Possible triacylglycerol synthase (diacylglycerol acyltransferase); Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for storage lipid synthesis (By similarity).

Rv1323, (MTCY130.08), len: 389 aa. Probable fadA4,acetyl-CoA acetyltransferase, equivalent to THIL_MYCLE|P46707 possible acetyl-CoA C-acetyltransferase from Mycobacterium leprae (393 aa), FASTA scores: opt: 2218, E(): 0, (87.0% identity in 392 aa overlap). Also highly similar to others e.g. CAB70629.1|AL137242 probable acetoacetyl-CoA thiolase from Streptomyces coelicolor (401 aa); T51772 acetyl-CoA C-acetyltransferase [validated] from Alcaligenes latus (392 aa); etc. Some homologies indicate ATA start codon. Contains PS00098 Thiolases acyl-enzyme intermediate signature, PS00737 Thiola [...]

Possible triacylglycerol synthase (diacylglycerol acyltransferase); Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for storage lipid synthesis (By similarity).

Polyketide synthase Pks2; Catalyzes the synthesis of the hepta- and octamethyl phthioceranic acids and/or hydroxyphthioceranic acids that are the major acyl constituents of sulfolipids.

Possible triacylglycerol synthase (diacylglycerol acyltransferase); Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for storage lipid synthesis (By similarity).

Putative triacylglycerol synthase (diacylglycerol acyltransferase) Tgs4; Required for maintaining the appropriate mycolic acid composition and permeability of the envelope on its exposure to acidic pH. Upon expression in E.coli functions as a triacylglycerol synthase, making triacylglycerol (TG) from diolein and long-chain fatty acyl-CoA. Has very weak wax synthase activity, incorporating palmityl alcohol into wax esters in the presence of palmitoyl-CoA.

Probable bacterioferritin BfrA; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.

Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily.

Probable bacterioferritin BfrA; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.

Iron-dependent repressor and activator IdeR; Metal-dependent DNA-binding protein that controls transcription of many genes involved in iron metabolism. Acts as a repressor of siderophore biosynthesis and as a positive modulator of iron storage. Also regulates expression of transporters, proteins involved in siderophore synthesis, iron storage and transcriptional regulators.

Probable bacterioferritin BfrA; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.

Iron-regulated transporter IrtA; Part of the ABC transporter complex IrtAB involved in iron import. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation. Required for replication in human macrophages and in mouse lungs.

Probable bacterioferritin BfrA; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.

Bifunctional enzyme MbtA: salicyl-AMP ligase (SAL-AMP ligase) + salicyl-S-ArCP synthetase; Involved in the initial steps of the mycobactin biosynthetic pathway. Catalyzes the salicylation of the aryl carrier protein (ArCP) domain of MbtB through a two-step reaction. The first step is the ATP- dependent adenylation of salicylate to generate a salicyl-AMP intermediate. The second step is the transfer of this activated salicylate to MbtB to form a salicyl-ArCP domain thioester.

Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily.

Probable bacterioferritin BfrA; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.

Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily.

Iron-dependent repressor and activator IdeR; Metal-dependent DNA-binding protein that controls transcription of many genes involved in iron metabolism. Acts as a repressor of siderophore biosynthesis and as a positive modulator of iron storage. Also regulates expression of transporters, proteins involved in siderophore synthesis, iron storage and transcriptional regulators.

Bacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily.

Iron-regulated transporter IrtA; Part of the ABC transporter complex IrtAB involved in iron import. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation. Required for replication in human macrophages and in mouse lungs.

Probable metal cation-transporting P-type ATPase C CtpC; High affinity, slow turnover Mn(2+) transporting ATPase, which is required for virulence. Controls the Mn(2+) cytoplasmic quota and is involved in the uploading of Mn(2+) into secreted metalloproteins. Required for tolerance to Zn(2+) and oxidative stress. Plays a crucial role in the ability to resist zinc poisoning in human macrophages. Shows a preference for Mn(2+), but Zn(2+), Co(2+) and Cu(2+) can act as alternative substrates although at slower turnover rates ; Belongs to the cation transport ATPase (P-type) (TC 3.A.3) famil [...]

