ID   A0A7U9AVP1_ECOLX        Unreviewed;       272 AA.
AC   A0A7U9AVP1;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   03-MAY-2023, entry version 7.
DE   RecName: Full=HMP-PP phosphatase {ECO:0000256|HAMAP-Rule:MF_01847};
DE            EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_01847};
GN   Name=cof {ECO:0000256|HAMAP-Rule:MF_01847};
GN   ORFNames=ECKG_00309 {ECO:0000313|EMBL:EGI26760.1};
OS   Escherichia coli TA206.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=656440 {ECO:0000313|EMBL:EGI26760.1};
RN   [1] {ECO:0000313|EMBL:EGI26760.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TA206 {ECO:0000313|EMBL:EGI26760.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Escherichia coli TA206.";
RL   Submitted (JAN-2010) 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:0000256|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:0000256|HAMAP-Rule:MF_01847};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01847};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family.
CC       {ECO:0000256|HAMAP-Rule:MF_01847}.
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DR   EMBL; GL884168; EGI26760.1; -; Genomic_DNA.
DR   RefSeq; WP_000113027.1; NZ_GL884168.1.
DR   AlphaFoldDB; A0A7U9AVP1; -.
DR   SMR; A0A7U9AVP1; -.
DR   GeneID; 75202871; -.
DR   Proteomes; UP000003960; Unassembled WGS sequence.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-UniRule.
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   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   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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01847};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01847};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01847}.
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01847"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01847"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01847"
FT   BINDING         212
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01847"
SQ   SEQUENCE   272 AA;  30329 MW;  D8FC03565373EADC CRC64;
     MARLAAFDMD GTLLMPDHHL GEKTLSTLAR LRERDITLTF ATGRHALEMQ HILGALSLDA
     YLITGNGTRV HSLEGELLHR DDLPADVAEL VLYQQWDTRA SMHIFNDDGW FTGKEIPALL
     QAFVYSGFRY QIIDVKKMPL GSVTKICFCG DHDDLTRLQI QLYEALGERA HLCFSATDCL
     EVLPVGCNKG AALTVLTQHL GLSLRDCMAF GDAMNDREML GSVGSGFIMG NAMPQLRAEL
     PHLPVIGHCR NQAVSHYLTH WLDYPHLPYS PE
//