ID C4ZK30_THASP Unreviewed; 266 AA.
AC C4ZK30; A0A5C7SFK9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN OrderedLocusNames=Tmz1t_2282 {ECO:0000313|EMBL:ACK55021.1};
GN ORFNames=E6Q80_16760 {ECO:0000313|EMBL:TXH81726.1};
OS Thauera aminoaromatica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=164330 {ECO:0000313|EMBL:ACK55021.1, ECO:0000313|Proteomes:UP000002186};
RN [1] {ECO:0000313|Proteomes:UP000002186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MZ1T {ECO:0000313|Proteomes:UP000002186};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sayler G.S.;
RT "Complete sequence of chromosome of Thauera sp. MZ1T.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACK55021.1, ECO:0000313|Proteomes:UP000002186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MZ1T {ECO:0000313|EMBL:ACK55021.1,
RC ECO:0000313|Proteomes:UP000002186};
RX PubMed=23407619; DOI=10.4056/sigs.2696029;
RA Jiang K., Sanseverino J., Chauhan A., Lucas S., Copeland A., Lapidus A.,
RA Del Rio T.G., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D.,
RA Brettin T., Detter J.C., Han C., Chang Y.J., Larimer F., Land M.,
RA Hauser L., Kyrpides N.C., Mikhailova N., Moser S., Jegier P., Close D.,
RA Debruyn J.M., Wang Y., Layton A.C., Allen M.S., Sayler G.S.;
RT "Complete genome sequence of Thauera aminoaromatica strain MZ1T.";
RL Stand. Genomic Sci. 6:325-335(2012).
RN [3] {ECO:0000313|EMBL:TXH81726.1, ECO:0000313|Proteomes:UP000321192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bin_27_1 {ECO:0000313|EMBL:TXH81726.1};
RA Stamps B.W., Spear J.R.;
RT "Metagenome Assembled Genomes from an Advanced Water Purification
RT Facility.";
RL Submitted (SEP-2018) 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|ARBA:ARBA00009759, ECO:0000256|RuleBase:RU364068}.
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DR EMBL; CP001281; ACK55021.1; -; Genomic_DNA.
DR EMBL; SSFD01000268; TXH81726.1; -; Genomic_DNA.
DR RefSeq; WP_012585460.1; NZ_SSFD01000268.1.
DR AlphaFoldDB; C4ZK30; -.
DR STRING; 85643.Tmz1t_2282; -.
DR KEGG; tmz:Tmz1t_2282; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_0_0_4; -.
DR OrthoDB; 9785695at2; -.
DR Proteomes; UP000002186; Chromosome.
DR Proteomes; UP000321192; 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 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:UP000002186}.
SQ SEQUENCE 266 AA; 28931 MW; B0AD94E4B8E1E3D2 CRC64;
MHPTLNIAVK AARRAASVIN RASTQLDLLT VQSKSPNDFV TEVDRAAEQA IIEVLRDAFP
GHGILAEESG ESGPESEYTW IIDPLDGTTN FIHGMPQYAV SIAQTKNGVL EHAVVYDPNT
NEMFTASRGA GAFLNDRRIR VSRRTRLNEA LIGTGFPFRQ FDHVDAYLAM FKELTQKTAG
IRRPGAASLD LAYVASGRFD GFWEMGLSPW DMAAGVLLIQ EAGGLVSDLS GEANYLTTGN
LVAGTPKIFG QLLPIIQAWR PANLRA
//
