Thioredoxin TrxC (TRX) (MPT46); Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.

Probable ATP-dependent helicase DinG; Probable helicase involved in DNA repair and perhaps also replication; Belongs to the helicase family. DinG subfamily.

Rv1471, (MTV007.18), len: 123 aa. Probable trxB1,thioredoxin, similar to many bacterial thioredoxins e.g. P33636|THI2_ECOLI from Escherichia coli (139 aa), FASTA scores: opt: 290, E(): 1.8e-13, (44.3% identity in 97 aa overlap); etc. Highly similar to Rv1470|TrxA probable thioredoxin from Mycobacterium tuberculosis (124 aa), FASTA scores: opt: 402, E(): 1.2e-32, (54.4% identity in 114 aa overlap). Contains PS00194 Thioredoxin family active site. Belongs to the thioredoxin family. Note that previously known as trxB.

Alkyl hydroperoxide reductase C protein AhpC (alkyl hydroperoxidase C); Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Together with AhpD, DlaT and Lpd, constitutes an NADH-dependent peroxidase active against hydrogen and alkyl peroxides as well as serving as a peroxynitrite reductase, thus protecting the bacterium against reactive nitrogen intermediates and oxidative stress generated by the host immune system. D [...]

Rv3913, (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 [...]

Rv1470, (MTV007.17), len: 124 aa. Probable trxA,thioredoxin, similar to many e.g. P12243|THI1_SYNP7 thioredoxin 1 from Synechococcus sp. (106 aa), FASTA scores: opt: 201, E(): 9.2e-08, (35.4% identity in 99 aa overlap); etc. Highly similar to downstream ORF Rv1471|trxB1 probable thioredoxin from Mycobacterium tuberculosis (123 aa), FASTA scores: opt: 402, E(): 0,(54.4% identity in 114 aa overlap). Warning: note that Rv3914|MT4033|MTV028.05|trxC can be alternatively named trxA.

Possible thioredoxin; Rv1324, (MTCY130.09), len: 304 aa. Possible thioredoxin, similar to several e.g. U00014|Q49716 TRXA from Mycobacterium leprae (255 aa), FASTA scores: opt: 1014, E(): 0, (69.7% identity in 228 aa overlap); THIO_RHOSH|P08058 TrxA from Rhodobacter sphaeroides (105 aa), FASTA scores: opt 196, E(): 1.9e-06, (33.0% identity in 103 aa overlap). Contains PS00339 Aminoacyl-transfer RNA synthetases class-II signature 2. A core mycobacterial gene; conserved in mycobacterial strains (See Marmiesse et al., 2004).

Probable Mrp-related protein Mrp; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; In the C-terminal section; belongs to the Mrp/NBP35 ATP- binding proteins family.

Prephenate dehydrogenase TyrA (PDH) (hydroxyphenylpyruvate synthase); Catalyzes the NAD(+)-dependent conversion of prephenate to p- hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E.coli and some other bacteria, that are bifunctional and possess a CM domain.