Gene Rv2780
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | May play a role in cell wall synthesis as L-alanine is an important constituent of the peptidoglycan layer [catalytic activity: L-alanine + H(2)O + NAD(+) = pyruvate + NH(3) + NADH]. |
| Product | Secreted L-alanine dehydrogenase Ald (40 kDa antigen) (TB43) |
| Comments | Rv2780, (MT2850, MTV002.45), len: 371 aa. Ald, secreted L-alanine dehydrogenase (40 kd antigen); equivalent to Q9CBV6|ALD|ML1532 L-alanine dehydrogenase from Mycobacterium leprae (371 aa), FASTA scores: opt: 2081, E(): 4e-115, (85.45% identity in 371 aa overlap). Also highly similar to others e.g. Q9S227|SCI51.13c from Streptomyces coelicolor (371 aa), FASTA scores: opt: 1575, E(): 2.3e-85, (66.05% identity in 371 aa overlap); Q9K827|BH3180 from Bacillus halodurans (371 aa), FASTA scores: opt: 1341, E(): 1.4e-71, (56.45% identity in 372 aa overlap); Q9RT70|DR1895 from Deinococcus radiodurans (390 aa), FASTA scores: opt: 1319, E(): 2.8e-70, (54.2% identity in 371 aa overlap); etc. Contains PS00836 and PS00837 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 1 and 2. Predicted possible vaccine candidate (See Zvi et al., 2008). |
| Functional category | Intermediary metabolism and respiration |
| Proteomics | The product of this CDS corresponds to spots 1_298 and 1_321 identified in culture supernatant by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany (see Jungblut et al., 1999; Mollenkopf et al., 1999; Mattow et al., 2001), and spots 2780 identified in short term culture filtrate and cell wall by proteomics at the Statens Serum Institute (Denmark) (see Rosenkrands et al., 2000a; 2000b). Also identified at the Statens Serum Institute (Denmark) under aerobic and low oxygen conditions (see Rosenkrands et al., 2002). 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 and Edman degradation (See Mattow et al., 2003). Identified in the cytosol of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified by mass spectrometry in the culture filtrate and whole cell lysates of M. tuberculosis H37Rv but not the membrane protein fraction (See de Souza et al., 2011). |
| Transcriptomics | mRNA identified by microarray analysis and up-regulated after 24h and 96h of starvation (see Betts et al., 2002). |
| 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). Non essential gene by Himar1 transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Non-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 | 3086820 | 3087935 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv2780|ald
MRVGIPTETKNNEFRVAITPAGVAELTRRGHEVLIQAGAGEGSAITDADFKAAGAQLVGTADQVWADADLLLKVKEPIAAEYGRLRHGQILFTFLHLAASRACTDALLDSGTTSIAYETVQTADGALPLLAPMSEVAGRLAAQVGAYHLMRTQGGRGVLMGGVPGVEPADVVVIGAGTAGYNAARIANGMGATVTVLDINIDKLRQLDAEFCGRIHTRYSSAYELEGAVKRADLVIGAVLVPGAKAPKLVSNSLVAHMKPGAVLVDIAIDQGGCFEGSRPTTYDHPTFAVHDTLFYCVANMPASVPKTSTYALTNATMPYVLELADHGWRAACRSNPALAKGLSTHEGALLSERVATDLGVPFTEPASVLA
Bibliography
- Andersen AB et al. [1992]. Structure and function of a 40,000-molecular-weight protein antigen of Mycobacterium tuberculosis. Sequence Product Function
- Hutter B et al. [1998]. Host vector system for high-level expression and purification of recombinant, enzymatically active alanine dehydrogenase of Mycobacterium tuberculosis. Product Biochemistry
- 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
- Hutter B et al. [1999]. Properties of the 40 kDa antigen of Mycobacterium tuberculosis, a functional L-alanine dehydrogenase. Phylogeny Biochemistry Function
- Mollenkopf HJ et al. [1999]. A dynamic two-dimensional polyacrylamide gel electrophoresis database: the mycobacterial proteome via Internet. Proteomics
- Rosenkrands I et al. [2000]. Towards the proteome of Mycobacterium tuberculosis. Proteomics
- Rosenkrands I, Weldingh K, Jacobsen S, Hansen CV, Florio W, Gianetri I and Andersen P [2000]. Mapping and identification of Mycobacterium tuberculosis proteins by two-dimensional gel electrophoresis, microsequencing and immunodetection. Proteomics
- Mattow J, Jungblut PR, Schaible UE, Mollenkopf HJ, Lamer S, Zimny-Arndt U, Hagens K, Muller EC and Kaufmann SH [2001]. Identification of proteins from Mycobacterium tuberculosis missing in attenuated Mycobacterium bovis BCG strains. Proteomics
- Rosenkrands I et al. [2002]. Hypoxic response of Mycobacterium tuberculosis studied by metabolic labeling and proteome analysis of cellular and extracellular proteins. Proteomics Regulation
- Betts JC et al. [2002]. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Transcriptome
- 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
- Sassetti CM et al. [2003]. Genes required for mycobacterial growth defined by high density mutagenesis. Mutant
- Gu S et al. [2003]. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Proteomics
- Mawuenyega KG et al. [2005]. Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Proteomics
- Agren D et al. [2008]. Three-dimensional structures of apo- and holo-L-alanine dehydrogenase from Mycobacterium tuberculosis reveal conformational changes upon coenzyme binding. Structure
- Tripathi SM et al. [2008]. Crystal structures of the Mycobacterium tuberculosis secretory antigen alanine dehydrogenase (Rv2780) in apo and ternary complex forms captures "open" and "closed" enzyme conformations. Structure
- Zvi A et al. [2008]. Whole genome identification of Mycobacterium tuberculosis vaccine candidates by comprehensive data mining and bioinformatic analyses. Immunology
- Griffin JE et al. [2011]. High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism. Mutant
- de Souza GA et al. [2011]. Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway. Proteomics
- 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
