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Reviewed, UniProtKB/Swiss-Prot P0A512 (CP51_MYCTU)

Last modified June 16, 2009. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Lanosterol 14-alpha demethylase
    EC=1.14.13.70
Alternative name(s):
    Cytochrome P450 51
    CYPLI
    P450-LIA1
    Sterol 14-alpha demethylase
    P450-14DM
Gene names
Name: cyp51
Ordered Locus Names: Rv0764c, MT0788
ORF Names: MTCY369.09c
OrganismMycobacterium tuberculosis [Complete proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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.

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.

Pathway

Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6.

Subunit structure

Monomer Probable.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the cytochrome P450 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Lanosterol 14-alpha demethylase
PRO_0000052017

Sites

Metal binding3941Iron (heme axial ligand)

Secondary structure

............................................................................... 451
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A512-1 [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

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"CYP51-like gene of Mycobacterium tuberculosis actually encodes a P450 similar to eukaryotic CYP51."
Aoyama Y., Horiuchi T., Gotoh O., Noshiro M., Yoshida Y.
J. Biochem. 124:694-696(1998) [PubMed: 9756611] [Abstract]
Cited for: CHARACTERIZATION.
[4]"Characterization and catalytic properties of the sterol 14 alpha-demethylase from Mycobacterium tuberculosis."
Bellamine A., Mangla A.T., Nes W.D., Waterman M.R.
Proc. Natl. Acad. Sci. U.S.A. 96:8937-8942(1999) [PubMed: 10430874] [Abstract]
Cited for: CHARACTERIZATION.
[5]"Structural requirements for substrate recognition of Mycobacterium tuberculosis 14alpha-demethylase: implications for sterol biosynthesis."
Bellamine A., Mangla A.T., Dennis A.L., Nes W.D., Waterman M.R.
J. Lipid Res. 42:128-136(2001) [PubMed: 11160374] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Crystal structure of cytochrome P450 14 alpha-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors."
Podust L.M., Poulos T.L., Waterman M.R.
Proc. Natl. Acad. Sci. U.S.A. 98:3068-3073(2001) [PubMed: 11248033] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

BX842574 Genomic DNA. Translation: CAB02394.1.
AE000516 Genomic DNA. Translation: AAK45030.1.
PIRG70706.
RefSeqNP_215278.1.
NP_335216.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1E9XX-ray2.10A1-451[»]
1EA1X-ray2.21A1-451[»]
1H5ZX-ray2.05A1-451[»]
1U13X-ray2.01A1-451[»]
1X8VX-ray1.55A1-451[»]
2BZ9X-ray2.21A/B1-451[»]
2CI0X-ray1.53A1-451[»]
2CIBX-ray1.50A1-451[»]
2VKUX-ray1.95A1-451[»]
2W09X-ray1.57A1-451[»]
2W0AX-ray1.60A1-451[»]
2W0BX-ray1.56A1-451[»]
ModBaseSearch...

Genome annotation databases

GeneID888819.
926091.
GenomeReviewsGene locus MT0788 in contig AE000516_GR.
Gene locus Rv0764c in contig AL123456_GR.
KEGGmtc:MT0788.
mtu:Rv0764c.
TIGRMT0788.

Organism-specific databases

TubercuListRv0764c.

Phylogenomic databases

HOGENOMP0A512.
OMAP0A512. MEQVTGG.

Enzyme and pathway databases

BRENDA1.14.13.70. 809.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR017973. Cyt_P450_C.
IPR017972. Cyt_P450_CS.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHERPTHR19383. Cyt_P450. 1 hit.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00465. EP450IV.
PR00385. P450.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB04573. Estriol.

Entry information

Entry nameCP51_MYCTU
AccessionPrimary (citable) accession number: P0A512
Secondary accession number(s): P77901
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents