COF_YERPY
ID COF_YERPY Reviewed; 273 AA.
AC B1JHR2;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=YPK_3225;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000950; ACA69494.1; -; Genomic_DNA.
DR RefSeq; WP_012105573.1; NZ_CP009792.1.
DR AlphaFoldDB; B1JHR2; -.
DR SMR; B1JHR2; -.
DR EnsemblBacteria; ACA69494; ACA69494; YPK_3225.
DR KEGG; ypy:YPK_3225; -.
DR PATRIC; fig|502800.11.peg.3952; -.
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..273
FT /note="HMP-PP phosphatase"
FT /id="PRO_0000343007"
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; 30512 MW; 03D7F46D47763F08 CRC64;
MYRLAAFDMD GTLLMRDHKI GSITLNALHQ LADAGVTLTF ATGRHYLDMK GILSHSGLNG
YLITGNGTRV CDAEGNPLYG MDLPAELVEF VLRTPWQTNA SIHLFRDDGW FTDRNDPDLL
IAHTTSGFHF QLTEWDELPL TGNHKFCFIA SHQELVELKA QLEQQMSGEA DFCFSATDCL
EVLPRGCNKG VALEKLSHHL DLTLADCMAF GDAMNDKEML SRVGRGLVMG NALPQLKQEL
PQLQIIGRCE QQGVAHYLHH WLSSPHLTYS PEF
