ID A0A076NN78_9CORY Unreviewed; 286 AA.
AC A0A076NN78;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, 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 ORFNames=CIMIT_07175 {ECO:0000313|EMBL:AIJ33706.1};
OS Corynebacterium imitans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=156978 {ECO:0000313|EMBL:AIJ33706.1, ECO:0000313|Proteomes:UP000028780};
RN [1] {ECO:0000313|EMBL:AIJ33706.1, ECO:0000313|Proteomes:UP000028780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44264 {ECO:0000313|EMBL:AIJ33706.1,
RC ECO:0000313|Proteomes:UP000028780};
RA Mollmann S., Albersmeier A., Ruckert C., Tauch A.;
RT "Complete genome sequence of Corynebacterium imitans DSM 44264, isolated
RT from a five-month-old boy with suspected pharyngeal diphtheria.";
RL Submitted (AUG-2014) 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; CP009211; AIJ33706.1; -; Genomic_DNA.
DR RefSeq; WP_038590952.1; NZ_LT906467.1.
DR AlphaFoldDB; A0A076NN78; -.
DR STRING; 156978.CIMIT_07175; -.
DR KEGG; cii:CIMIT_07175; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_0_1_11; -.
DR OrthoDB; 9772456at2; -.
DR Proteomes; UP000028780; 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 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.
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:UP000028780}.
SQ SEQUENCE 286 AA; 29646 MW; A480BA9D81CA3EE7 CRC64;
MNTAANHVPS PAELRDMCVD LVTDAAEFVA HQRAFLTKHG SVAMVAETKS SEVDPVTAVD
KGCEARVVKR LAELRPDDGI IGEEGSAVPT RTGVEWVIDP IDGTVNFIYG VPAYAVSVGV
AVDGELVAGA VADVARGVVY RAAVGAGASV LIDGTAHPLR ASRASQLATT LVATGFAYDA
GWRGLQAEIL QHILPVVRDI RRMGSAALDL CRVAEGSVDA YYEHGTHPWD YAAGAVIAAE
AGAVVHHPGL VDRGGQGALV TACAPGIADE FADLLHKAGA QRDLQA
//
