ERG11

Functionⁱ

Lanosterol 14-alpha demethylase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:8647850, PubMed:28258218).

The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity).

Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids (By similarity).

Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis (By similarity).

Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis (PubMed:6378256, PubMed:9161422).

Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core (PubMed:2185141).

In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions (By similarity).

The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis (PubMed:8647850, PubMed:28258218).

The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol (PubMed:11897574).

4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3 (PubMed:10783002, PubMed:12702354, PubMed:15552648).

ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25 (By similarity).

Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol (PubMed:9593144, PubMed:20946868).

The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol (By similarity).

The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol (PubMed:10433965).

The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain (By similarity).

Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (By similarity).

By similarity12 Publications

Catalytic activityⁱ

lanosterol
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 3
O₂
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See the description of this molecule in ChEBI.
+ 3
reduced [NADPH—hemoprotein reductase]
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Search chemical reactions in Rhea for this molecule.
=
4,4-dimethyl-5α-cholesta-8,14,24-trien-3β-ol
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
formate
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 4
H⁺
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See the description of this molecule in ChEBI.
+ 4
H₂O
Search proteins in UniProtKB for this molecule.
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See the description of this molecule in ChEBI.
+ 3
oxidized [NADPH—hemoprotein reductase]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.13
  "The mechanism of the acyl-carbon bond cleavage reaction catalyzed by recombinant sterol 14 alpha-demethylase of Candida albicans (other names are: lanosterol 14 alpha-demethylase, P-45014DM, and CYP51)."
  Shyadehi A.Z., Lamb D.C., Kelly S.L., Kelly D.E., Schunck W.H., Wright J.N., Corina D., Akhtar M.
  J. Biol. Chem. 271:12445-12450(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
- Ref.32
  "Structural analyses of Candida albicans sterol 14alpha-demethylase complexed with azole drugs address the molecular basis of azole-mediated inhibition of fungal sterol biosynthesis."
  Hargrove T.Y., Friggeri L., Wawrzak Z., Qi A., Hoekstra W.J., Schotzinger R.J., York J.D., Guengerich F.P., Lepesheva G.I.
  J. Biol. Chem. 292:6728-6743(2017) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 48-528 IN COMPLEX WITH INHIBITOR AND HEME, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, PATHWAY.
EC:
1.14.14.154
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.13
  "The mechanism of the acyl-carbon bond cleavage reaction catalyzed by recombinant sterol 14 alpha-demethylase of Candida albicans (other names are: lanosterol 14 alpha-demethylase, P-45014DM, and CYP51)."
  Shyadehi A.Z., Lamb D.C., Kelly S.L., Kelly D.E., Schunck W.H., Wright J.N., Corina D., Akhtar M.
  J. Biol. Chem. 271:12445-12450(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
- Ref.32
  "Structural analyses of Candida albicans sterol 14alpha-demethylase complexed with azole drugs address the molecular basis of azole-mediated inhibition of fungal sterol biosynthesis."
  Hargrove T.Y., Friggeri L., Wawrzak Z., Qi A., Hoekstra W.J., Schotzinger R.J., York J.D., Guengerich F.P., Lepesheva G.I.
  J. Biol. Chem. 292:6728-6743(2017) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 48-528 IN COMPLEX WITH INHIBITOR AND HEME, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, PATHWAY.
This reaction proceeds in the
forward
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.13
  "The mechanism of the acyl-carbon bond cleavage reaction catalyzed by recombinant sterol 14 alpha-demethylase of Candida albicans (other names are: lanosterol 14 alpha-demethylase, P-45014DM, and CYP51)."
  Shyadehi A.Z., Lamb D.C., Kelly S.L., Kelly D.E., Schunck W.H., Wright J.N., Corina D., Akhtar M.
  J. Biol. Chem. 271:12445-12450(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
- Ref.32
  "Structural analyses of Candida albicans sterol 14alpha-demethylase complexed with azole drugs address the molecular basis of azole-mediated inhibition of fungal sterol biosynthesis."
  Hargrove T.Y., Friggeri L., Wawrzak Z., Qi A., Hoekstra W.J., Schotzinger R.J., York J.D., Guengerich F.P., Lepesheva G.I.
  J. Biol. Chem. 292:6728-6743(2017) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 48-528 IN COMPLEX WITH INHIBITOR AND HEME, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, PATHWAY.
direction.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
lanosterol
zoom
+
3
O₂
+
3
reduced [NADPH—hemoprotein reductase]
FMNH₂
=
4,4-dimethyl-5α-cholesta-8,14,24-trien-3β-ol
zoom
+
formate
zoom
+
4
H⁺
+
4
H₂O
+
3
oxidized [NADPH—hemoprotein reductase]
FMN

