ID D8P9N6_9BACT Unreviewed; 273 AA.
AC D8P9N6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:CBK39945.1};
GN ORFNames=NIDE0161 {ECO:0000313|EMBL:CBK39945.1};
OS Nitrospira defluvii.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=330214 {ECO:0000313|EMBL:CBK39945.1, ECO:0000313|Proteomes:UP000001660};
RN [1] {ECO:0000313|EMBL:CBK39945.1, ECO:0000313|Proteomes:UP000001660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20624973; DOI=10.1073/pnas.1003860107;
RA Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B.,
RA Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.;
RT "A Nitrospira metagenome illuminates the physiology and evolution of
RT globally important nitrite-oxidizing bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 0:13479-13484(2010).
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; FP929003; CBK39945.1; -; Genomic_DNA.
DR AlphaFoldDB; D8P9N6; -.
DR STRING; 330214.NIDE0161; -.
DR KEGG; nde:NIDE0161; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_0_2_0; -.
DR OrthoDB; 9772456at2; -.
DR Proteomes; UP000001660; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001660}.
SQ SEQUENCE 273 AA; 29894 MW; E6FB600831831B5E CRC64;
MQTSKRPSSE DCTVFLATAI RAAEAAGTVL LEHARSGFRI DYKAAINLVT DADRGAEESI
VRTILSAHPS HRILAEERGE DGAADSPYRW IIDPLDGTTN FAHGFPFYSV SIGLECDGEC
IVGVVLDPVR RELFTAVLGQ GAYLNGERLR VSIIQTLEHS LLVTGFAYNI RETTNNNLDH
FSRISLRAQG VRRTGSAALD LSYVAAGRFD GYWEVKLSPW DMAAGIVILR EAGGVVSGFS
RSRFSLYGQE LVATNGHIHD QLLRAINQHP DPH
//
