ID A0A142YNR7_9PLAN Unreviewed; 276 AA.
AC A0A142YNR7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN Name=suhB_2 {ECO:0000313|EMBL:AMV40682.1};
GN ORFNames=VT85_24840 {ECO:0000313|EMBL:AMV40682.1};
OS Planctomyces sp. SH-PL62.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Planctomyces.
OX NCBI_TaxID=1636152 {ECO:0000313|EMBL:AMV40682.1, ECO:0000313|Proteomes:UP000076365};
RN [1] {ECO:0000313|EMBL:AMV40682.1, ECO:0000313|Proteomes:UP000076365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH-PL62 {ECO:0000313|EMBL:AMV40682.1,
RC ECO:0000313|Proteomes:UP000076365};
RA van der Voort M., Raaijmakers J.M.;
RT "Genome minning of novel planctomycete species.";
RL Submitted (APR-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}.
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DR EMBL; CP011273; AMV40682.1; -; Genomic_DNA.
DR RefSeq; WP_068420790.1; NZ_CP011273.1.
DR AlphaFoldDB; A0A142YNR7; -.
DR STRING; 1636152.VT85_24840; -.
DR KEGG; plh:VT85_24840; -.
DR PATRIC; fig|1636152.3.peg.5614; -.
DR Proteomes; UP000076365; 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; 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, ECO:0000313|EMBL:AMV40682.1};
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:UP000076365}.
SQ SEQUENCE 276 AA; 29620 MW; 078BCA8D671AD853 CRC64;
MDRWKAELEV AEAAAKAGGA VATGYFRGGL AADVKNAEGQ GTYNLVTRAD VEAERAVVEV
IKKAFPGHAI YGEEGQGDGG EGAAILASED VWIVDPIDGT SNFVHGIPHF GVSVAYYHKG
DATVGVVGNP LYDDWYTAVR GGGAFHRGRR ARVSPCARLD EVLVGFGYFY DRGAMMEATL
EACAEILRRR SHGLRRLGAA TLDLAYVGVG SFGAFFEYEL APWDFAAGRL FVEEAGGRVT
NCHGDPLTLR KDGVLASNGL VHDELVAIMN EYFRKP
//
