ID   COF_SALPA               Reviewed;         272 AA.
AC   Q5PFM4;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=SPA2265;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV78150.1; -; Genomic_DNA.
DR   RefSeq; WP_000113030.1; NC_006511.1.
DR   AlphaFoldDB; Q5PFM4; -.
DR   SMR; Q5PFM4; -.
DR   EnsemblBacteria; AAV78150; AAV78150; SPA2265.
DR   KEGG; spt:SPA2265; -.
DR   HOGENOM; CLU_044146_5_2_6; -.
DR   OMA; MPDHRLG; -.
DR   Proteomes; UP000008185; 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..272
FT                   /note="HMP-PP phosphatase"
FT                   /id="PRO_0000342990"
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;  30104 MW;  19924922D9AB36CB CRC64;
     MARLAAFDMD GTLLMPDHHL GRETIATLAR LRERDITLTF ATGRHVLEMR HILGTLSLDA
     YLITGNGTRI HSLEGDVLHR QDLDPQVADT VMHHAWDTRA SMHVFNDNGW FTGQEIPALL
     QAHVYSGFRY QVIDIKSIPA HQVTKICFCG DHDDLIRLRI QLNEALEERA HLCFSAVDCL
     EVLPLGCNKG SALAVLSNHL GLSLADCMAF GDAMNDREML GSVGRGLIMG NAMPQLIAAL
     PHLSVIGHCG NQAVSHFLTH WLDNPHLPYS PE