ID A0Q7K6_FRATN Unreviewed; 262 AA.
AC A0Q7K6;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN OrderedLocusNames=FTN_1346 {ECO:0000313|EMBL:ABK90221.1};
GN ORFNames=AW25_657 {ECO:0000313|EMBL:AJI61930.1};
OS Francisella tularensis subsp. novicida (strain U112).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=401614 {ECO:0000313|EMBL:ABK90221.1, ECO:0000313|Proteomes:UP000000762};
RN [1] {ECO:0000313|EMBL:ABK90221.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=U112 {ECO:0000313|EMBL:ABK90221.1};
RA Brittnacher M., Rohmer L., Zhou Y., Abmayr S., D'Argenio D., Bovee D.,
RA Chang J., Chen J., Drees B., Ernst R., Fong C., Forsman M., Gallagher L.,
RA Gallis B., Gillett W., Goodlett D., Guina T., Guenthner D., Haugen E.,
RA Hayden H., Jacobs M., Kang A., Larson Freeman T., Levy R., Lim R.,
RA Manoil C., Olson M.V., Radey M., Shaffer S., Svensson K., Taylor G.,
RA Wasnick M., Kaul R., Miller S.I.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000000762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U112 {ECO:0000313|Proteomes:UP000000762};
RX PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M.,
RA Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C.,
RA Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J.,
RA Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A.,
RA Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V.,
RA Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.;
RT "Comparison of Francisella tularensis genomes reveals evolutionary events
RT associated with the emergence of human pathogenic strains.";
RL Genome Biol. 8:R102.1-R102.16(2007).
RN [3] {ECO:0000313|EMBL:AJI61930.1, ECO:0000313|Proteomes:UP000031872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U112 {ECO:0000313|EMBL:AJI61930.1,
RC ECO:0000313|Proteomes:UP000031872};
RX PubMed=25931589;
RA Johnson S.L., Daligault H.E., Davenport K.W., Coyne S.R., Frey K.G.,
RA Koroleva G.I., Broomall S.M., Bishop-Lilly K.A., Bruce D.C., Chertkov O.,
RA Freitas T., Jaissle J., Ladner J.T., Rosenzweig C.N., Gibbons H.S.,
RA Palacios G.F., Redden C.L., Xu Y., Minogue T.D., Chain P.S.;
RT "Genome sequencing of 18 francisella strains to aid in assay development
RT and testing.";
RL Genome Announc. 3:0-0(2015).
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|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|RuleBase:RU364068}.
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DR EMBL; CP000439; ABK90221.1; -; Genomic_DNA.
DR EMBL; CP009633; AJI61930.1; -; Genomic_DNA.
DR RefSeq; WP_003016111.1; NZ_CP009633.1.
DR AlphaFoldDB; A0Q7K6; -.
DR GeneID; 75264921; -.
DR KEGG; ftn:FTN_1346; -.
DR KEGG; ftx:AW25_657; -.
DR BioCyc; FTUL401614:G1G75-1391-MONOMER; -.
DR Proteomes; UP000000762; Chromosome.
DR Proteomes; UP000031872; 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: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 PANTHER; PTHR20854; INOSITOL MONOPHOSPHATASE; 1.
DR PANTHER; PTHR20854:SF4; INOSITOL-1-MONOPHOSPHATASE-RELATED; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR PROSITE; PS00629; IMP_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU364068};
KW Lithium {ECO:0000256|ARBA:ARBA00022671};
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 262 AA; 28868 MW; FFE89CE79E21D15F CRC64;
MKPILNSVTT IARKAGKIIL QAQNDLSSIK ISQKLDNTTV SNIDIAVENF IIDNIKKSGF
NDYFITEENG EFGNKDSRFT WIIDPIDGTN NFVHGLPHCC ISIAAKKDDD IVLGVIYNPF
LDLMFCAYKG QGALLNGKKI RVAQNQDLKN TLISASLKYS RRIFNDSYVA ELIKLQQTIS
GYRYSGSIAM DMAYLAAGYI DGLWACGNVK IWDLAAGYII MKEAGAVVTN IHGTSDLDSG
LIVAGNKKIQ PKLIKILAKH IK
//
