Gene Rv2276
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. It has been shown to bind tighly to a range of azole-based antifungal drugs (e.g. miconazole, clotrimazole). |
| Product | Cytochrome P450 121 Cyp121 |
| Comments | Rv2276, (MT2336, MTCY339.34c), len: 396 aa. Cyp121, cytochrome P450 (see citation below), similar to e.g. G303644 (397 aa) opt: 675, z-score: 776.4, E(): 2.7e-36, (33.7% identity in 407 aa overlap); contains PS00086 Cytochrome P450 cysteine heme-iron ligand signature, similar to MTCY339.42, 29.2% identity in 298 aa overlap. |
| Functional category | Intermediary metabolism and respiration |
| Mutant | Non-essential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Non-essential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Found to be deleted (partially or completely) in one or more clinical isolates (See Tsolaki et al., 2004). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 2547749 | 2548939 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2276|cyp121
MTATVLLEVPFSARGDRIPDAVAELRTREPIRKVRTITGAEAWLVSSYALCTQVLEDRRFSMKETAAAGAPRLNALTVPPEVVNNMGNIADAGLRKAVMKAITPKAPGLEQFLRDTANSLLDNLITEGAPADLRNDFADPLATALHCKVLGIPQEDGPKLFRSLSIAFMSSADPIPAAKINWDRDIEYMAGILENPNITTGLMGELSRLRKDPAYSHVSDELFATIGVTFFGAGVISTGSFLTTALISLIQRPQLRNLLHEKPELIPAGVEELLRINLSFADGLPRLATADIQVGDVLVRKGELVLVLLEGANFDPEHFPNPGSIELDRPNPTSHLAFGRGQHFCPGSALGRRHAQIGIEALLKKMPGVDLAVPIDQLVWRTRFQRRIPERLPVLW
Bibliography
- Mowat CG et al. [2002]. Crystallization and preliminary crystallographic analysis of a novel cytochrome P450 from Mycobacterium tuberculosis. Structure
- Leys D et al. [2003]. Atomic structure of Mycobacterium tuberculosis CYP121 to 1.06 A reveals novel features of cytochrome P450. Structure
- Tsolaki AG, Hirsh AE, DeRiemer K, Enciso JA, Wong MZ, Hannan M, Goguet de la Salmoniere YO, Aman K, Kato-Maeda M and Small PM [2004]. Functional and evolutionary genomics of Mycobacterium tuberculosis: insights from genomic deletions in 100 strains. Mutant
- Seward HE et al. [2006]. Crystal structure of the Mycobacterium tuberculosis P450 CYP121-fluconazole complex reveals new azole drug-P450 binding mode. Structure
- Fontán PA et al. [2008]. Mycobacterium tuberculosis sigma factor E regulon modulates the host inflammatory response. Regulon
- DeJesus MA et al. [2017]. Comprehensive Essentiality Analysis of the Mycobacterium tuberculosis Genome via Saturating Transposon Mutagenesis. Mutant
- Minato Y et al. [2019]. Genomewide Assessment of Mycobacterium tuberculosis Conditionally Essential Metabolic Pathways. Mutant