Cofactorⁱ

heme2 Publications

Activity regulationⁱ

The catalytic activity is inhibited by the binding of azoles clotrimazole, miconazole, fluconazole, ketoconazole, oteseconazole (VT-1161), tetraconazole, the triazole SCH39304, and the triazole derivative ICI 153066.5 Publications

Kineticsⁱ

K_M=
6.3 µM for lanosterol
1 Publication
Manual assertion based on experiment inⁱ
Ref.32
"Structural analyses of Candida albicans sterol 14alpha-demethylase complexed with azole drugs address the molecular basis of azole-mediated inhibition of fungal sterol biosynthesis."
Hargrove T.Y., Friggeri L., Wawrzak Z., Qi A., Hoekstra W.J., Schotzinger R.J., York J.D., Guengerich F.P., Lepesheva G.I.
J. Biol. Chem. 292:6728-6743(2017) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 48-528 IN COMPLEX WITH INHIBITOR AND HEME, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, PATHWAY.

Pathwayⁱ: zymosterol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes zymosterol from lanosterol.2 Publications 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	Length
Binding siteⁱ	64	Oteseconazole; inhibitorCombined sources	1
Binding siteⁱ	118	Itraconazole; inhibitorCombined sources	1
Binding siteⁱ	307	Posaconazole; inhibitor; via carbonyl oxygenCombined sources	1
Binding siteⁱ	377	Oteseconazole; inhibitorCombined sources	1
Metal bindingⁱ	470	Iron (heme axial ligand)Combined sources	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

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

BRENDAⁱ	1.14.13.70, 11936 1.14.14.154, 1096
UniPathwayⁱ	UPA00770;UER00754

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Lanosterol 14-alpha demethylase1 Publication (EC:1.14.14.1542 Publications) Short name: LDM1 Publication Alternative name(s): Cytochrome P450 511 Publication Cytochrome P450-14DM1 Publication Cytochrome P450-LIA11 Publication Short name: CYPLI1 Publication Ergosterol biosynthesis protein 111 Publication Sterol 14-alpha demethylase1 Publication
Gene namesⁱ	Name:ERG111 Publication Synonyms:CYP511 Publication, ERG16 Ordered Locus Names:CAALFM_C500660CA ORF Names:CaO19.922
Organismⁱ	Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifierⁱ	237561 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Candida/Lodderomyces clade › Candida › Candida albicans
Proteomesⁱ	UP000000559 Componentⁱ: Chromosome 5

Organism-specific databases

Candida Genome Database More...CGDⁱ	CAL0000176310, ERG11
VEuPathDBⁱ	FungiDB:C5_00660C_A

Topology

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transmembraneⁱ	15 – 37	HelicalSequence analysisAdd BLAST		23

Keywords - Cellular componentⁱ

Endoplasmic reticulum, Membrane

Pathology & Biotechⁱ

Miscellaneous databases

PHI-baseⁱ

PHI:8030
PHI:8187

Chemistry databases

ChEMBLⁱ	CHEMBL1780
Drug and drug target database More...DrugBankⁱ	DB04794, Bifonazole DB00257, Clotrimazole DB01127, Econazole DB00196, Fluconazole DB08933, Luliconazole DB01110, Miconazole DB00239, Oxiconazole DB01263, Posaconazole DB01153, Sertaconazole DB00251, Terconazole DB01007, Tioconazole DB00582, Voriconazole
DrugCentral More...DrugCentralⁱ	P10613

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000052003	1 – 528	Lanosterol 14-alpha demethylaseAdd BLAST		528

Expressionⁱ

Inductionⁱ

Induced after prolonged growth with antifungal drugs such as clotrimazole, miconazole, fluconazole, itraconazole, ketoconazole, terbinafine and fenpropimorph.2 Publications

