ID   COF_ECO8A               Reviewed;         272 AA.
AC   B7M3T9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=HMP-PP phosphatase {ECO:0000255|HAMAP-Rule:MF_01847};
DE            EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_01847};
GN   Name=cof {ECO:0000255|HAMAP-Rule:MF_01847}; OrderedLocusNames=ECIAI1_0450;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Catalyzes the hydrolysis of 4-amino-2-methyl-5-
CC       hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2-methyl-5-
CC       hydroxymethylpyrimidine phosphate (HMP-P). {ECO:0000255|HAMAP-
CC       Rule:MF_01847}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + H2O = 4-
CC         amino-2-methyl-5-(phosphooxymethyl)pyrimidine + H(+) + phosphate;
CC         Xref=Rhea:RHEA:27914, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57841, ChEBI:CHEBI:58354;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01847};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01847};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family.
CC       {ECO:0000255|HAMAP-Rule:MF_01847}.
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DR   EMBL; CU928160; CAQ97322.1; -; Genomic_DNA.
DR   RefSeq; WP_001309304.1; NC_011741.1.
DR   AlphaFoldDB; B7M3T9; -.
DR   SMR; B7M3T9; -.
DR   KEGG; ecr:ECIAI1_0450; -.
DR   HOGENOM; CLU_044146_5_2_6; -.
DR   OMA; MPDHRLG; -.
DR   GO; GO:0002145; F:4-amino-5-hydroxymethyl-2-methylpyrimidine diphosphatase activity; IEA:RHEA.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   HAMAP; MF_01847; HMP_PP_phosphat; 1.
DR   InterPro; IPR000150; Cof.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023938; HMP-PP_phosphatase.
DR   PANTHER; PTHR47267:SF2; PTHR47267:SF2; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR00099; Cof-subfamily; 1.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR   PROSITE; PS01228; COF_1; 1.
DR   PROSITE; PS01229; COF_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..272
FT                   /note="HMP-PP phosphatase"
FT                   /id="PRO_1000188501"
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01847"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01847"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01847"
FT   BINDING         212
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01847"
SQ   SEQUENCE   272 AA;  30345 MW;  D8FC1F3BE5B4EADC CRC64;
     MARLAAFDMD GTLLMPDHHL GEKTLSTLAR LRERDITLTF ATGRHALEMQ HILGALSLDA
     YLITGNGTRV HSLEGELLHR DDLPADVAEL VLYQQWDTRA SMHIFNDDGW FTGKEIPALL
     QAFVYSGFRY QIIDVKKMPL GSVTKICFCG DHDDLTRLQI QLYEALGERA HLCFSATDCL
     EVLPVGCNKG AALTVLTQHL GLSLRDCMAF GDAMNDREML GCVGSGFIMG NAMPQLRAEL
     PHLPVIGHCR NQAVSHYLTH WLDYPHLPYS PE