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Database: UniProt
Entry: A6TCF4_KLEP7
LinkDB: A6TCF4_KLEP7
Original site: A6TCF4_KLEP7 
ID   A6TCF4_KLEP7            Unreviewed;       267 AA.
AC   A6TCF4;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE            EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN   Name=suhB {ECO:0000313|EMBL:ABR78275.1};
GN   ORFNames=KPN_02865 {ECO:0000313|EMBL:ABR78275.1};
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620 {ECO:0000313|EMBL:ABR78275.1, ECO:0000313|Proteomes:UP000000265};
RN   [1] {ECO:0000313|EMBL:ABR78275.1, ECO:0000313|Proteomes:UP000000265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2] {ECO:0000313|EMBL:ABR78275.1, ECO:0000313|Proteomes:UP000000265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001033,
CC         ECO:0000256|RuleBase:RU364068};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|RuleBase:RU364068};
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000256|ARBA:ARBA00009759, ECO:0000256|RuleBase:RU364068}.
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DR   EMBL; CP000647; ABR78275.1; -; Genomic_DNA.
DR   RefSeq; WP_002913995.1; NC_009648.1.
DR   AlphaFoldDB; A6TCF4; -.
DR   STRING; 272620.KPN_02865; -.
DR   jPOST; A6TCF4; -.
DR   PaxDb; 272620-KPN_02865; -.
DR   EnsemblBacteria; ABR78275; ABR78275; KPN_02865.
DR   GeneID; 64294097; -.
DR   KEGG; kpn:KPN_02865; -.
DR   HOGENOM; CLU_044118_0_4_6; -.
DR   Proteomes; UP000000265; Chromosome.
DR   GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:UniProtKB-EC.
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:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-KW.
DR   CDD; cd01639; IMPase; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 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   InterPro; IPR022337; Inositol_monophosphatase_SuhB.
DR   PANTHER; PTHR20854; INOSITOL MONOPHOSPHATASE; 1.
DR   PANTHER; PTHR20854:SF50; NUS FACTOR SUHB; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   PRINTS; PR01959; SBIMPHPHTASE.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364068};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU364068};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364068};
KW   Transcription {ECO:0000256|ARBA:ARBA00022814};
KW   Transcription antitermination {ECO:0000256|ARBA:ARBA00022814};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00022814}.
SQ   SEQUENCE   267 AA;  29320 MW;  5EA4A8E55DA4F00A CRC64;
     MHPMLNIAVR AARKAGNLIA KHYETPDTVE TSQKGSNDFV TNVDKAAEAI IIETIRKSYP
     QHTIITEESG EHAGEEQDVQ WVIDPLDGTT NFVKRLPHFS VSIAVRIKGR TEVAVVYDPM
     RNELFTATRG QGAQLNGYRL RGSNARDLDG TIIATGFPFK AKQHATTYMN ILGNMFTECA
     DFRRTGSAAL DLAYVAAGRV DGYFEIALKP WDFAAGELIA REAGAIVCDF TGGHNYMLTG
     NIVAGNPRVV KAMLANMREQ LSDALKR
//
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