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virulence, detoxification, adaptation
information pathways
cell wall and cell processes
stable RNAs
insertion seqs and phages
intermediary metabolism and respiration
regulatory proteins
conserved hypotheticals
lipid metabolism
General annotation
FunctionThought to be involved in glutamate biosynthesis [catalytic activity: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate].
ProductPossible aspartate aminotransferase AspB (transaminase A) (ASPAT) (glutamic--oxaloacetic transaminase) (glutamic--aspartic transaminase)
CommentsRv3565, (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 categoryIntermediary metabolism and respiration
ProteomicsIdentified 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).
TranscriptomicsmRNA 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).
MutantNon-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
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3565|aspB