ID C0ZHX7_BREBN Unreviewed; 258 AA.
AC C0ZHX7;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN OrderedLocusNames=BBR47_42740 {ECO:0000313|EMBL:BAH45251.1};
OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH45251.1, ECO:0000313|Proteomes:UP000001877};
RN [1] {ECO:0000313|EMBL:BAH45251.1, ECO:0000313|Proteomes:UP000001877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47 / JCM 6285 / NBRC 100599
RC {ECO:0000313|Proteomes:UP000001877};
RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA Udaka S., Tanikawa S., Fujita N.;
RT "Brevibacillus brevis strain 47, complete genome.";
RL Submitted (MAR-2005) 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|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; AP008955; BAH45251.1; -; Genomic_DNA.
DR RefSeq; WP_015892517.1; NC_012491.1.
DR AlphaFoldDB; C0ZHX7; -.
DR STRING; 358681.BBR47_42740; -.
DR KEGG; bbe:BBR47_42740; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_0_4_9; -.
DR Proteomes; UP000001877; 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 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU364068, ECO:0000313|EMBL:BAH45251.1};
KW Magnesium {ECO:0000256|RuleBase:RU364068};
KW Metal-binding {ECO:0000256|RuleBase:RU364068};
KW Reference proteome {ECO:0000313|Proteomes:UP000001877}.
SQ SEQUENCE 258 AA; 29346 MW; BF08C4F09D7D40EB CRC64;
MIEIAKEAAS VAGAFLKERF LEQLVPDEEL HNDVKLPEDK GSEQRIIEVL HRHFPTHTIF
SEEVGMVSRE EEYLWIIDPL DGTNNYFIGY PYFSISIALQ HKGELVLGVV YNPVAGQMFW
AEKGKGAYLN GKRLNVNNRQ DLTRAVGTYI RGRNTVTKEE EMAFTEPFVF QTKRLMRNIA
PALDWCLLAN GWLDYIVMQR SNIMDVAAGI VIAQEAGATI TDWSGKPYQH EPFQQDHTPS
LVASNGHLHE TIRGMIRQ
//
