NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 10895 / NRRL Y-1056 / CBS 109.51;
DOI=10.1126/science.1095781; PubMed=15001715 [NCBI, ExPASy, EBI, Israel, Japan]
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.;
"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome.";
Science 304:304-307(2004).

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

AE016817; AAS52083.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_984259.1; -.

3D structure databases

ModBase

Q759W0.

Organism-specific databases

AGD

ADR162W; -.

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.

ProtoNet

Q759W0.

Genome annotation databases

4620421; -.

fig|33169.1.peg.1904; -.

Phylogenomic databases

HOGENOM

Q759W0; -.

Other

UniRef

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

Keywords

Complete proteome; 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`	`1 529`	`529`	`Cytochrome P450 51.`	`PRO_0000052002`
`METAL`	`468 468`		`Iron (heme axial ligand) (By similarity).`

Sequence information

Length: 529 AA [This is the length of the unprocessed precursor]

Molecular weight: 60506 Da [This is the MW of the unprocessed precursor]

CRC64: BE674CB09ABD67DA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSESLLQTVV AYVELVLHHF MALSWTQQLS IVIVAPFIYS LVWQTLYSFR KDRVPLVPFM 

        70         80         90        100        110        120 
VPWVGSALAY GRAPYEFFGK CQQKYGDVFA FMLLGRVMTV YLGTKGHEFI LNAKLAEVSA 

       130        140        150        160        170        180 
EEAYTKLTTP VFGEGVVYDC PNHRLMEQKK FCKNALSTEA FRRYVPMVMD EVRKYLRTSK 

       190        200        210        220        230        240 
HFMMNERSSG VVNVMETQPE MTIFTASRSL LGAEMHSMLD ADFAYLYADL DKGFTPLNFV 

       250        260        270        280        290        300 
FRDLPLDNYR RRDNAQRTIS STYMKVIERR RKNNDVQDRD LIDALMTSAQ YKDGVKMTDQ 

       310        320        330        340        350        360 
QIANLLIGVL MGGQHTSAAT SAWVLLHLAE RPDIQEELYE EQMRVLDGGA KELTYELLQE 

       370        380        390        400        410        420 
MPLLNQVIKE TLRMHHPLHS LFRKVTRDMP VPNTSYVIPK DHYVLASPGF CHLSEEYFPN 

       430        440        450        460        470        480 
AKEFNPHRWD NDAASSVSTG EKVDYGFGAI SKGVSSPYLP FGGGRHRCIG EGFAYMQLGT 

       490        500        510        520 
IFSVVVRSMK WHFPADMKGV PNPDFTSMVT LPSEPCRIAW ERRVPDQII

Q759W0 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