ID G2LPE6_BUCUM Unreviewed; 263 AA.
AC G2LPE6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
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:AEO08083.1};
GN ORFNames=BUAMB_266 {ECO:0000313|EMBL:AEO08083.1};
OS Buchnera aphidicola str. Ua (Uroleucon ambrosiae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=1005057 {ECO:0000313|EMBL:AEO08083.1, ECO:0000313|Proteomes:UP000006139};
RN [1] {ECO:0000313|EMBL:AEO08083.1, ECO:0000313|Proteomes:UP000006139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ua {ECO:0000313|EMBL:AEO08083.1,
RC ECO:0000313|Proteomes:UP000006139};
RX PubMed=21912528; DOI=10.1371/journal.pgen.1002252;
RA Degnan P.H., Ochman H., Moran N.A.;
RT "Sequence conservation and functional constraint on intergenic spacers in
RT reduced genomes of the obligate symbiont buchnera.";
RL PLoS Genet. 7:E1002252-E1002252(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; CP002648; AEO08083.1; -; Genomic_DNA.
DR RefSeq; WP_014499987.1; NC_017259.1.
DR AlphaFoldDB; G2LPE6; -.
DR STRING; 1005057.BUAMB_266; -.
DR KEGG; buh:BUAMB_266; -.
DR PATRIC; fig|1005057.4.peg.253; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_0_0_6; -.
DR OrthoDB; 9785695at2; -.
DR Proteomes; UP000006139; 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU364068};
KW Magnesium {ECO:0000256|RuleBase:RU364068};
KW Metal-binding {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 263 AA; 30527 MW; CFE4E926EA00992B CRC64;
MRPMLNIAVR AVRKGGNFII QNYDIRKFIK EDKEKKKIFI KSIIYQTNKL ISDIIYKSYP
NHIILKDNQC HLLNQYEKNT IWIINALDGK NNFIKYFPHF CVSIAIFTKN INEISVIYDP
IKNDLFTAIK GQGSQLNGYR TRCSNFNNLY STTAAVHLPN KNFDNTLLYS EIYQKLILCG
ISLRCTGSTI LDLAYVAAGK IDCLFYFHSE AYDFVTGKLQ VRESGCLINT FKKVNDNNNF
YGYIISNPQF VKLIAEKIQE YHF
//
