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 01-MAY-2013, entry version 69.
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.
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1773;
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.,
RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the
RT complete 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
RT tuberculosis.";
RL BMC Microbiol. 10:50-50(2010).
CC -!- FUNCTION: Catalyzes the dephosphorylation of inositol 1-phosphate
CC (I-1-P) to yield free myo-inositol, a key metabolite in
CC mycobacteria (By similarity).
CC -!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol
CC + phosphate.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-
CC inositol from D-glucose 6-phosphate: step 2/2.
CC -!- INDUCTION: When comparing gene expression levels of the four
CC IMPase family genes in exponential cultures of M.tuberculosis, the
CC level of cysQ is the highest, almost equal to sigA; impA and impC
CC are expressed at approximately 40% of this level, while suhB is
CC lowest, at 12% of the cysQ level.
CC -!- DISRUPTION PHENOTYPE: Strains lacking this gene show no difference
CC in colony morphology and no differences in levels of
CC phosphatidylinosotol mannosides (PIMs), lipomannan (LM),
CC lipoarabinomannan (LAM) or mycothiol (in the absence of exogenous
CC inositol).
CC -!- SIMILARITY: Belongs to the inositol monophosphatase family.
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DR EMBL; BX842577; CAA17593.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP44368.1; -; Genomic_DNA.
DR PIR; C70819; C70819.
DR RefSeq; NP_216120.1; NC_000962.3.
DR RefSeq; YP_006514993.1; NC_018143.1.
DR ProteinModelPortal; O53907; -.
DR SMR; O53907; 28-257.
DR STRING; 83332.Rv1604; -.
DR PRIDE; O53907; -.
DR GeneID; 13316382; -.
DR GeneID; 885567; -.
DR KEGG; mtu:Rv1604; -.
DR KEGG; mtv:RVBD_1604; -.
DR PATRIC; 18152107; VBIMycTub87468_1786.
DR TubercuList; Rv1604; -.
DR eggNOG; COG0483; -.
DR HOGENOM; HOG000282238; -.
DR KO; K01092; -.
DR OMA; PGDFATE; -.
DR ProtClustDB; CLSK791276; -.
DR UniPathway; UPA00823; UER00788.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:EC.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA: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:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
DR InterPro; IPR000760; Inositol_monophosphatase.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR PANTHER; PTHR20854; PTHR20854; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR PROSITE; PS00629; IMP_1; FALSE_NEG.
DR PROSITE; PS00630; IMP_2; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1 270 Probable inositol 1-monophosphatase ImpA.
FT /FTId=PRO_0000404321.
FT REGION 87 90 Substrate binding (By similarity).
FT METAL 69 69 Magnesium 1 (By similarity).
FT METAL 85 85 Magnesium 1 (By similarity).
FT METAL 85 85 Magnesium 2 (By similarity).
FT METAL 87 87 Magnesium 1; via carbonyl oxygen (By
FT similarity).
FT METAL 88 88 Magnesium 2 (By similarity).
FT METAL 216 216 Magnesium 2 (By similarity).
FT BINDING 69 69 Substrate (By similarity).
FT BINDING 187 187 Substrate (By similarity).
FT BINDING 216 216 Substrate (By similarity).
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
//
