COF_SALPK
ID COF_SALPK Reviewed; 272 AA.
AC B5BD74;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=SSPA2107;
OS Salmonella paratyphi A (strain AKU_12601).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=554290;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AKU_12601;
RX PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA Mungall K., Dougan G., Parkhill J.;
RT "Pseudogene accumulation in the evolutionary histories of Salmonella
RT enterica serovars Paratyphi A and Typhi.";
RL BMC Genomics 10:36-36(2009).
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; FM200053; CAR60317.1; -; Genomic_DNA.
DR RefSeq; WP_000113030.1; NC_011147.1.
DR AlphaFoldDB; B5BD74; -.
DR SMR; B5BD74; -.
DR KEGG; sek:SSPA2107; -.
DR HOGENOM; CLU_044146_5_2_6; -.
DR OMA; MPDHRLG; -.
DR Proteomes; UP000001869; 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_1000188512"
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
