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COF_CITK8
ID   COF_CITK8               Reviewed;         272 AA.
AC   A8AK07;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 79.
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=CKO_02714;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABV13820.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000822; ABV13820.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_024130593.1; NC_009792.1.
DR   AlphaFoldDB; A8AK07; -.
DR   SMR; A8AK07; -.
DR   STRING; 290338.CKO_02714; -.
DR   EnsemblBacteria; ABV13820; ABV13820; CKO_02714.
DR   GeneID; 45136569; -.
DR   KEGG; cko:CKO_02714; -.
DR   HOGENOM; CLU_044146_5_2_6; -.
DR   OrthoDB; 1374424at2; -.
DR   Proteomes; UP000008148; 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; Reference proteome.
FT   CHAIN           1..272
FT                   /note="HMP-PP phosphatase"
FT                   /id="PRO_0000342974"
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;  30204 MW;  95F4D45826013AA2 CRC64;
     MARLAAFDMD GTLLMPNHHL GHETLATLAR LRERDITLTF ATGRHVLEMR HILGAISMDA
     FLITGNGTRI HSQEGDMLHR QDLDPAIADR VLHQAWDTRA SMHVFNDNGW FTGSAIPALL
     QAHVYSGFHY QIVDVKRIPA HQVTKICFCG DHDDLIRLRI QLNEALGERA NLCFSAVDCL
     EVLPLGCNKG SALAVLSDHL GLSLTECMAF GDAMNDREML ESVGRGLIMG NAMPQLIAEL
     PHLSVIGHCR NQAVSHFLTH WLDNPHLPYS PE
 
 
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