IMPA_MYCS2
ID IMPA_MYCS2 Reviewed; 276 AA.
AC A0QX86; I7G1F6; O51845; Q79BH3;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=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=MSMEG_3210, MSMEI_3128;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN INOSITOL BIOSYNTHESIS, GENE
RP NAME, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=9401044; DOI=10.1128/jb.179.24.7827-7833.1997;
RA Parish T., Liu J., Nikaido H., Stoker N.G.;
RT "A Mycobacterium smegmatis mutant with a defective inositol monophosphate
RT phosphatase gene homolog has altered cell envelope permeability.";
RL J. Bacteriol. 179:7827-7833(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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:0000305|PubMed:9401044}.
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. {ECO:0000269|PubMed:9401044}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of this gene results in an altered
CC colony morphology, reduced levels of PI dimannoside (PIM2), and altered
CC permeability of the cell wall. {ECO:0000269|PubMed:9401044}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; AF005905; AAB94817.1; -; Genomic_DNA.
DR EMBL; U77950; AAB94795.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK70281.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39592.1; -; Genomic_DNA.
DR RefSeq; WP_003894599.1; NZ_SIJM01000015.1.
DR RefSeq; YP_887524.1; NC_008596.1.
DR AlphaFoldDB; A0QX86; -.
DR SMR; A0QX86; -.
DR STRING; 246196.MSMEI_3128; -.
DR EnsemblBacteria; ABK70281; ABK70281; MSMEG_3210.
DR EnsemblBacteria; AFP39592; AFP39592; MSMEI_3128.
DR GeneID; 66734610; -.
DR KEGG; msg:MSMEI_3128; -.
DR KEGG; msm:MSMEG_3210; -.
DR PATRIC; fig|246196.19.peg.3172; -.
DR eggNOG; COG0483; Bacteria.
DR OMA; PWVWVLD; -.
DR OrthoDB; 1741160at2; -.
DR BRENDA; 3.1.3.11; 3512.
DR BRENDA; 3.1.3.25; 3512.
DR UniPathway; UPA00823; UER00788.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IMP:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
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 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..276
FT /note="Inositol-1-monophosphatase ImpA"
FT /id="PRO_0000404322"
FT BINDING 74
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 92..95
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 276 AA; 28675 MW; 9A027E396CEA9A9F CRC64;
MTVVGELDPQ KLTALVATAA EILDAASVPF VAGHRADSAV RKQGNDFATE VDLAIERQVV
RALTEATGIG VHGEEFGGEP IDSPLVWVLD PIDGTFNYAA GSPMAAILLG LLADGEPVAG
LTWLPFTGEK YSALVGGPLY SDGKPCPPLG SPTLADSIIG IQTFNIDSRG RFPGRYRVEV
LANLSRVCSR VRMHGATGVD LAYVAAGILG GAISFGHHIW DHAAGVALVR AAGGVVTDLT
GAPWTVDSKS VLAAAPGVHE KMLEIVKSTG KPEDYL