O-phosphoserine sulfhydrylase; Catalyzes the formation of a covalent CysO-cysteine adduct via a sulfur transfer, using the thiocarboxylated sulfur carrier protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as sulfur acceptor. Can also use sodium sulfide as sulfur donor in vitro, albeit with less efficiency, but not thiosulfate or thio-nitro- benzoate. O-acetylserine (OAS) is a very poor substrate in comparison with OPS. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis; Belongs to the cysteine synthase/cystathionine beta- sy [...]

Rv1285, (MTCY373.04), len: 332 aa. Probable cysD,sulfate adenylyltransferase subunit 2 (see Wooff et al.,2002), homology suggests start site at aa 24 or 28, similar to e.g. CYSD_ECOLI|P21156 sulfate adenylate transferase subunit 2 from Escherichia coli (302 aa), FASTA score: opt: 973, E():0, (52.5% identity in 303 aa overlap). Also similar to Mycobacterium tuberculosis Rv2392,3'-phosphoadenylylsulfate reductase. Belongs to the PAPS reductase family. CYSD subfamily. Thought to be differentially expressed within host cells (see Triccas et al., 1999).

O-phosphoserine sulfhydrylase; Catalyzes the formation of a covalent CysO-cysteine adduct via a sulfur transfer, using the thiocarboxylated sulfur carrier protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as sulfur acceptor. Can also use sodium sulfide as sulfur donor in vitro, albeit with less efficiency, but not thiosulfate or thio-nitro- benzoate. O-acetylserine (OAS) is a very poor substrate in comparison with OPS. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis; Belongs to the cysteine synthase/cystathionine beta- sy [...]

Rv1285, (MTCY373.04), len: 332 aa. Probable cysD,sulfate adenylyltransferase subunit 2 (see Wooff et al.,2002), homology suggests start site at aa 24 or 28, similar to e.g. CYSD_ECOLI|P21156 sulfate adenylate transferase subunit 2 from Escherichia coli (302 aa), FASTA score: opt: 973, E():0, (52.5% identity in 303 aa overlap). Also similar to Mycobacterium tuberculosis Rv2392,3'-phosphoadenylylsulfate reductase. Belongs to the PAPS reductase family. CYSD subfamily. Thought to be differentially expressed within host cells (see Triccas et al., 1999).

Sulfate adenylyltransferase subunit 1; ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity; In the C-terminal section; belongs to the APS kinase family.

O-phosphoserine sulfhydrylase; Catalyzes the formation of a covalent CysO-cysteine adduct via a sulfur transfer, using the thiocarboxylated sulfur carrier protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as sulfur acceptor. Can also use sodium sulfide as sulfur donor in vitro, albeit with less efficiency, but not thiosulfate or thio-nitro- benzoate. O-acetylserine (OAS) is a very poor substrate in comparison with OPS. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis; Belongs to the cysteine synthase/cystathionine beta- sy [...]

Probable metal cation-transporting P-type ATPase C CtpC; High affinity, slow turnover Mn(2+) transporting ATPase, which is required for virulence. Controls the Mn(2+) cytoplasmic quota and is involved in the uploading of Mn(2+) into secreted metalloproteins. Required for tolerance to Zn(2+) and oxidative stress. Plays a crucial role in the ability to resist zinc poisoning in human macrophages. Shows a preference for Mn(2+), but Zn(2+), Co(2+) and Cu(2+) can act as alternative substrates although at slower turnover rates ; Belongs to the cation transport ATPase (P-type) (TC 3.A.3) famil [...]

O-phosphoserine sulfhydrylase; Catalyzes the formation of a covalent CysO-cysteine adduct via a sulfur transfer, using the thiocarboxylated sulfur carrier protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as sulfur acceptor. Can also use sodium sulfide as sulfur donor in vitro, albeit with less efficiency, but not thiosulfate or thio-nitro- benzoate. O-acetylserine (OAS) is a very poor substrate in comparison with OPS. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis; Belongs to the cysteine synthase/cystathionine beta- sy [...]

