[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 36112 / DSM 8217; Craft D.L., Loper J.C.; Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.

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

AF046863; AAF20263.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P77901; 1E9X. [HSSP ENTRY / PDB]

ModBase

Q9UVC3.

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

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`	`1 512`	`512`	`Cytochrome P450 51.`	`PRO_0000052006`
`METAL`	`458 458`		`Iron (heme axial ligand) (By similarity).`

Sequence information

Length: 512 AA [This is the length of the unprocessed precursor]

Molecular weight: 57677 Da [This is the MW of the unprocessed precursor]

CRC64: 5E10C9D415CA15B1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAIVSQISRF ITFTIISMGY SVLAVGVALT IHILSQLIVP KNPNEPPNVF SLIPVLGNAV 

        70         80         90        100        110        120 
QFGMNPVAFL QECQKKYGDV FTFTMVGKRV TVCLGADGNQ FVFNSKQNLS SAAEAYNHMT 

       130        140        150        160        170        180 
KYVFGPDVVY DAPHAVFMEQ KKFIKAGLNS DCFRQHVPMI VQETEEFFKK FNKPTGFIEA 

       190        200        210        220        230        240 
YETFGSLIIY TASRCLMGKE IRASLDGNVA KLYYDLDQGF KPINFIFPNL PLPSYRRRDV 

       250        260        270        280        290        300 
ACKKMADLYS SIIQRRKDEK DNNNADLLQA LMDATYKDGT HIPDHHIAGM MIAVLFGGQH 

       310        320        330        340        350        360 
TSATTSAWTI LELANRPDII KALREEQIEK LGSLKADLTF DNLKDLPLLE AAIRETLRLH 

       370        380        390        400        410        420 
PPIFQMMRRV VADKIVYEKN GMEIPKGNFI CAAPGVTQVD PTYFNEPTTY NPYRWIEKTD 

       430        440        450        460        470        480 
PVHQLEQGDD ANIDYGFGAV GISSKSPFLP FGAGRHRCIG EQFGYLQLKT VISTFIRTFD 

       490        500        510 
FDLDGKSVPK SDYTSMVVVP EHTAKVRYTW RE

Q9UVC3 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