UniProtKB - P9WPP9 (CP51_MYCTU)
Protein
Lanosterol 14-alpha demethylase
Gene
cyp51
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
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.2 Publications
Catalytic activityi
- a 14α-methyl steroid + 3 O2 + 3 reduced [NADPH—hemoprotein reductase] = a Δ14 steroid + formate + 4 H+ + 4 H2O + 3 oxidized [NADPH—hemoprotein reductase]1 PublicationEC:1.14.14.1541 Publication
Cofactori
heme1 Publication
Activity regulationi
Inhibited by alpha-ethyl-N-4-pyridinyl-benzeneacetamide (EPBA) and 4,4'-dihydroxybenzophenone (DHBP).1 Publication
: zymosterol biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes zymosterol from lanosterol.Proteins known to be involved in the 6 steps of the subpathway in this organism are:
- Lanosterol 14-alpha demethylase (cyp51)
- no protein annotated in this organism
- no protein annotated in this organism
- no protein annotated in this organism
- no protein annotated in this organism
- no protein annotated in this organism
View all proteins of this organism that are known to be involved in the subpathway that synthesizes zymosterol from lanosterol, the pathway zymosterol biosynthesis and in Steroid biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 72 | Heme6 Publications | 1 | |
Binding sitei | 76 | Heme6 Publications | 1 | |
Binding sitei | 97 | Heme6 Publications | 1 | |
Binding sitei | 259 | Substrate | 1 | |
Binding sitei | 326 | Heme6 Publications | 1 | |
Binding sitei | 392 | Heme6 Publications | 1 | |
Metal bindingi | 394 | Iron (heme axial ligand) | 1 | |
Binding sitei | 433 | Substrate | 1 |
GO - Molecular functioni
- heme binding Source: MTBBASE
- iron ion binding Source: InterPro
- sterol 14-demethylase activity Source: MTBBASE
GO - Biological processi
- oxidation-reduction process Source: GO_Central
- sterol biosynthetic process Source: UniProtKB-KW
- sterol metabolic process Source: MTBBASE
Keywordsi
Molecular function | Monooxygenase, Oxidoreductase |
Biological process | Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism |
Ligand | Heme, Iron, Metal-binding |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-4912-MONOMER |
UniPathwayi | UPA00770;UER00754 |
Chemistry databases
SwissLipidsi | SLP:000001161 |
Names & Taxonomyi
Protein namesi | Recommended name: Lanosterol 14-alpha demethylase (EC:1.14.14.1541 Publication)Alternative name(s): CYPLI Cytochrome P450 51 Cytochrome P450-14DM Cytochrome P450-LIA1 Sterol 14-alpha demethylase |
Gene namesi | Name:cyp51 Ordered Locus Names:Rv0764c ORF Names:MTCY369.09c |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv0764c |
Subcellular locationi
- Cytoplasm Curated
GO - Cellular componenti
- cytosol Source: MTBBASE
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000052017 | 1 – 451 | Lanosterol 14-alpha demethylaseAdd BLAST | 451 |
Proteomic databases
PaxDbi | P9WPP9 |
PRIDEi | P9WPP9 |
Interactioni
Subunit structurei
Homodimer.
6 PublicationsProtein-protein interaction databases
STRINGi | 83332.Rv0764c |
Chemistry databases
BindingDBi | P9WPP9 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P9WPP9 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the cytochrome P450 family.Curated
Phylogenomic databases
eggNOGi | ENOG41068W2 Bacteria COG2124 LUCA |
KOi | K05917 |
OMAi | AWTLIEL |
PhylomeDBi | P9WPP9 |
Family and domain databases
Gene3Di | 1.10.630.10, 1 hit |
InterProi | View protein in InterPro IPR001128 Cyt_P450 IPR017972 Cyt_P450_CS IPR002403 Cyt_P450_E_grp-IV IPR036396 Cyt_P450_sf |
Pfami | View protein in Pfam PF00067 p450, 1 hit |
PRINTSi | PR00465 EP450IV PR00385 P450 |
SUPFAMi | SSF48264 SSF48264, 1 hit |
PROSITEi | View protein in PROSITE PS00086 CYTOCHROME_P450, 1 hit |
i Sequence
Sequence statusi: Complete.
