Gene Rv3565
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Thought to be involved in glutamate biosynthesis [catalytic activity: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate]. |
| Product | Possible aspartate aminotransferase AspB (transaminase A) (ASPAT) (glutamic--oxaloacetic transaminase) (glutamic--aspartic transaminase) |
| Comments | Rv3565, (MTCY06G11.12), len: 388 aa. Possible aspB, aspartate aminotransferase, similar to many e.g. Q9A5J2|CC2455 aminotransferase class I from Caulobacter crescentus (381 aa), FASTA scores: opt: 1112, E(): 1e-61, (45.85% identity in 384 aa overlap); Q9HV76|PA4722 probable aminotransferase from Pseudomonas aeruginosa (390 aa), FASTA scores: opt: 863, E(): 3.1e-46, (37.2% identity in 390 aa overlap); Q9RWP3|DR0623 aspartate aminotransferase from Deinococcus radiodurans (388 aa), FASTA scores: opt: 713, E(): 6.3e-37, (35.5% identity in 383 aa overlap); Q9HQK2|ASPC2|VNG1121G aspartate aminotransferase from Halobacterium sp. strain NRC-1 (391 aa), FASTA scores: opt: 710, E(): 9.8e-37, (34.45% identity in 380 aa overlap); O33822|AAT_THEAQ|ASPC aspartate aminotransferase from Thermus aquaticus (383 aa), FASTA scores: opt: 695, E(): 8.2e-36, (35.1% identity in 376 aa overlap); etc. Contains PS00105 Aminotransferases class-I pyridoxal-phosphate attachment site. Belongs to class-I of pyridoxal-phosphate-dependent aminotransferases. Cofactor: pyridoxal phosphate (by similarity). |
| Functional category | Intermediary metabolism and respiration |
| Proteomics | Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen 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). |
| Transcriptomics | mRNA identified by microarray analysis; transcription repressed at low pH in vitro conditions, which may mimic an environmental signal encountered by phagocytosed bacteria (see citation below). |
| Mutant | Non-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 | 4006200 | 4007366 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3565|aspB
VTDRVALRAGVPPFYVMDVWLAAAERQRTHGDLVNLSAGQPSAGAPEPVRAAAAAALHLNQLGYSVALGIPELRDAIAADYQRRHGITVEPDAVVITTGSSGGFLLAFLACFDAGDRVAMASPGYPCYRNILSALGCEVVEIPCGPQTRFQPTAQMLAEIDPPLRGVVVASPANPTGTVIPPEELAAIASWCDASDVRLISDEVYHGLVYQGAPQTSCAWQTSRNAVVVNSFSKYYAMTGWRLGWLLVPTVLRRAVDCLTGNFTICPPVLSQIAAVSAFTPEATAEADGNLASYAINRSLLLDGLRRIGIDRLAPTDGAFYVYADVSDFTSDSLAFCSKLLADTGVAIAPGIDFDTARGGSFVRISFAGPSGDIEEALRRIGSWLPSQ
Bibliography
- Fisher MA, Plikaytis BB and Shinnick TM [2002]. Microarray analysis of the Mycobacterium tuberculosis transcriptional response to the acidic conditions found in phagosomes. Transcriptome Regulation
- Målen 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
