IMPA_MYCTU
ID IMPA_MYCTU Reviewed; 270 AA.
AC O53907; L0TA49;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Probable inositol 1-monophosphatase ImpA;
DE Short=I-1-Pase;
DE Short=IMPase;
DE Short=Inositol-1-phosphatase;
DE EC=3.1.3.25;
GN Name=impA; OrderedLocusNames=Rv1604;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20167072; DOI=10.1186/1471-2180-10-50;
RA Movahedzadeh F., Wheeler P.R., Dinadayala P., Av-Gay Y., Parish T.,
RA Daffe M., Stoker N.G.;
RT "Inositol monophosphate phosphatase genes of Mycobacterium tuberculosis.";
RL BMC Microbiol. 10:50-50(2010).
CC -!- FUNCTION: Catalyzes the dephosphorylation of inositol 1-phosphate (I-1-
CC P) to yield free myo-inositol, a key metabolite in mycobacteria.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 2/2.
CC -!- INDUCTION: When comparing gene expression levels of the four IMPase
CC family genes in exponential cultures of M.tuberculosis, the level of
CC cysQ is the highest, almost equal to sigA; impA and impC are expressed
CC at approximately 40% of this level, while suhB is lowest, at 12% of the
CC cysQ level. {ECO:0000269|PubMed:20167072}.
CC -!- DISRUPTION PHENOTYPE: Strains lacking this gene show no difference in
CC colony morphology and no differences in levels of phosphatidylinosotol
CC mannosides (PIMs), lipomannan (LM), lipoarabinomannan (LAM) or
CC mycothiol (in the absence of exogenous inositol).
CC {ECO:0000269|PubMed:20167072}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44368.1; -; Genomic_DNA.
DR PIR; C70819; C70819.
DR RefSeq; NP_216120.1; NC_000962.3.
DR RefSeq; WP_003911572.1; NZ_NVQJ01000016.1.
DR AlphaFoldDB; O53907; -.
DR SMR; O53907; -.
DR STRING; 83332.Rv1604; -.
DR PaxDb; O53907; -.
DR DNASU; 885567; -.
DR GeneID; 885567; -.
DR KEGG; mtu:Rv1604; -.
DR TubercuList; Rv1604; -.
DR eggNOG; COG0483; Bacteria.
DR InParanoid; O53907; -.
DR OMA; PWVWVLD; -.
DR PhylomeDB; O53907; -.
DR UniPathway; UPA00823; UER00788.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IBA:GO_Central.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR PROSITE; PS00630; IMP_2; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..270
FT /note="Probable inositol 1-monophosphatase ImpA"
FT /id="PRO_0000404321"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 87..90
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 270 AA; 27979 MW; D86E14851E4DC8CD CRC64;
MHLDSLVAPL VEQASAILDA ATALFLVGHR ADSAVRKKGN DFATEVDLAI ERQVVAALVA
ATGIEVHGEE FGGPAVDSRW VWVLDPIDGT INYAAGSPLA AILLGLLHDG VPVAGLTWMP
FTDPRYTAVA GGPLIKNGVP QPPLADAELA NVLVGVGTFS ADSRGQFPGR YRLAVLEKLS
RVSSRLRMHG STGIDLVFVA DGILGGAISF GGHVWDHAAG VALVRAAGGV VTDLAGQPWT
PASRSALAGP PRVHAQILEI LGSIGEPEDY
