ID   COF_SHIDS               Reviewed;         148 AA.
AC   Q32JB1;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Putative HMP-PP phosphatase;
DE            EC=3.6.1.-;
GN   Name=cof; OrderedLocusNames=SDY_0383;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. It is N-terminaly
CC       truncated compared to othologs. {ECO:0000305}.
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DR   EMBL; CP000034; ABB60596.1; -; Genomic_DNA.
DR   RefSeq; YP_402085.1; NC_007606.1.
DR   AlphaFoldDB; Q32JB1; -.
DR   SMR; Q32JB1; -.
DR   STRING; 300267.SDY_0383; -.
DR   EnsemblBacteria; ABB60596; ABB60596; SDY_0383.
DR   KEGG; sdy:SDY_0383; -.
DR   PATRIC; fig|300267.13.peg.454; -.
DR   HOGENOM; CLU_1757584_0_0_6; -.
DR   Proteomes; UP000002716; Chromosome.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
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   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; TIGR01484; HAD-SF-IIB; 1.
DR   PROSITE; PS01229; COF_2; 1.
PE   5: Uncertain;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..148
FT                   /note="Putative HMP-PP phosphatase"
FT                   /id="PRO_0000342996"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   148 AA;  16353 MW;  9FA7916BEB9BD4FA CRC64;
     MPVHLNQIID VKKMPLGSVT KICFCGDHDD LTRLQIQLYE ALGERAHLCF SATDCLEVLP
     VGCNKGAALT VLTQHLGLSL RDCMAFGDAM NDREMLGSVG SGFIMGNAMP QLRAELPHLP
     VIGHCRNQAV SHYLTHWLDY PHLPYSPE