SUHB_MYCTU
ID SUHB_MYCTU Reviewed; 290 AA.
AC P9WKI9; L0TC07; O07203; P65165;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Inositol-1-monophosphatase SuhB;
DE Short=I-1-Pase;
DE Short=IMPase;
DE Short=Inositol-1-phosphatase;
DE EC=3.1.3.25;
GN Name=suhB; OrderedLocusNames=Rv2701c; ORFNames=MTCY05A6.22c;
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 FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF LEU-81;
RP GLU-83; ASP-104; ASP-107; TRP-234 AND ASP-235.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11914086; DOI=10.1021/bi0160056;
RA Nigou J., Dover L.G., Besra G.S.;
RT "Purification and biochemical characterization of Mycobacterium
RT tuberculosis SuhB, an inositol monophosphatase involved in inositol
RT biosynthesis.";
RL Biochemistry 41:4392-4398(2002).
RN [3]
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).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17725819; DOI=10.1186/1472-6807-7-55;
RA Brown A.K., Meng G., Ghadbane H., Scott D.J., Dover L.G., Nigou J.,
RA Besra G.S., Futterer K.;
RT "Dimerization of inositol monophosphatase Mycobacterium tuberculosis SuhB
RT is not constitutive, but induced by binding of the activator Mg2+.";
RL BMC Struct. Biol. 7:55-55(2007).
CC -!- FUNCTION: Catalyzes the dephosphorylation of inositol 1-phosphate (I-1-
CC P) to yield free myo-inositol, a key metabolite in mycobacteria. Is
CC also able to hydrolyze a variety of polyol phosphates such as glucitol-
CC 6-phosphate, inositol 2-phosphate (I-2-P), glycerol-2-phosphate, and
CC 2'-AMP, albeit with reduced efficiency. {ECO:0000269|PubMed:11914086}.
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 Evidence={ECO:0000269|PubMed:11914086};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11914086};
CC Note=Magnesium. Co(2+) and Fe(2+) can replace Mg(2+) but lead to a
CC partial activity (30%), and Mn(2+) leads to a partial activity of 13%.
CC {ECO:0000269|PubMed:11914086};
CC -!- ACTIVITY REGULATION: Inhibited by Li(+) with IC50 value of 0.9 mM but
CC not by Na(+) or K(+). Also inhibited by Zn(2+) (IC50 value of 0.5 uM)
CC and by concentrations of Mg(2+) higher than 100 mM.
CC {ECO:0000269|PubMed:11914086}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.177 mM for inositol-1-phosphate (at pH 8.5 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:11914086};
CC Vmax=7.2 umol/min/mg enzyme with inositol-1-phosphate as substrate
CC (at pH 8.5 and 37 degrees Celsius) {ECO:0000269|PubMed:11914086};
CC pH dependence:
CC Optimum pH is 8.5. Exhibits a dramatic drop in activity at low pH,
CC with less than 50% activity remaining at pH 7. In contrast, the
CC activity is extremely stable at alkaline pH, with more than 50%
CC activity remaining at pH 12. {ECO:0000269|PubMed:11914086};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius. Loses 80% activity after a
CC 2 minutes incubation at 70 degrees Celsius.
CC {ECO:0000269|PubMed:11914086};
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 2/2.
CC -!- SUBUNIT: Homodimer. Dimerization is induced by Mg(2+) binding.
CC {ECO:0000269|PubMed:17725819}.
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; CCP45499.1; -; Genomic_DNA.
DR PIR; H70530; H70530.
DR RefSeq; NP_217217.1; NC_000962.3.
DR RefSeq; WP_003413939.1; NZ_NVQJ01000017.1.
DR PDB; 2Q74; X-ray; 2.60 A; A/B/C=1-290.
DR PDBsum; 2Q74; -.
DR AlphaFoldDB; P9WKI9; -.
DR SMR; P9WKI9; -.
DR STRING; 83332.Rv2701c; -.
DR iPTMnet; P9WKI9; -.
DR PaxDb; P9WKI9; -.
DR DNASU; 887210; -.
DR GeneID; 45426689; -.
DR GeneID; 887210; -.
DR KEGG; mtu:Rv2701c; -.
DR TubercuList; Rv2701c; -.
DR eggNOG; COG0483; Bacteria.
DR OMA; RVDGYWE; -.
DR PhylomeDB; P9WKI9; -.
DR UniPathway; UPA00823; UER00788.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IDA:MTBBASE.
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:0000287; F:magnesium ion binding; IDA:MTBBASE.
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 CDD; cd01639; IMPase; 1.
DR InterPro; IPR033942; IMPase.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..290
FT /note="Inositol-1-monophosphatase SuhB"
FT /id="PRO_0000142564"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 106..109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT MUTAGEN 81
FT /note="L->A: No effect on activity. 10-fold more resistant
FT to inhibition by Li(+)."
FT /evidence="ECO:0000269|PubMed:11914086"
FT MUTAGEN 83
FT /note="E->D: Less than 4% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:11914086"
FT MUTAGEN 104
FT /note="D->N: Less than 4% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:11914086"
FT MUTAGEN 107
FT /note="D->N: Less than 4% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:11914086"
FT MUTAGEN 234
FT /note="W->L: Less than 4% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:11914086"
FT MUTAGEN 235
FT /note="D->N: Less than 4% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:11914086"
FT HELIX 8..33
FT /evidence="ECO:0007829|PDB:2Q74"
FT HELIX 55..74
FT /evidence="ECO:0007829|PDB:2Q74"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:2Q74"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:2Q74"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:2Q74"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:2Q74"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:2Q74"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:2Q74"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:2Q74"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:2Q74"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:2Q74"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2Q74"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:2Q74"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2Q74"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:2Q74"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:2Q74"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:2Q74"
FT HELIX 211..220
FT /evidence="ECO:0007829|PDB:2Q74"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:2Q74"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:2Q74"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:2Q74"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:2Q74"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:2Q74"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:2Q74"
SQ SEQUENCE 290 AA; 30027 MW; 2C8A3F9A15D515CE CRC64;
MTRPDNEPAR LRSVAENLAA EAAAFVRGRR AEVFGISRAG DGDGAVRAKS SPTDPVTVVD
TDTERLLRDR LAQLRPGDPI LGEEGGGPAD VTATPSDRVT WVLDPIDGTV NFVYGIPAYA
VSIGAQVGGI TVAGAVADVA ARTVYSAATG LGAHLTDERG RHVLRCTGVD ELSMALLGTG
FGYSVRCREK QAELLAHVVP LVRDVRRIGS AALDLCMVAA GRLDAYYEHG VQVWDCAAGA
LIAAEAGARV LLSTPRAGGA GLVVVAAAPG IADELLAALQ RFNGLEPIPD
