ID COF_YERPA Reviewed; 273 AA.
AC Q1C4L7;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=YPA_2643;
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(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; CP000308; ABG14605.1; -; Genomic_DNA.
DR RefSeq; WP_002208632.1; NZ_CP009906.1.
DR AlphaFoldDB; Q1C4L7; -.
DR SMR; Q1C4L7; -.
DR GeneID; 57975563; -.
DR KEGG; ypa:YPA_2643; -.
DR Proteomes; UP000001971; 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 CDD; cd07516; HAD_Pase; 1.
DR Gene3D; 3.30.1240.10; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR00099; Cof-subfamily; 1.
DR NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR PANTHER; PTHR47267; -; 1.
DR PANTHER; PTHR47267:SF2; HMP-PP PHOSPHATASE; 1.
DR Pfam; PF08282; Hydrolase_3; 1.
DR SFLD; SFLDG01140; C2.B:_Phosphomannomutase_and_P; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 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_0000343003"
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; 30482 MW; 6E61242C53277A1C CRC64;
MYRLAAFDMD GTLLMRDHKI GSITLNALHQ LADAGVTLTF ATGRHYLDMK GILSHSGLNG
YLITGNGTRV CDAEGNPLYG MDLPAELVEF VLRTPWQTNA SIHLFRDDGW FTDRNDPDLL
IAHTTSGFHF QLTEWDELPL TGNHKFCFIA SHQELVELKA QLEQQMGGEA DFCFSATDCL
EVLPRGCNKG VALEKLSHHL DLTLADCMAF GDAMNDKEML SRVGRGLVMG NALPQLKQEL
PQLQIIGRCE QQGVAHYLHH WLSSPHLTYS PEF
//