Interactionⁱ

Protein-protein interaction databases

STRINGⁱ	237561.P10613

STRINGⁱ

237561.P10613

Chemistry databases

BindingDBⁱ

P10613

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	28 – 40	Combined sources	13
Turnⁱ	56 – 58	Combined sources	3
Helixⁱ	61 – 66	Combined sources	6
Helixⁱ	68 – 79	Combined sources	12
Beta strandⁱ	81 – 87	Combined sources	7
Beta strandⁱ	90 – 95	Combined sources	6
Helixⁱ	98 – 105	Combined sources	8
Turnⁱ	109 – 111	Combined sources	3
Helixⁱ	114 – 126	Combined sources	13
Beta strandⁱ	128 – 130	Combined sources	3
Helixⁱ	136 – 147	Combined sources	12
Helixⁱ	152 – 172	Combined sources	21
Turnⁱ	174 – 176	Combined sources	3
Turnⁱ	178 – 180	Combined sources	3
Beta strandⁱ	182 – 187	Combined sources	6
Helixⁱ	188 – 205	Combined sources	18
Helixⁱ	207 – 212	Combined sources	6
Helixⁱ	215 – 225	Combined sources	11
Helixⁱ	231 – 234	Combined sources	4
Helixⁱ	241 – 266	Combined sources	26
Beta strandⁱ	272 – 274	Combined sources	3
Helixⁱ	276 – 282	Combined sources	7
Helixⁱ	294 – 325	Combined sources	32
Helixⁱ	327 – 344	Combined sources	18
Helixⁱ	348 – 350	Combined sources	3
Helixⁱ	353 – 356	Combined sources	4
Helixⁱ	360 – 372	Combined sources	13
Beta strandⁱ	379 – 383	Combined sources	5
Beta strandⁱ	387 – 389	Combined sources	3
Beta strandⁱ	392 – 396	Combined sources	5
Beta strandⁱ	401 – 404	Combined sources	4
Helixⁱ	406 – 410	Combined sources	5
Turnⁱ	413 – 415	Combined sources	3
Beta strandⁱ	416 – 418	Combined sources	3
Helixⁱ	424 – 428	Combined sources	5
Helixⁱ	430 – 434	Combined sources	5
Beta strandⁱ	438 – 440	Combined sources	3
Beta strandⁱ	444 – 454	Combined sources	11
Helixⁱ	466 – 468	Combined sources	3
Helixⁱ	473 – 490	Combined sources	18
Beta strandⁱ	491 – 494	Combined sources	4
Beta strandⁱ	496 – 499	Combined sources	4
Beta strandⁱ	506 – 509	Combined sources	4
Beta strandⁱ	517 – 522	Combined sources	6

Show more details

3D structure databases

SMRⁱ	P10613
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the cytochrome P450 family.Curated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG0684, Eukaryota
HOGENOMⁱ	CLU_001570_15_0_1
InParanoidⁱ	P10613
Database of Orthologous Groups More...OrthoDBⁱ	572303at2759

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
Pfam protein domain database More...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

Sequenceⁱ

Sequence statusⁱ: Complete.

P10613-1 [UniParc]FASTA Add 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 key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	19	V → D in AAB08099 (PubMed:9210671).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱ	105	F → L in strain: fluconazole-resistant isolates. 1 Publication	1
Natural variantⁱ	129	G → A in strain: azole-resistant isolates. 1 Publication	1
Natural variantⁱ	132	Y → H in strain: azole-resistant isolates. 2 Publications	1
Natural variantⁱ	145	F → L in strain: fluconazole-resistant isolates. 1 Publication	1
Natural variantⁱ	149	A → V in strain: fluconazole-resistant isolates. 1 Publication	1
Natural variantⁱ	153	D → E in strain: fluconazole-resistant isolates. 1 Publication	1
Natural variantⁱ	165	E → Y in strain: fluconazole-resistant isolates. 1 Publication	1
Natural variantⁱ	266	E → D in strain: fluconazole-resistant isolates. 1 Publication	1
Natural variantⁱ	279	S → F in strain: fluconazole-resistant isolates. 1 Publication	1
Natural variantⁱ	287	K → R in strain: fluconazole-resistant isolates. 1 Publication	1
Natural variantⁱ	405	S → F in strain: azole-resistant isolates. 1 Publication	1
Natural variantⁱ	448	G → E in strain: fluconazole-resistant isolates. 1 Publication	1
Natural variantⁱ	450	G → E in strain: fluconazole-resistant isolates. 1 Publication	1
Natural variantⁱ	452	V → A in strain: fluconazole-resistant isolates. 1 Publication	1
Natural variantⁱ	464	G → S in strain: fluconazole-resistant isolates. 2 Publications	1
Natural variantⁱ	465	G → S in strain: fluconazole-resistant isolates. 1 Publication	1
Natural variantⁱ	467	R → K in strain: Isolate 13; azole-resistant. 3 Publications	1
Natural variantⁱ	488	V → I in strain: fluconazole-resistant isolates. 1 Publication	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
PIRⁱ	S02713, O4CK51
NCBI Reference Sequences More...RefSeqⁱ	XP_716761.1, XM_711668.2

