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virulence, detoxification, adaptation
information pathways
cell wall and cell processes
stable RNAs
insertion seqs and phages
intermediary metabolism and respiration
regulatory proteins
conserved hypotheticals
lipid metabolism
General annotation
FunctionNecessary for the biosynthesis of purines, thymydylate, methionine, histidine, pantothenate, and formyl tRNA-met [catalytic activity: 5,10-methylenetetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH] [catalytic activity: 5,10-methenyltetrahydrofolate + H(2)O = 10-formyltetrahydrofolate].
ProductProbable bifunctional protein FolD: methylenetetrahydrofolate dehydrogenase + methenyltetrahydrofolate cyclohydrolase
CommentsRv3356c, (MTV004.13c), len: 281 aa. Probable folD, bifunctional enzyme include methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase , equivalent to O32879|fold|ML0674 methylenetetrahydrofolate dehydrogenase (putative methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase) from Mycobacterium leprae (282 aa), FASTA scores: opt: 1624, E(): 1.2e-93, (86.45% identity in 281 aa overlap). Also similar to many others e.g. Q9K3J6|fold from Streptomyces coelicolor (284 aa), FASTA scores: opt: 1223, E(): 9.5e-69, (66.65% identity in 279 aa overlap); Q9K966|fold from Bacillus halodurans (279 aa), FASTA scores: opt: 886, E(): 7.7e-48, (47.15% identity in 280 aa overlap); P54382|FOLD_BACSU from Bacillus subtilis (283 aa), FASTA scores: opt: 820, E(): 9.7e-44, (45.7% identity in 280 aa overlap); P51696|FOLD_PHOPO from Photobacterium phosphoreum (285 aa), FASTA scores: opt: 778, E(): 4e-41, (44.9% identity in 283 aa overlap); P24186|FOLD_ECOLI|ads|B0529 from Escherichia coli (287 aa), FASTA scores: opt: 741, E(): 0,44.4, (44.4% identity in 277 aa overlap); etc. Also highly similar to MLCB1779_9 from Mycobacterium leprae cosmid B1779 (282 aa) (86.5% identity in 281 aa overlap). Similar to other dehydrogenase/cyclohydrolase enzymes or domains.
Functional categoryIntermediary metabolism and respiration
ProteomicsIdentified by proteomics at the Statens Serum Institute (Denmark) (See Rosenkrands et al., 2000). Identified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Identified in culture filtrates of M. tuberculosis H37Rv (See Malen et al., 2007). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in the culture filtrate, membrane protein fraction, and whole cell lysates of M. tuberculosis H37Rv (See de Souza et al., 2011). Translational start site supported by proteomics data (See de Souza et al., 2011).
MutantEssential 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
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3356c|folD