P9WPP9-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSAVALPRVS GGHDEHGHLE EFRTDPIGLM QRVRDECGDV GTFQLAGKQV
60 70 80 90 100
VLLSGSHANE FFFRAGDDDL DQAKAYPFMT PIFGEGVVFD ASPERRKEML
110 120 130 140 150
HNAALRGEQM KGHAATIEDQ VRRMIADWGE AGEIDLLDFF AELTIYTSSA
160 170 180 190 200
CLIGKKFRDQ LDGRFAKLYH ELERGTDPLA YVDPYLPIES FRRRDEARNG
210 220 230 240 250
LVALVADIMN GRIANPPTDK SDRDMLDVLI AVKAETGTPR FSADEITGMF
260 270 280 290 300
ISMMFAGHHT SSGTASWTLI ELMRHRDAYA AVIDELDELY GDGRSVSFHA
310 320 330 340 350
LRQIPQLENV LKETLRLHPP LIILMRVAKG EFEVQGHRIH EGDLVAASPA
360 370 380 390 400
ISNRIPEDFP DPHDFVPARY EQPRQEDLLN RWTWIPFGAG RHRCVGAAFA
410 420 430 440 450
IMQIKAIFSV LLREYEFEMA QPPESYRNDH SKMVVQLAQP ACVRYRRRTG
V
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP43511.1 |
PIRi | G70706 |
RefSeqi | NP_215278.1, NC_000962.3 WP_003898577.1, NZ_NVQJ01000035.1 |
Genome annotation databases
EnsemblBacteriai | CCP43511; CCP43511; Rv0764c |
GeneIDi | 888819 |
KEGGi | mtu:Rv0764c mtv:RVBD_0764c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP43511.1 |
PIRi | G70706 |
RefSeqi | NP_215278.1, NC_000962.3 WP_003898577.1, NZ_NVQJ01000035.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
SMRi | P9WPP9 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv0764c |
Chemistry databases
BindingDBi | P9WPP9 |
ChEMBLi | CHEMBL5090 |
DrugCentrali | P9WPP9 |
SwissLipidsi | SLP:000001161 |
Proteomic databases
PaxDbi | P9WPP9 |
PRIDEi | P9WPP9 |
Genome annotation databases
EnsemblBacteriai | CCP43511; CCP43511; Rv0764c |
GeneIDi | 888819 |
KEGGi | mtu:Rv0764c mtv:RVBD_0764c |
Organism-specific databases
TubercuListi | Rv0764c |
Phylogenomic databases
eggNOGi | ENOG41068W2 Bacteria COG2124 LUCA |
KOi | K05917 |
OMAi | AWTLIEL |
PhylomeDBi | P9WPP9 |
Enzyme and pathway databases
UniPathwayi | UPA00770;UER00754 |
BioCyci | MTBH37RV:G185E-4912-MONOMER |
Miscellaneous databases
PROi | PR:P9WPP9 |
Family and domain databases
Gene3Di | 1.10.630.10, 1 hit |
InterProi | View protein in InterPro IPR001128 Cyt_P450 IPR017972 Cyt_P450_CS IPR002403 Cyt_P450_E_grp-IV IPR036396 Cyt_P450_sf |
Pfami | View protein in Pfam PF00067 p450, 1 hit |
PRINTSi | PR00465 EP450IV PR00385 P450 |
SUPFAMi | SSF48264 SSF48264, 1 hit |
PROSITEi | View protein in PROSITE PS00086 CYTOCHROME_P450, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CP51_MYCTU | |
Accessioni | P9WPP9Primary (citable) accession number: P9WPP9 Secondary accession number(s): L0T4U1, P0A512, P77901 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | October 16, 2019 | |
This is version 38 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references