Genome annotation databases

GeneIDⁱ	3641571
KEGGⁱ	cal:CAALFM_C500660CA

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P10613	Cytochrome P450 L1A1		CANAX		528	UniRef100_P10613
Lanosterol 14-alpha-demethylase (Fragment)		CANAX		516
Lanosterol 14-alpha-demethylase (Fragment)		CANAX		512
Lanosterol 14-alpha-demethylase (Fragment)		CANAX		244
Lanosterol 14-alpha-demethylase (Fragment)		CANAX		123
+10

Protein	Similar proteins		Species	Score	Length	Source
P10613	Cytochrome P450 L1A1		CANAX		528	UniRef90_P10613
Lanosterol 14-alpha demethylase		CANDC		528
Erg11		CANDU		528
Cytochrome P450 51		CANAW		528
Lanosterol 14-alpha-demethylase (Fragment)		CANAX		516
+198

Protein	Similar proteins		Species	Score	Length	Source
P10613	Lanosterol 14-alpha demethylase	)	CANGA		533	UniRef50_P10613
Lanosterol 14-alpha demethylase		CANTR		528
Lanosterol 14-alpha demethylase		ASHGO		529
Lanosterol 14-alpha demethylase CYP51	)	YEAST		530
Cytochrome P450 L1A1		CANAX		528
+483

Cross-referencesⁱ

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
PIRⁱ	S02713, O4CK51
RefSeqⁱ	XP_716761.1, XM_711668.2

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	5FSA	X-ray	2.86	A/B	49-528	[»]
	5TZ1	X-ray	2.00	A/B	48-528	[»]
	5V5Z	X-ray	2.90	A	1-528	[»]
SMRⁱ	P10613
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	237561.P10613

STRINGⁱ

237561.P10613

Chemistry databases

BindingDBⁱ	P10613
ChEMBLⁱ	CHEMBL1780
DrugBankⁱ	DB04794, Bifonazole DB00257, Clotrimazole DB01127, Econazole DB00196, Fluconazole DB08933, Luliconazole DB01110, Miconazole DB00239, Oxiconazole DB01263, Posaconazole DB01153, Sertaconazole DB00251, Terconazole DB01007, Tioconazole DB00582, Voriconazole
DrugCentralⁱ	P10613

Genome annotation databases

GeneIDⁱ	3641571
KEGGⁱ	cal:CAALFM_C500660CA

Organism-specific databases

CGDⁱ	CAL0000176310, ERG11
VEuPathDBⁱ	FungiDB:C5_00660C_A

Phylogenomic databases

eggNOGⁱ	KOG0684, Eukaryota
HOGENOMⁱ	CLU_001570_15_0_1
InParanoidⁱ	P10613
OrthoDBⁱ	572303at2759

Enzyme and pathway databases

UniPathwayⁱ	UPA00770;UER00754
BRENDAⁱ	1.14.13.70, 11936 1.14.14.154, 1096

Miscellaneous databases

PHI-baseⁱ	PHI:8030 PHI:8187
Protein Ontology More...PROⁱ	PR:P10613

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_CANAL
Accessionⁱ	P10613Primary (citable) accession number: P10613 Secondary accession number(s): A0A1D8PMZ1, Q5A524, Q92208
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
	Last sequence update:	November 1, 1995
	Last modified:	February 23, 2022
	This is version 160 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

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UniProtKB - P10613 (CP51_CANAL)

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Lanosterol 14-alpha demethylase

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: zymosterol biosynthesis

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Endoplasmic reticulum

Plasma Membrane

Other locations

Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Miscellaneous databases

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

Pathwayⁱ: zymosterol biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