Rv2386c - isochorismate synthase mbtI
Protein Domains

Gene Information
LocusRv2386c
SymbolmbtI
Gene Nameisochorismate synthase mbtI
Location2678653 - 2680005 (-)
SpeciesMycobacterium tuberculosis H37Rv complete genome.
LengthGene:1353 bp
Protein:451 aa
External LinksTuberculist
Target Gene Information
String Protein-Protein Interactions
STITCH Chemical-Protein Interactions
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Orthologs
Orthogroup Number31355
Related GenesMAP2205c MAV_1792 MSMEG_4524 MT2454 MUL_3648 nfa6190
Transcriptional Regulation
Operons View gene in operon browser
Regulatory Network
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Expression Correlation Genes with Correlated Expression
Scatterplot of Gene Expression

Sequence
Proteins
Genomic Sequence
Community Annotations Pending Curatorial Review
FieldValueStatusCreatorDate
TermTBRXN:SALCS salicylate synthase - IPIactivenjamshidi2012-10-05
This step is needed for the biosynthesis of mycoabctin which is needed for Fe acquisition. Stoichiometry and reaction are inferred - no solid evidence for it yet. see PMID: 9831524, 10419938, 12657046
authors,CM. Sassetti,DH. Boyd,EJ. Rubin Genes required for mycobacterial growth defined by high density mutagenesis. Mol. Microbiol. 2003
TermTBRXN:SALCS salicylate synthase - IPIactivenjamshidi2012-10-05
This step is needed for the biosynthesis of mycoabctin which is needed for Fe acquisition. Stoichiometry and reaction are inferred - no solid evidence for it yet. see PMID: 9831524, 10419938, 12657046
authors,JJ. De Voss,K. Rutter,BG. Schroeder,CE. Barry Iron acquisition and metabolism by mycobacteria. J. Bacteriol. 1999
TermTBRXN:SALCS salicylate synthase - IPIactivenjamshidi2012-10-05
This step is needed for the biosynthesis of mycoabctin which is needed for Fe acquisition. Stoichiometry and reaction are inferred - no solid evidence for it yet. see PMID: 9831524, 10419938, 12657046
LE. Quadri, J. Sello et al. Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin. Chem. Biol. 1998
InteractionRegulatory Rv2711activepriyadarshinipriyanka20012012-10-05
Co-expression (Functional linkage)
LE. Quadri, J. Sello et al. Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin. Chem. Biol. 1998
InteractionRegulatory Rv2711activepriyadarshinipriyanka20012012-10-05
Co-expression (Functional linkage)
authors,JJ. De Voss,K. Rutter,BG. Schroeder,CE. Barry Iron acquisition and metabolism by mycobacteria. J. Bacteriol. 1999
InteractionRegulatory Rv2711activepriyadarshinipriyanka20012012-10-05
Co-expression (Functional linkage)
GM. Rodriguez, MI. Voskuil et al. ideR, An essential gene in mycobacterium tuberculosis: role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response. Infect. Immun. 2002
InteractionRegulatedBy Rv2711activeyamir.moreno2012-10-05
Literature previously reported link (from Balazsi et al. 2008). Traceable author statement to experimental support.
G. Balázsi, AP. Heath et al. The temporal response of the Mycobacterium tuberculosis gene regulatory network during growth arrest. Mol. Syst. Biol. 2008
OtherEC:4.2.99.21activeextern:JZUCKER2012-03-06
Assay of protein purified to homogeneity from its native host
AJ. Harrison, M. Yu et al. The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase. J. Bacteriol. 2006
TermEC:4.1.3.27 Anthranilate synthase. - NRactiveextern:JZUCKER2012-03-06
Assay of protein purified to homogeneity from its native host
AJ. Harrison, M. Yu et al. The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase. J. Bacteriol. 2006
TermEC:5.4.4.2 Isochorismate synthase. - NRactiveextern:JZUCKER2012-03-06
Assay of protein purified to homogeneity from its native host
AJ. Harrison, M. Yu et al. The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase. J. Bacteriol. 2006