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Database: UniProt
Entry: E6YJ57_BARC7
LinkDB: E6YJ57_BARC7
Original site: E6YJ57_BARC7 
ID   E6YJ57_BARC7            Unreviewed;       263 AA.
AC   E6YJ57;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
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:CBI76895.1};
GN   OrderedLocusNames=BARCL_1223 {ECO:0000313|EMBL:CBI76895.1};
OS   Bartonella clarridgeiae (strain CCUG 45776 / CIP 104772 / 73).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=696125 {ECO:0000313|EMBL:CBI76895.1, ECO:0000313|Proteomes:UP000009101};
RN   [1] {ECO:0000313|Proteomes:UP000009101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 104772 / 73 {ECO:0000313|Proteomes:UP000009101};
RA   Engel P., Salzburger W., Marius L., Chao-Chin C., Soichi M., Christa L.,
RA   Alexandra C., Aurelie L., Claudine M., Stephan S.C., Christoph D.;
RT   "Genome sequencing of Bartonella species and comparative genomics.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBI76895.1, ECO:0000313|Proteomes:UP000009101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 104772 / 73 {ECO:0000313|Proteomes:UP000009101};
RX   PubMed=21347280; DOI=10.1371/journal.pgen.1001296;
RA   Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C.,
RA   Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.;
RT   "Parallel evolution of a type IV secretion system in radiating lineages of
RT   the host-restricted bacterial pathogen Bartonella.";
RL   PLoS Genet. 7:E1001296-E1001296(2011).
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; FN645454; CBI76895.1; -; Genomic_DNA.
DR   RefSeq; WP_013545518.1; NC_014932.1.
DR   AlphaFoldDB; E6YJ57; -.
DR   STRING; 696125.BARCL_1223; -.
DR   KEGG; bcd:BARCL_1223; -.
DR   eggNOG; COG0483; Bacteria.
DR   HOGENOM; CLU_044118_0_4_5; -.
DR   OrthoDB; 9785695at2; -.
DR   Proteomes; UP000009101; 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   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}.
SQ   SEQUENCE   263 AA;  29203 MW;  25684817B80DB237 CRC64;
     MAHSAIMHIM VQAAIKAGRS LVRDYGEVQN LQVSLKGPAD YVSQADCKAE KIIFNELSKA
     RPKFGFLMEE SQEIIGEDSQ HRFIVDPLDG TINFLHGLPF FAVSIALERQ GQIVAGVIYN
     PILDELFTAE RGCGAFLNDR RCRVAVRRKL EHCIIATGLP HLGRPNHENY LVELRNVMAE
     VSGIRRFGAA SLDLAYVAAG RVDGFWEDNL QIWDMAAGLL MVREAGGFIS DKDGEQDIFG
     KKNIVAGNEV IHAELKKILK KEV
//
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