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UniProtKB/Swiss-Prot entry P0A512


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CP51_MYCTU
Primary accession number P0A512
Secondary accession number P77901
Integrated into Swiss-Prot on March 15, 2005
Sequence was last modified on March 15, 2005 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 37)
Name and origin of the protein
Protein name Cytochrome P450 51
Synonyms EC 1.14.13.70
CYPLI
P450-LIA1
Sterol 14-alpha demethylase
Lanosterol 14-alpha demethylase
P450-14DM
Gene name
Name: cyp51
OrderedLocusNames: Rv0764c, MT0788
ORFNames: MTCY369.09c
From
Mycobacterium tuberculosis [TaxID: 1773] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
DOI=10.1038/31159; PubMed=9634230 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.";
Nature 393:537-544(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CDC 1551 / Oshkosh;
DOI=10.1128/JB.184.19.5479-5490.2002; PubMed=12218036 [NCBI, ExPASy, EBI, Israel, Japan]
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., Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains.";
J. Bacteriol. 184:5479-5490(2002).
[3]
CHARACTERIZATION.
PubMed=9756611 [NCBI, ExPASy, EBI, Israel, Japan]
Aoyama Y., Horiuchi T., Gotoh O., Noshiro M., Yoshida Y.;
"CYP51-like gene of Mycobacterium tuberculosis actually encodes a P450 similar to eukaryotic CYP51.";
J. Biochem. 124:694-696(1998).
[4]
CHARACTERIZATION.
DOI=10.1073/pnas.96.16.8937; PubMed=10430874 [NCBI, ExPASy, EBI, Israel, Japan]
Bellamine A., Mangla A.T., Nes W.D., Waterman M.R.;
"Characterization and catalytic properties of the sterol 14 alpha-demethylase from Mycobacterium tuberculosis.";
Proc. Natl. Acad. Sci. U.S.A. 96:8937-8942(1999).
[5]
CHARACTERIZATION.
PubMed=11160374 [NCBI, ExPASy, EBI, Israel, Japan]
Bellamine A., Mangla A.T., Dennis A.L., Nes W.D., Waterman M.R.;
"Structural requirements for substrate recognition of Mycobacterium tuberculosis 14alpha-demethylase: implications for sterol biosynthesis.";
J. Lipid Res. 42:128-136(2001).
[6]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1073/pnas.061562898; PubMed=11248033 [NCBI, ExPASy, EBI, Israel, Japan]
Podust L.M., Poulos T.L., Waterman M.R.;
"Crystal structure of cytochrome P450 14 alpha-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors.";
Proc. Natl. Acad. Sci. U.S.A. 98:3068-3073(2001).
Comments
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
BX842574; CAB02394.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000516; AAK45030.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G70706; G70706.
RefSeq NP_215278.1; -.
NP_335216.1; -.
3D structure databases
PDB
1E9X; X-ray; 2.10 A; A=1-451.[ExPASy / RCSB / EBI]
1EA1; X-ray; 2.21 A; A=1-451.[ExPASy / RCSB / EBI]
1H5Z; X-ray; 2.05 A; A=1-451.[ExPASy / RCSB / EBI]
1U13; X-ray; 2.01 A; A=1-451.[ExPASy / RCSB / EBI]
1X8V; X-ray; 1.55 A; A=1-451.[ExPASy / RCSB / EBI]
2BZ9; X-ray; 2.21 A; A/B=1-451.[ExPASy / RCSB / EBI]
2CI0; X-ray; 1.53 A; A=1-451.[ExPASy / RCSB / EBI]
2CIB; X-ray; 1.50 A; A=1-451.[ExPASy / RCSB / EBI]
2VKU; X-ray; 1.95 A; A=1-451.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1E9X; -.
1EA1; -.
1H5Z; -.
1U13; -.
1X8V; -.
2BZ9; -.
2CI0; -.
2CIB; -.
2VKU; -.
ModBase P0A512.
Organism-specific databases
TubercuList Rv0764c; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (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.
Genome annotation databases
GeneID 888819; -.
926091; -.
GenomeReviews AE000516_GR; MT0788.
AL123456_GR; Rv0764c.
KEGG mtc:MT0788; -.
mtu:Rv0764c; -.
TIGR MT0788; -.
Phylogenomic databases
HOGENOM P0A512; -.
Other
DrugBank DB04573; Estriol.
ProtoNet P0A512.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Heme; Iron; Lipid synthesis; Metal-binding; Monooxygenase; NADP; Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   451  451     Cytochrome P450 51. PRO_0000052017
METAL   394   394        Iron (heme axial ligand). 
HELIX   19    24  6      
HELIX   26    37  12      
STRAND   39    45  7      
STRAND   48    53  6      
HELIX   55    64  10      
TURN   67    69  3      
HELIX   77    79  3      
HELIX   80    83  4      
HELIX   93   101  9      
TURN   102   105  4      
HELIX   107   125  19      
STRAND   130   135  6      
HELIX   136   152  17      
HELIX   155   158  4      
HELIX   163   174  12      
HELIX   178   181  4      
HELIX   189   214  26      
STRAND   218   220  3      
HELIX   225   231  7      
STRAND   237   240  4      
HELIX   243   274  32      
HELIX   276   289  14      
HELIX   290   292  3      
HELIX   296   299  4      
HELIX   305   317  13      
STRAND   324   330  7      
STRAND   332   334  3      
STRAND   337   339  3      
STRAND   344   347  4      
HELIX   349   352  4      
TURN   356   358  3      
STRAND   359   361  3      
HELIX   367   370  4      
TURN   372   374  3      
HELIX   376   379  4      
TURN   381   383  3      
HELIX   390   392  3      
HELIX   397   414  18      
STRAND   415   421  7      
HELIX   423   425  3      
STRAND   431   434  4      
STRAND   442   447  6      
Sequence information
Length: 451 AA [This is the length of the unprocessed precursor] Molecular weight: 50878 Da [This is the MW of the unprocessed precursor] CRC64: B3D671EA9542A57B [This is a checksum on the sequence]
        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 

P0A512 in FASTA format

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