1 S75389 Genomic DNA Translation: AAB32679.1 |
RefSeqi | XP_445876.1, XM_445876.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5JLC | X-ray | 2.40 | A | 20-533 | [»] | |
AlphaFoldDBi | P50859 | |||||
SMRi | P50859 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 5478.XP_445876.1 |
Chemistry databases
DrugBanki | DB09040, Efinaconazole DB11633, Isavuconazole DB01167, Itraconazole DB01026, Ketoconazole |
Proteomic databases
PRIDEi | P50859 |
Genome annotation databases
EnsemblFungii | CAG58795; CAG58795; CAGL0E04334g |
GeneIDi | 2887532 |
KEGGi | cgr:CAGL0E04334g |
Organism-specific databases
CGDi | CAL0128884, ERG11 |
VEuPathDBi | FungiDB:CAGL0E04334g |
Phylogenomic databases
eggNOGi | KOG0684, Eukaryota |
HOGENOMi | CLU_001570_15_0_1 |
InParanoidi | P50859 |
OMAi | AWTLIEL |
Enzyme and pathway databases
UniPathwayi | UPA00770;UER00754 |
Family and domain databases
Gene3Di | 1.10.630.10, 1 hit |
InterProi | View protein in InterPro IPR001128, Cyt_P450 IPR017972, Cyt_P450_CS IPR002403, Cyt_P450_E_grp-IV IPR036396, Cyt_P450_sf |
Pfami | View protein in Pfam PF00067, p450, 1 hit |
PRINTSi | PR00465, EP450IV PR00385, P450 |
SUPFAMi | SSF48264, SSF48264, 1 hit |
PROSITEi | View protein in PROSITE PS00086, CYTOCHROME_P450, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CP51_CANGA | |
Accessioni | P50859Primary (citable) accession number: P50859 Secondary accession number(s): Q02312 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | October 1, 1996 | |
Last modified: | May 25, 2022 | |
This is version 144 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families