ID A5CUU6_CLAM3 Unreviewed; 269 AA.
AC A5CUU6;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
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:CAN02884.1};
GN OrderedLocusNames=CMM_2799 {ECO:0000313|EMBL:CAN02884.1};
OS Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Clavibacter.
OX NCBI_TaxID=443906 {ECO:0000313|EMBL:CAN02884.1, ECO:0000313|Proteomes:UP000001564};
RN [1] {ECO:0000313|EMBL:CAN02884.1, ECO:0000313|Proteomes:UP000001564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 382 {ECO:0000313|EMBL:CAN02884.1,
RC ECO:0000313|Proteomes:UP000001564};
RX PubMed=18192381; DOI=10.1128/JB.01595-07;
RA Gartemann K.H., Abt B., Bekel T., Burger A., Engemann J., Flugel M.,
RA Gaigalat L., Goesmann A., Grafen I., Kalinowski J., Kaup O., Kirchner O.,
RA Krause L., Linke B., McHardy A., Meyer F., Pohle S., Ruckert C.,
RA Schneiker S., Zellermann E.M., Puhler A., Eichenlaub R., Kaiser O.,
RA Bartels D.;
RT "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT in pathogenicity.";
RL J. Bacteriol. 190:2138-2149(2008).
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; AM711867; CAN02884.1; -; Genomic_DNA.
DR RefSeq; WP_012039487.1; NC_009480.1.
DR AlphaFoldDB; A5CUU6; -.
DR KEGG; cmi:CMM_2799; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_0_1_11; -.
DR OrthoDB; 9772456at2; -.
DR Proteomes; UP000001564; 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}.
SQ SEQUENCE 269 AA; 28141 MW; 8F4E6718869F0775 CRC64;
MTTPGDTALL TIARDIAVRA GELALRRRRE GVEVAASKSS PEDIVTHTDR ETEDLIRQAL
RDVRPDDGFL GEESEGTSGS SGLTWVVDPI DGTVNFLYGI PAWAVSIAVV EGEADPLTWT
ARAGCVVNPT LGEVYTATKG GGSALDGRPL AVNAGVPLSL ALVGTGFSYG AETRMRQGRV
ITDLLGEVRD IRRIGAASLD LCNVAAGRTD AYFERGLKPW DHAAGGLIAA EAGARVTGIG
GGPASAELLI AADPELARAL EERLERPRA
//
