[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT PHE-136. STRAIN=FPE11; DOI=10.1016/S0378-1119(97)00141-8; PubMed=9300816 [NCBI, ExPASy, EBI, Israel, Japan] Delye C., Laigret F., Corio-Costet M.-F.; "Cloning and sequence analysis of the eburicol 14alpha-demethylase gene of the obligate biotrophic grape powdery mildew fungus."; Gene 195:29-33(1997).
[2]	SEQUENCE REVISION TO 515-517. Delye C., Laigret F., Corio-Costet M.-F.; Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[3]	MOLECULAR BASIS OF FUNGICIDE RESISTANCE. STRAIN=PAZ11; PubMed=9251183 [NCBI, ExPASy, EBI, Israel, Japan] Delye C., Laigret F., Corio-Costet M.-F.; "A mutation in the 14 alpha-demethylase gene of Uncinula necator that correlates with resistance to a sterol biosynthesis inhibitor."; Appl. Environ. Microbiol. 63:2966-2970(1997).

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-8,14,24²⁸-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). Membrane; Single-pass membrane protein.
SIMILARITY: Belongs to the cytochrome P450 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U72657; AAC49811.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U72658; AAC49812.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U83840; AAC49801.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

O14442.

Ontologies

GO:0016020;	Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0008398;	Molecular function: sterol 14-demethylase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0016126;	Biological process: sterol biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001128; Cyt_P450.
IPR002403; Cyt_P450_E_grp-IV.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.630.10; Cyt_P450; 1.

PANTHER

PTHR19383; Cyt_P450; 1.

Pfam

PF00067; p450; 1.
Pfam graphical view of domain structure.

PRINTS

PR00465; EP450IV.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.

Other

ProtoNet

O14442.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Heme; Iron; Lipid synthesis; Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 524`	`524`	`Cytochrome P450 51.`	`PRO_0000052010`
`METAL`	`469 469`		`Iron (heme axial ligand) (By similarity).`
`VARIANT`	`136 136`	`1`	`Y -> F (in strain: PAZ11; resistant to triadimenol; a sterol demethylation-inhibiting fungicide).`

Sequence information

Length: 524 AA [This is the length of the unprocessed precursor]

Molecular weight: 59840 Da [This is the MW of the unprocessed precursor]

CRC64: 24BE154B176CE09A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYIADILSDL LTQQTTRYGW IFMVTSIAFS IILLAVGLNV LSQLLFRRPY EPPVVFHWFP 

        70         80         90        100        110        120 
IIGSTISYGI DPYKFYFDCR AKYGDIFTFI LLGKKVTVYL GLQGNNFILN GKLKDVNAEE 

       130        140        150        160        170        180 
IYTNLTTPVF GRDVVYDCPN SKLMEQKKFM KTALTIEAFH SYVTIIQNEV EAYINNCVSF 

       190        200        210        220        230        240 
QGESGTVNIS KVMAEITIYT ASHALQGEEV RENFDSSFAA LYHDLDMGFT PINFTFYWAP 

       250        260        270        280        290        300 
LPWNRARDHA QRTVARTYMN IIQARREEKR SGENKHDIMW ELMRSTYKDG TPVPDREIAH 

       310        320        330        340        350        360 
MMIALLMAGQ HSSSSTSSWI MLWLAARPDI MEELYEEQLR IFGSEKPFPP LQYEDLSKLQ 

       370        380        390        400        410        420 
LHQNVLKEVL RLHAPIHSIM RKVKNPMIVP GTKYVIPTSH VLISSPGCTS QDATFFPDPL 

       430        440        450        460        470        480 
KWDPHRWDIG SGKVLGNDAV DEKYDYGYGL TSTGASSPYL PFGAGRHRCI GEQFATLQLV 

       490        500        510        520 
TIMATMVRFF RFRNIDGKQG VVKTDYSSLF SMPLAPALIG WEKR

O14442 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools