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virulence, detoxification, adaptation
information pathways
cell wall and cell processes
stable RNAs
insertion seqs and phages
PE/PPE
intermediary metabolism and respiration
unknown
regulatory proteins
conserved hypotheticals
lipid metabolism
pseudogenes
General annotation
TypeCDS
FunctionEnzyme that catalyse the reduction of disulphides by pyridine nucleotides through an enzyme disulphide and a flavin. Seems regulated by sigh (Rv3223c product). [catalytic activity: NADPH + oxidized thioredoxin = NADP(+) + reduced thioredoxin].
ProductProbable thioredoxin reductase TrxB2 (TRXR) (TR)
CommentsRv3913, (MT4032, MTV028.04), len: 335 aa. Probable trxB2, thioredoxin reductase (see citation below), equivalent to O30973|TRXB_MYCSM thioredoxin reductase from Mycobacterium smegmatis (311 aa), FASTA scores: opt: 1575, E(): 1.8e-87, (78.35% identity in 305 aa overlap); and highly similar, but shorter at C-terminus, to P46843|TRXB_MYCLE|TRXB/a|TRX|ML2703 bifunctional thioredoxin reductase/thioredoxin from Mycobacterium leprae (458 aa), FASTA scores: opt: 1766, E(): 8.7e-99, (83.25% identity in 328 aa overlap). Also highly similar to many e.g. P52215|TRXB_STRCO|SCH24.12 from Streptomyces coelicolor (321 aa), FASTA scores: opt: 1249, E(): 7.2e-68, (60.4% identity in 313 aa overlap); Q9Z8M4|TRXB_CHLPN from Chlamydia pneumoniae (Chlamydophila pneumoniae) (311 aa), FASTA scores: opt: 978, E(): 1.3e-51, (49.85% identity in 307 aa overlap); P09625|TRXB_ECOLI|B0888 from Escherichia coli strain K12 (320 aa), FASTA scores: opt: 948, E(): 8.6e-50, (49.2% identity in 309 aa overlap); etc. Contains PS00573 Pyridine nucleotide-disulphide oxidoreductases class-II active site. Belongs to the pyridine nucleotide-disulfide oxidoreductases class-II. Cofactor: FAD (by similarity).
Functional categoryIntermediary metabolism and respiration
ProteomicsIdentified by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany (See Jungblut et al., 1999). 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). Translational start site supported by proteomics data (See Kelkar et al., 2011).
TranscriptomicsmRNA identified by DNA microarray analysis and up-regulated at high temperatures (see Stewart et al., 2002). mRNA detected by RT-PCR in M. tuberculosis H37Rv under several in vitro growth conditions (oxidative stress and control) (See Akif et al., 2008).
MutantEssential 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 by Himar1 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
TypeStartEndOrientation
CDS44017284402735+
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3913|trxB2
MTAPPVHDRAHHPVRDVIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGALMTTTDVENYPGFRNGITGPELMDEMREQALRFGADLRMEDVESVSLHGPLKSVVTADGQTHRARAVILAMGAAARYLQVPGEQELLGRGVSSCATCDGFFFRDQDIAVIGGGDSAMEEATFLTRFARSVTLVHRRDEFRASKIMLDRARNNDKIRFLTNHTVVAVDGDTTVTGLRVRDTNTGAETTLPVTGVFVAIGHEPRSGLVREAIDVDPDGYVLVQGRTTSTSLPGVFAAGDLVDRTYRQAVTAAGSGCAAAIDAERWLAEHAATGEADSTDALIGAQR
      
Bibliography