Ferredoxin sulfite reductase; Identified by match to protein family HMM PF01077; match to protein family HMM PF03460; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

UDP-N-acetylglucosamine pyrophosphorylase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belongs to the transferase hexapeptide repeat family.

Pyridoxamine 5'-phosphate oxidase family protein; Identified by match to protein family HMM PF01243.

F420-dependent glucose-6-phosphate dehydrogenase; Catalyzes the coenzyme F420-dependent oxidation of glucose 6- phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in resistance to oxidative stress, via its consumption of G6P that serves as a source of reducing power to combat oxidative stress in mycobacteria. Cannot use NAD, NADP, FAD or FMN instead of coenzyme F420 as an electron acceptor. Exhibits nearly no activity with D-mannose-6- phosphate or D-fructose-6-phosphate as substrate. Belongs to the F420-dependent glucose-6-phosphate dehydrogenase family.

Pyridoxamine 5'-phosphate oxidase family protein; Identified by match to protein family HMM PF01243.

FAD binding domain, putative; Catalyzes the reduction of a single double bond in the isoprenoid tail of menaquinone (MK-9) in M.smegmatis, likely the beta- isoprene unit, forming the predominant form of menaquinone found in mycobacteria, MK-9(II-H2).

Lppg:fo 2-phospho-l-lactate transferase; Catalyzes the transfer of the phosphoenolpyruvate moiety from enoylpyruvoyl-2-diphospho-5'-guanosine (EPPG) to 7,8-didemethyl-8- hydroxy-5-deazariboflavin (FO) with the formation of dehydro coenzyme F420-0 and GMP.

F420-0:gamma-glutamyl ligase; Bifunctional enzyme that catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L- lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2- dependent reduction of dehydro-F420-0 to form F420-0. Is able to add up to six glutamates to F420-0, producing F420-3 as the major product with lesser amount of F420-4,5,6, consistent with it producing the polyglutamated F420 compounds present in Mycobacterium smegmatis. In the N-terminal section; belong [...]

Lppg:fo 2-phospho-l-lactate transferase; Catalyzes the transfer of the phosphoenolpyruvate moiety from enoylpyruvoyl-2-diphospho-5'-guanosine (EPPG) to 7,8-didemethyl-8- hydroxy-5-deazariboflavin (FO) with the formation of dehydro coenzyme F420-0 and GMP.

F420-dependent glucose-6-phosphate dehydrogenase; Catalyzes the coenzyme F420-dependent oxidation of glucose 6- phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in resistance to oxidative stress, via its consumption of G6P that serves as a source of reducing power to combat oxidative stress in mycobacteria. Cannot use NAD, NADP, FAD or FMN instead of coenzyme F420 as an electron acceptor. Exhibits nearly no activity with D-mannose-6- phosphate or D-fructose-6-phosphate as substrate. Belongs to the F420-dependent glucose-6-phosphate dehydrogenase family.

F420-0:gamma-glutamyl ligase; Bifunctional enzyme that catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L- lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2- dependent reduction of dehydro-F420-0 to form F420-0. Is able to add up to six glutamates to F420-0, producing F420-3 as the major product with lesser amount of F420-4,5,6, consistent with it producing the polyglutamated F420 compounds present in Mycobacterium smegmatis. In the N-terminal section; belong [...]

Lppg:fo 2-phospho-l-lactate transferase; Catalyzes the transfer of the phosphoenolpyruvate moiety from enoylpyruvoyl-2-diphospho-5'-guanosine (EPPG) to 7,8-didemethyl-8- hydroxy-5-deazariboflavin (FO) with the formation of dehydro coenzyme F420-0 and GMP.

F420-0:gamma-glutamyl ligase; Bifunctional enzyme that catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L- lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2- dependent reduction of dehydro-F420-0 to form F420-0. Is able to add up to six glutamates to F420-0, producing F420-3 as the major product with lesser amount of F420-4,5,6, consistent with it producing the polyglutamated F420 compounds present in Mycobacterium smegmatis. In the N-terminal section; belong [...]

F420-dependent glucose-6-phosphate dehydrogenase; Catalyzes the coenzyme F420-dependent oxidation of glucose 6- phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in resistance to oxidative stress, via its consumption of G6P that serves as a source of reducing power to combat oxidative stress in mycobacteria. Cannot use NAD, NADP, FAD or FMN instead of coenzyme F420 as an electron acceptor. Exhibits nearly no activity with D-mannose-6- phosphate or D-fructose-6-phosphate as substrate. Belongs to the F420-dependent glucose-6-phosphate dehydrogenase family.

