ID   COF_YERE8               Reviewed;         273 AA.
AC   A1JNL2;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=YE3125;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL13160.1; -; Genomic_DNA.
DR   RefSeq; WP_011816893.1; NC_008800.1.
DR   RefSeq; YP_001007307.1; NC_008800.1.
DR   AlphaFoldDB; A1JNL2; -.
DR   SMR; A1JNL2; -.
DR   STRING; 393305.YE3125; -.
DR   EnsemblBacteria; CAL13160; CAL13160; YE3125.
DR   KEGG; yen:YE3125; -.
DR   PATRIC; fig|393305.7.peg.3327; -.
DR   eggNOG; COG0561; Bacteria.
DR   HOGENOM; CLU_044146_5_2_6; -.
DR   OMA; MPDHRLG; -.
DR   Proteomes; UP000000642; Chromosome.
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..273
FT                   /note="HMP-PP phosphatase"
FT                   /id="PRO_0000343000"
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   273 AA;  30467 MW;  71F4CA94B0185D0C CRC64;
     MYRLAAFDMD GTLLMRDHRI GGATLNALHQ LVDNGMILTF ATGRHYLDMK GILSHSGING
     YLITGNGTRV CDMDGMHLDG MDLPAELVEF VLRTPWQTNA SIHIFRDDGW FTDYNDPALL
     AAHKTSSFQF QLTALDALPK TGNHKICFIA PHQELAELKI QLEQHMGDQA DFCFSAVDCL
     EMLPRGCNKG AALERLSHHL DLTLADCMAF GDAMNDKEML SRVGRGLVMG NALPQLKQEL
     PQLQVIGRCE EQGVAHYLQH WLSSPHLTYS PEF