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virulence, detoxification, adaptation
information pathways
cell wall and cell processes
stable RNAs
insertion seqs and phages
PE/PPE
intermediary metabolism and respiration
unknown
regulatory proteins
conserved hypotheticals
lipid metabolism
pseudogenes
General annotation
TypeCDS
FunctionInvolved in de novo purine biosynthesis (at the ninth and tenth steps) [catalytic activity 1: 10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide = tetrahydrofolate + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide] [catalytic activity 2: imp + H2O = 5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide].
ProductProbable bifunctional purine biosynthesis protein PurH: phosphoribosylaminoimidazolecarboxamide formyltransferase (AICAR transformylase) (5'-phosphoribosyl-5-aminoimidazole-4-carboxamide formyltransferase) + inosinemonophosphate cyclohydrolase (imp cyclohydrolase) (inosinicase) (imp synthetase) (ATIC)
CommentsRv0957, (MTCY10D7.17c), len: 523 aa. Probable purH, bifunctional purine biosynthesis protein including 5'-phosphoribosyl-5-aminoimidazole-4-carboxamide formyltransferase and inosine-monophosphate (imp) cyclohydrolase, equivalent to AL035500|MLCL373_8 putative phosphoribosylaminoimidazolecarboxamide formyltransferase from Mycobacterium leprae (527 aa), FASTA score: (88.1% identity in 520 aa overlap); and AF05727.1|AF191543_2|AF191543|PurH from Mycobacterium avium subsp. paratuberculosis (527 aa). Also highly similar to others e.g. CAB92677.1|AL356832 bifunctional purine biosynthesis protein from Streptomyces coelicolor (523 aa); NP_388534.1|NC_000964 phosphoribosylaminoimidazole carboxy formyl formyltransferase + inosine-monophosphate cyclohydrolase from Bacillus subtilis (512 aa); P15639|PUR9_ECOLI phosphoribosylaminoimidazolecarboxamide formyltransferase from Escherichia coli (529 aa), FASTA scores: opt: 1147, E(): 0, (44.8% identity in 533 aa overlap); etc. Belongs to the PurH family.
Functional categoryIntermediary metabolism and respiration
ProteomicsIdentified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Identified by mass spectrometry in M. tuberculosis H37Rv-infected guinea pig lungs at 90 days but not 30 days (See Kruh et al., 2010). Identified by mass spectrometry in the culture filtrate and whole cell lysates of M. tuberculosis H37Rv but not the membrane protein fraction (See de Souza et al., 2011).
MutantEssential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Essential 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
Coordinates
TypeStartEndOrientation
CDS10682051069776+
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv0957|purH
MSTDDGRRPIRRALISVYDKTGLVDLAQGLSAAGVEIISTGSTAKTIADTGIPVTPVEQLTGFPEVLDGRVKTLHPRVHAGLLADLRKSEHAAALEQLGIEAFELVVVNLYPFSQTVESGASVDDCVEQIDIGGPAMVRAAAKNHPSAAVVTDPLGYHGVLAALRAGGFTLAERKRLASLAFQHIAEYDIAVASWMQQTLAPEHPVAAFPQWFGRSWRRVAMLRYGENPHQQAALYGDPTAWPGLAQAEQLHGKDMSYNNFTDADAAWRAAFDHEQTCVAIIKHANPCGIAISSVSVADAHRKAHECDPLSAYGGVIAANTEVSVEMAEYVSTIFTEVIVAPGYAPGALDVLARKKNIRVLVAAEPLAGGSELRPISGGLLIQQSDQLDAHGDNPANWTLATGSPADPATLTDLVFAWRACRAVKSNAIVIAADGATVGVGMGQVNRVDAARLAVERGGERVRGAVAASDAFFPFPDGLETLAAAGVTAVVHPGGSVRDEEVTEAAAKAGVTLYLTGARHFAH