F420-dependent glucose-6-phosphate dehydrogenase; Catalyzes the coenzyme F420-dependent oxidation of glucose 6- phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in resistance to oxidative stress, via its consumption of G6P that serves as a source of reducing power to combat oxidative stress in mycobacteria. Cannot use NAD, NADP, FAD or FMN instead of coenzyme F420 as an electron acceptor. Exhibits nearly no activity with D-mannose-6- phosphate or D-fructose-6-phosphate as substrate. Belongs to the F420-dependent glucose-6-phosphate dehydrogenase family.

Pyridoxamine 5'-phosphate oxidase family protein; Identified by match to protein family HMM PF01243.

F420-dependent glucose-6-phosphate dehydrogenase; Catalyzes the coenzyme F420-dependent oxidation of glucose 6- phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in resistance to oxidative stress, via its consumption of G6P that serves as a source of reducing power to combat oxidative stress in mycobacteria. Cannot use NAD, NADP, FAD or FMN instead of coenzyme F420 as an electron acceptor. Exhibits nearly no activity with D-mannose-6- phosphate or D-fructose-6-phosphate as substrate. Belongs to the F420-dependent glucose-6-phosphate dehydrogenase family.

Lppg:fo 2-phospho-l-lactate transferase; Catalyzes the transfer of the phosphoenolpyruvate moiety from enoylpyruvoyl-2-diphospho-5'-guanosine (EPPG) to 7,8-didemethyl-8- hydroxy-5-deazariboflavin (FO) with the formation of dehydro coenzyme F420-0 and GMP.

F420-dependent glucose-6-phosphate dehydrogenase; Catalyzes the coenzyme F420-dependent oxidation of glucose 6- phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in resistance to oxidative stress, via its consumption of G6P that serves as a source of reducing power to combat oxidative stress in mycobacteria. Cannot use NAD, NADP, FAD or FMN instead of coenzyme F420 as an electron acceptor. Exhibits nearly no activity with D-mannose-6- phosphate or D-fructose-6-phosphate as substrate. Belongs to the F420-dependent glucose-6-phosphate dehydrogenase family.

F420-0:gamma-glutamyl ligase; Bifunctional enzyme that catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L- lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2- dependent reduction of dehydro-F420-0 to form F420-0. Is able to add up to six glutamates to F420-0, producing F420-3 as the major product with lesser amount of F420-4,5,6, consistent with it producing the polyglutamated F420 compounds present in Mycobacterium smegmatis. In the N-terminal section; belong [...]

F420-dependent glucose-6-phosphate dehydrogenase; Catalyzes the coenzyme F420-dependent oxidation of glucose 6- phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in resistance to oxidative stress, via its consumption of G6P that serves as a source of reducing power to combat oxidative stress in mycobacteria. Cannot use NAD, NADP, FAD or FMN instead of coenzyme F420 as an electron acceptor. Exhibits nearly no activity with D-mannose-6- phosphate or D-fructose-6-phosphate as substrate. Belongs to the F420-dependent glucose-6-phosphate dehydrogenase family.

Triosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family.

UDP-N-acetylglucosamine pyrophosphorylase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belongs to the transferase hexapeptide repeat family.

Ferredoxin sulfite reductase; Identified by match to protein family HMM PF01077; match to protein family HMM PF03460; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

UDP-N-acetylglucosamine pyrophosphorylase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belongs to the transferase hexapeptide repeat family.

UDP-N-acetylmuramoylalanine--D-glutamate ligase; Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). Belongs to the MurCDEF family.

FAD binding domain, putative; Catalyzes the reduction of a single double bond in the isoprenoid tail of menaquinone (MK-9) in M.smegmatis, likely the beta- isoprene unit, forming the predominant form of menaquinone found in mycobacteria, MK-9(II-H2).

Pyridoxamine 5'-phosphate oxidase family protein; Identified by match to protein family HMM PF01243.

UDP-N-acetylmuramoylalanine--D-glutamate ligase; Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). Belongs to the MurCDEF family.

UDP-N-acetylglucosamine pyrophosphorylase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belongs to the transferase hexapeptide repeat family.

Triosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family.

F420-dependent glucose-6-phosphate dehydrogenase; Catalyzes the coenzyme F420-dependent oxidation of glucose 6- phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in resistance to oxidative stress, via its consumption of G6P that serves as a source of reducing power to combat oxidative stress in mycobacteria. Cannot use NAD, NADP, FAD or FMN instead of coenzyme F420 as an electron acceptor. Exhibits nearly no activity with D-mannose-6- phosphate or D-fructose-6-phosphate as substrate. Belongs to the F420-dependent glucose-6-phosphate dehydrogenase family.