Skip Header

Contribute Send feedback
Read comments (?) or add your own

P0A513 (CP51_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lanosterol 14-alpha demethylase
EC=1.14.13.70
Alternative name(s):
CYPLI
Cytochrome P450 51
Cytochrome P450-14DM
Cytochrome P450-LIA1
Sterol 14-alpha demethylase
Gene names
Name:cyp51
Ordered Locus Names:Mb0787c
OrganismMycobacterium bovis [Complete proteome] [HAMAP]
Taxonomic identifier1765 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Its precise biological substrate is not known. Catalyzes C14-demethylation of lanosterol, 24,25-dihydrolanosterol and obtusifoliol 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-8,14,24(28)-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.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Biological processLipid synthesis
Steroid biosynthesis
Sterol biosynthesis
   Cellular componentCytoplasm
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processsterol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

sterol 14-demethylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Lanosterol 14-alpha demethylase
PRO_0000052016

Sites

Metal binding3941Iron (heme axial ligand)

Sequences

Sequence LengthMass (Da)Tools
P0A513 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: B3D671EA9542A57B

FASTA45150,878
        10         20         30         40         50         60 
MSAVALPRVS GGHDEHGHLE EFRTDPIGLM QRVRDECGDV GTFQLAGKQV VLLSGSHANE 

        70         80         90        100        110        120 
FFFRAGDDDL DQAKAYPFMT PIFGEGVVFD ASPERRKEML HNAALRGEQM KGHAATIEDQ 

       130        140        150        160        170        180 
VRRMIADWGE AGEIDLLDFF AELTIYTSSA CLIGKKFRDQ LDGRFAKLYH ELERGTDPLA 

       190        200        210        220        230        240 
YVDPYLPIES FRRRDEARNG LVALVADIMN GRIANPPTDK SDRDMLDVLI AVKAETGTPR 

       250        260        270        280        290        300 
FSADEITGMF ISMMFAGHHT SSGTASWTLI ELMRHRDAYA AVIDELDELY GDGRSVSFHA 

       310        320        330        340        350        360 
LRQIPQLENV LKETLRLHPP LIILMRVAKG EFEVQGHRIH EGDLVAASPA ISNRIPEDFP 

       370        380        390        400        410        420 
DPHDFVPARY EQPRQEDLLN RWTWIPFGAG RHRCVGAAFA IMQIKAIFSV LLREYEFEMA 

       430        440        450 
QPPESYRNDH SKMVVQLAQP ACVRYRRRTG V

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX248336 Genomic DNA. Translation: CAD93649.1.
RefSeqNP_854445.1. NC_002945.3.

3D structure databases

ProteinModelPortalP0A513.
SMRP0A513. Positions 1-449.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000015424; EBMYCP00000015259; EBMYCG00000015421.
GeneID1092457.
GenomeReviewsGene locus Mb0787c in contig BX248333_GR.
KEGGmbo:Mb0787c.
PATRIC18003389. VBIMycBov88188_0857.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000015571.
HOGENOMHBG566517.
OMAATYKDGR.
ProtClustDBCLSK790721.

Enzyme and pathway databases

BioCycMBOV233413:MB0787C-MONOMER.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
KOK05917.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00465. EP450IV.
PR00385. P450.
SUPFAMSSF48264. Cytochrome_P450. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCP51_MYCBO
AccessionPrimary (citable) accession number: P0A513
Secondary accession number(s): P77901
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents