Gene Rv2773c
in Mycobacterium tuberculosis H37Rv
General annotation
Type | CDS |
Function | Involved in biosynthesis of diaminopimelate and lysine from aspartate semialdehyde (at the second step) [catalytic activity: 2,3,4,5-tetrahydrodipicolinate + NAD(P)(+) = 2,3-dihydrodipicolinate + NAD(P)H]. |
Product | Dihydrodipicolinate reductase DapB (DHPR) |
Comments | Rv2773c, (MTV002.38c), len: 245 aa. DapB, dihydrodipicolinate reductase (see Pavelka et al., 1997), highly similar to many e.g. P40110|DAPB_CORGL from Corynebacterium glutamicum (Brevibacterium flavum) (248 aa), FASTA scores: opt: 1030, E(): 1.8e-58, (65.45% identity in 246 aa overlap); O86836|DAPB_STRCO|SC9A10.03 from Streptomyces coelicolor (250 aa), FASTA scores: opt: 997, E(): 2.3e-56, (61.15% identity in 247 aa overlap); P42976|DAPB_BACSU from Bacillus subtilis (267 aa), FASTA scores: opt: 608, E(): 1.7e-31, (45.95% identity in 209 aa overlap); P46829|DAPB_MYCBO from Mycobacterium bovis (see Cirillo et al., 1994) (271 aa), FASTA scores: opt: 505, E(): 6.3e-25, (36.2% identity in 246 aa overlap); etc. Belongs to the dihydrodipicolinate reductase family. |
Functional category | Intermediary metabolism and respiration |
Proteomics | The product of this CDS corresponds to spot 3_296 identified in culture supernatant by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany (see proteomics citations). Identified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Identified in the culture supernatant of M. tuberculosis H37Rv using mass spectrometry (See Mattow et al., 2003). Detected by 2-DE and MS in M. tuberculosis H37Rv purified from phagosomes of infected murine bone marrow macrophages but not in H37Rv broth-cultures (See Mattow et al., 2006). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in M. tuberculosis H37Rv-infected guinea pig lungs at 30 days but not 90 days (See Kruh et al., 2010). Identified by mass spectrometry in the membrane protein fraction and whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate (See de Souza 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). Slow growth mutant by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). 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 | 3081604 | 3082341 | - |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2773c|dapB MRVGVLGAKGKVGATMVRAVAAADDLTLSAELDAGDPLSLLTDGNTEVVIDFTHPDVVMGNLEFLIDNGIHAVVGTTGFTAERFQQVESWLVAKPNTSVLIAPNFAIGAVLSMHFAKQAARFFDSAEVIELHHPHKADAPSGTAARTAKLIAEARKGLPPNPDATSTSLPGARGADVDGIPVHAVRLAGLVAHQEVLFGTEGETLTIRHDSLDRTSFVPGVLLAVRRIAERPGLTVGLEPLLDLH
Bibliography
- Cirillo JD et al. [1994]. Genetic determination of the meso-diaminopimelate biosynthetic pathway of mycobacteria. Homolog Sequence Product Biochemistry
- Pavelka MS et al. [1997]. Cloning of the dapB gene, encoding dihydrodipicolinate reductase, from Mycobacterium tuberculosis. Product Secondary
- Jungblut PR, Schaible UE, Mollenkopf HJ, Zimny-Arndt U, Raupach B, Mattow J, Halada P, Lamer S, Hagens K and Kaufmann SH [1999]. Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: towards functional genomics of microbial pathogens. Proteomics
- Mollenkopf HJ et al. [1999]. A dynamic two-dimensional polyacrylamide gel electrophoresis database: the mycobacterial proteome via Internet. Proteomics
- Gu S et al. [2003]. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Proteomics
- Sassetti CM et al. [2003]. Genes required for mycobacterial growth defined by high density mutagenesis. Mutant
- Mattow J, Schaible UE, Schmidt F, Hagens K, Siejak F, Brestrich G, Haeselbarth G, Muller EC, Jungblut PR and Kaufmann SH [2003]. Comparative proteome analysis of culture supernatant proteins from virulent Mycobacterium tuberculosis H37Rv and attenuated M. bovis BCG Copenhagen. Proteomics
- Cirilli M et al. [2003]. The three-dimensional structures of the Mycobacterium tuberculosis dihydrodipicolinate reductase-NADH-2,6-PDC and -NADPH-2,6-PDC complexes. Structural and mutagenic analysis of relaxed nucleotide specificity. Structure
- Mattow J, Siejak F, Hagens K, Becher D, Albrecht D, Krah A, Schmidt F, Jungblut PR, Kaufmann SH and Schaible UE [2006]. Proteins unique to intraphagosomally grown Mycobacterium tuberculosis. Proteomics
- Kruh NA et al. [2010]. Portrait of a pathogen: the Mycobacterium tuberculosis proteome in vivo. Proteomics
- MÃ¥len H et al. [2010]. Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv. Proteomics
- 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