Rv1285, (MTCY373.04), len: 332 aa. Probable cysD,sulfate adenylyltransferase subunit 2 (see Wooff et al.,2002), homology suggests start site at aa 24 or 28, similar to e.g. CYSD_ECOLI|P21156 sulfate adenylate transferase subunit 2 from Escherichia coli (302 aa), FASTA score: opt: 973, E():0, (52.5% identity in 303 aa overlap). Also similar to Mycobacterium tuberculosis Rv2392,3'-phosphoadenylylsulfate reductase. Belongs to the PAPS reductase family. CYSD subfamily. Thought to be differentially expressed within host cells (see Triccas et al., 1999).

O-phosphoserine sulfhydrylase; Catalyzes the formation of a covalent CysO-cysteine adduct via a sulfur transfer, using the thiocarboxylated sulfur carrier protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as sulfur acceptor. Can also use sodium sulfide as sulfur donor in vitro, albeit with less efficiency, but not thiosulfate or thio-nitro- benzoate. O-acetylserine (OAS) is a very poor substrate in comparison with OPS. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis; Belongs to the cysteine synthase/cystathionine beta- sy [...]

Sulfate adenylyltransferase subunit 1; ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity; In the C-terminal section; belongs to the APS kinase family.

Sulfate adenylyltransferase subunit 1; ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity; In the C-terminal section; belongs to the APS kinase family.

Rv1285, (MTCY373.04), len: 332 aa. Probable cysD,sulfate adenylyltransferase subunit 2 (see Wooff et al.,2002), homology suggests start site at aa 24 or 28, similar to e.g. CYSD_ECOLI|P21156 sulfate adenylate transferase subunit 2 from Escherichia coli (302 aa), FASTA score: opt: 973, E():0, (52.5% identity in 303 aa overlap). Also similar to Mycobacterium tuberculosis Rv2392,3'-phosphoadenylylsulfate reductase. Belongs to the PAPS reductase family. CYSD subfamily. Thought to be differentially expressed within host cells (see Triccas et al., 1999).

Sulfate adenylyltransferase subunit 1; ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity; In the C-terminal section; belongs to the APS kinase family.

O-phosphoserine sulfhydrylase; Catalyzes the formation of a covalent CysO-cysteine adduct via a sulfur transfer, using the thiocarboxylated sulfur carrier protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as sulfur acceptor. Can also use sodium sulfide as sulfur donor in vitro, albeit with less efficiency, but not thiosulfate or thio-nitro- benzoate. O-acetylserine (OAS) is a very poor substrate in comparison with OPS. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis; Belongs to the cysteine synthase/cystathionine beta- sy [...]

Sulfate adenylyltransferase subunit 1; ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity; In the C-terminal section; belongs to the APS kinase family.

Polyketide synthase Pks2; Catalyzes the synthesis of the hepta- and octamethyl phthioceranic acids and/or hydroxyphthioceranic acids that are the major acyl constituents of sulfolipids.

Two component transcriptional regulatory protein DevR (probably LuxR/UhpA-family); Member of the two-component regulatory system DevR/DevS (also called DosR/DosS) involved in onset of the dormancy response. Regulates an approximately 48-member regulon. When phosphorylated binds and activates the promoter of DevR regulon genes in response to hypoxia. The presence of target DNA increases stability of phospho-DevR in vitro. Activates its own transcription under hypoxic but not aerobic conditions, probably binds as a dimer to tandem binding sites within the devR and hspX promoters. Accepts [...]

Iron-dependent repressor and activator IdeR; Metal-dependent DNA-binding protein that controls transcription of many genes involved in iron metabolism. Acts as a repressor of siderophore biosynthesis and as a positive modulator of iron storage. Also regulates expression of transporters, proteins involved in siderophore synthesis, iron storage and transcriptional regulators.