Gene Rv3247c
in Mycobacterium tuberculosis H37Rv
General annotation
Type | CDS |
Function | Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis [catalytic activity: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate]. |
Product | Thymidylate kinase Tmk (dTMP kinase) (thymidylic acid kinase) (TMPK) |
Comments | Rv3247c, (MTCY20B11.22c), len: 214 aa. tmk, thymidylate kinase, equivalent to Q9CCJ3|TMK|ML0772 putative thymidylate kinase from Mycobacterium leprae (210 aa), FASTA scores: opt: 1023, E(): 4.8e-57, (77.3% identity in 207 aa overlap). Also similar to other thymidylate kinases e.g. Q9RQJ9|KTHY_CAUCR|TMK|CC1824 from Caulobacter crescentus (208 aa), FASTA scores: opt: 179, E(): 0.0003, (31.3% identity in 214 aa overlap); Q9V1E9|KTHY_PYRAB|TMK|PAB0319 from Pyrococcus abyssi (205 aa), FASTA scores: opt: 176, E(): 0.00045, (29.1% identity in 189 aa overlap); etc. Belongs to the thymidylate kinase family. |
Functional category | Intermediary metabolism and respiration |
Proteomics | Identified by mass spectrometry in whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate or membrane protein fraction (See de Souza et al., 2011). Translational start site supported by proteomics data (See Kelkar et al., 2011). |
Mutant | Essential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Essential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Essential gene for in vitro growth of H37Rv, by Himar1 transposon mutagenesis (See Griffin et al., 2011). Check for mutants available at TARGET website |
Coordinates
Type | Start | End | Orientation |
---|---|---|---|
CDS | 3627419 | 3628063 | - |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3247c|tmk VLIAIEGVDGAGKRTLVEKLSGAFRAAGRSVATLAFPRYGQSVAADIAAEALHGEHGDLASSVYAMATLFALDRAGAVHTIQGLCRGYDVVILDRYVASNAAYSAARLHENAAGKAAAWVQRIEFARLGLPKPDWQVLLAVSAELAGERSRGRAQRDPGRARDNYERDAELQQRTGAVYAELAAQGWGGRWLVVGADVDPGRLAATLAPPDVPS
Bibliography
- Li de la Sierra I et al. [2001]. X-ray structure of TMP kinase from Mycobacterium tuberculosis complexed with TMP at 1.95 A resolution. Structure
- Ursby T et al. [2002]. Cryophotolysis of caged compounds: a technique for trapping intermediate states in protein crystals. Structure
- Fioravanti E et al. [2003]. Mycobacterium tuberculosis thymidylate kinase: structural studies of intermediates along the reaction pathway. Structure
- Haouz A et al. [2003]. Enzymatic and structural analysis of inhibitors designed against Mycobacterium tuberculosis thymidylate kinase. New insights into the phosphoryl transfer mechanism. Structure
- Fioravanti E et al. [2005]. The crystal structure of Mycobacterium tuberculosis thymidylate kinase in complex with 3'-azidodeoxythymidine monophosphate suggests a mechanism for competitive inhibition. Structure
- Kelkar DS et al. [2011]. Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Proteomics Sequence
- de Souza GA et al. [2011]. Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway. Proteomics
- Griffin JE et al. [2011]. High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism. Mutant
- 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