Lanosterol 14-alpha demethylase - Mycobacterium tuberculosis

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P0A512 (CP51_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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:	Rv0764c, MT0788
ORF Names:	MTCY369.09c

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	451 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Cytoplasm
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	sterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay Ref.3. Source: MTBBASE
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from direct assay Ref.3. Source: MTBBASE protein binding Inferred from physical interaction. Source: MTBBASE sterol 14-demethylase activity Inferred from direct assay Ref.4. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 451

451

Lanosterol 14-alpha demethylase

PRO_0000052017

Sites

Metal binding

394

Iron (heme axial ligand)

Secondary structure

451

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A512 [UniParc].

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

FASTA

451

50,878

        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' referencesShow '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. 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. 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

EMBL
GenBank
DDBJ

BX842574 Genomic DNA. Translation: CAB02394.1.
AE000516 Genomic DNA. Translation: AAK45030.1.

PIR

G70706.

RefSeq

NP_215278.1. NC_000962.2.
NP_335216.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E9X	X-ray	2.10	A	1-451	[»]
1EA1	X-ray	2.21	A	1-451	[»]
1H5Z	X-ray	2.05	A	1-451	[»]
1U13	X-ray	2.01	A	1-451	[»]
1X8V	X-ray	1.55	A	1-451	[»]
2BZ9	X-ray	2.21	A/B	1-451	[»]
2CI0	X-ray	1.53	A	1-451	[»]
2CIB	X-ray	1.50	A	1-451	[»]
2VKU	X-ray	1.95	A	1-451	[»]
2W09	X-ray	1.57	A	1-451	[»]
2W0A	X-ray	1.60	A	1-451	[»]
2W0B	X-ray	1.56	A	1-451	[»]

ProteinModelPortal

P0A512.

SMR

P0A512. Positions 1-449.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000002637; EBMYCP00000002637; EBMYCG00000002635.
EBMYCT00000071993; EBMYCP00000070052; EBMYCG00000071988.

GeneID

888819.
926091.

GenomeReviews

Gene locus MT0788 in contig AE000516_GR.
Gene locus Rv0764c in contig AL123456_GR.

KEGG

mtc:MT0788.
mtu:Rv0764c.

PATRIC

18123476. VBIMycTub22151_0866.

TIGR

MT0788.

Organism-specific databases

TubercuList

Rv0764c.

Phylogenomic databases

GeneTree

EBGT00050000015571.

HOGENOM

HBG566517.

OMA

ATYKDGR.

PhylomeDB

P0A512.

ProtClustDB

CLSK790721.

Family and domain databases

InterPro

IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view]

Gene3D

G3DSA:1.10.630.10. Cyt_P450. 1 hit.

K05917.

Pfam

PF00067. p450. 1 hit.
[Graphical view]

PRINTS

PR00465. EP450IV.
PR00385. P450.

SUPFAM

SSF48264. Cytochrome_P450. 1 hit.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB04573. Estriol.

Entry information

Entry name

CP51_MYCTU

Accession

Primary (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:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

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·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents