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Database: UniProt
Entry: A0A0Q7KLP5_9ACTN
LinkDB: A0A0Q7KLP5_9ACTN
Original site: A0A0Q7KLP5_9ACTN 
ID   A0A0Q7KLP5_9ACTN        Unreviewed;       266 AA.
AC   A0A0Q7KLP5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE            EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN   ORFNames=ASD10_13075 {ECO:0000313|EMBL:KQX76560.1};
OS   Aeromicrobium sp. Root472D3.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=1736540 {ECO:0000313|EMBL:KQX76560.1, ECO:0000313|Proteomes:UP000050971};
RN   [1] {ECO:0000313|EMBL:KQX76560.1, ECO:0000313|Proteomes:UP000050971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root472D3 {ECO:0000313|EMBL:KQX76560.1,
RC   ECO:0000313|Proteomes:UP000050971};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQX76560.1, ECO:0000313|Proteomes:UP000050971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root472D3 {ECO:0000313|EMBL:KQX76560.1,
RC   ECO:0000313|Proteomes:UP000050971};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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|RuleBase:RU364068}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQX76560.1}.
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DR   EMBL; LMET01000001; KQX76560.1; -; Genomic_DNA.
DR   RefSeq; WP_056610540.1; NZ_LMET01000001.1.
DR   AlphaFoldDB; A0A0Q7KLP5; -.
DR   STRING; 1736540.ASD10_13075; -.
DR   Proteomes; UP000050971; Unassembled WGS sequence.
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; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
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   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00629; IMP_1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {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   Reference proteome {ECO:0000313|Proteomes:UP000050971}.
SQ   SEQUENCE   266 AA;  28102 MW;  BD632CC51417EE5A CRC64;
     MSADREELLA LARRVGLEAA AYVRSARPAG RVDVSSTKSS ETDVVTAIDE ACERLIRERI
     FAARPDDGFV GEEGDDVVGA SGVDWVVDPI DGTVNFVYGI PTYGVSIAAR QDGEVVVGHV
     VNIASGAEWG AVAGAGSWRY DGDERLVLTA PPVARLAHAL VATGFNYVPE VRAKQAAAMA
     AFIPQVRDIR RIGSASLDLC GLAEGQFDAY VEQGLKPWDL AAGGLVAREA GLVLSGLDGE
     PDERLVMAAH PSVAEEYFEL VRACGF
//
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