AC MF_01847; DC Protein; auto TR HAMAP; MF_01847; -; 1; level=0 XX Names: HMP_PP_phosphat XX ID COF DE RecName: Full=HMP-PP phosphatase; DE EC=3.6.1.-; GN Name=cof; XX 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). 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family. XX DR PROSITE; PS01228; COF_1; 1; trigger=no DR PROSITE; PS01229; COF_2; 1; trigger=no DR Pfam; PF00702; Hydrolase; 1; trigger=no DR Pfam; PF08282; Hydrolase_3; 1; trigger=no DR NCBIfam; TIGR00099; Cof-subfamily; 1; trigger=no DR NCBIfam; TIGR01484; HAD-SF-IIB; 1; trigger=no XX KW Hydrolase KW Magnesium KW Metal-binding XX GO GO:0000287; F:magnesium ion binding GO GO:0016791; F:phosphatase activity XX FT From: COF_ECOLI (P46891) FT ACT_SITE 8 FT /note="Nucleophile" FT Condition: D FT BINDING 8 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: D FT BINDING 10 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: D FT BINDING 212 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: D XX Size: 260-274; Related: None; Template: P46891; Scope: Bacteria; Enterobacterales Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: The N-terminus of ECOLC is shorter. SHIDS is truncated and probably not functional. These sequences have not been included in the alignment. XX # Revision 1.18 2023/06/01 //