COF_ECOLI
ID COF_ECOLI Reviewed; 272 AA.
AC P46891; P71208; P77198; Q2MBY0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 148.
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};
GN OrderedLocusNames=b0446, JW0436;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RA Patzer S.I., Hantke K.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Hatada E., Ohmori H., Qiao Y., Tsuji M., Fukuda R.;
RT "Nucleotide sequence analysis of the E. coli chromosome around the 10.0 min
RT region.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION AS A HMP-PP PHOSPHATASE, CATALYTIC ACTIVITY, AND ROLE IN
RP ANTIBIOTIC RESISTANCE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15292217; DOI=10.1074/jbc.m404284200;
RA Lawhorn B.G., Gerdes S.Y., Begley T.P.;
RT "A genetic screen for the identification of thiamin metabolic genes.";
RL J. Biol. Chem. 279:43555-43559(2004).
RN [7]
RP FUNCTION AS A PHOSPHATASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND COFACTOR.
RX PubMed=16990279; DOI=10.1074/jbc.m605449200;
RA Kuznetsova E., Proudfoot M., Gonzalez C.F., Brown G., Omelchenko M.V.,
RA Borozan I., Carmel L., Wolf Y.I., Mori H., Savchenko A.V., Arrowsmith C.H.,
RA Koonin E.V., Edwards A.M., Yakunin A.F.;
RT "Genome-wide analysis of substrate specificities of the Escherichia coli
RT haloacid dehalogenase-like phosphatase family.";
RL J. Biol. Chem. 281:36149-36161(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). Can also hydrolyze other
CC substrates such as MeO-HMP-PP and 4-amino-2-trifluoromethyl 5-
CC hydroxymethylpyrimidine pyrophosphate (CF3-HMP-PP) to give MeO-HMP-P
CC and 4-amino-2-trifluoromethyl-5-hydroxymethylpyrimidine phosphate. This
CC hydrolysis generates resistance to the antibiotics (bacimethrin, CF3-
CC HMP) by reducing the formation of their toxic forms, 2'-methoxythiamin
CC pyrophosphate (MeO-TPP) and CF3-HMP-PP. Also hydrolyzes pyridoxal-
CC phosphate (PLP) and flavin mononucleotide (FMN), and purines (GMP and
CC IMP) as secondary substrates. {ECO:0000255|HAMAP-Rule:MF_01847,
CC ECO:0000269|PubMed:15292217, ECO:0000269|PubMed:16990279}.
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:0000269|PubMed:15292217};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01847,
CC ECO:0000269|PubMed:16990279};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01847,
CC ECO:0000269|PubMed:16990279};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01847,
CC ECO:0000269|PubMed:16990279};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01847,
CC ECO:0000269|PubMed:16990279};
CC Note=Magnesium. Can also use other divalent metal cations as manganese,
CC cobalt or zinc. {ECO:0000255|HAMAP-Rule:MF_01847,
CC ECO:0000269|PubMed:16990279};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.68 mM for PLP (with magnesium ions as cofactor and at pH 9)
CC {ECO:0000269|PubMed:16990279};
CC KM=2.5 mM for 2-deoxyglucose-6-P (with magnesium ions as cofactor and
CC at pH 9) {ECO:0000269|PubMed:16990279};
CC pH dependence:
CC Optimum pH is between 6 and 7.5. {ECO:0000269|PubMed:16990279};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family.
CC {ECO:0000255|HAMAP-Rule:MF_01847}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40202.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA91181.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z54355; CAA91181.1; ALT_INIT; Genomic_DNA.
DR EMBL; D82943; BAA11650.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40202.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73549.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76226.1; -; Genomic_DNA.
DR PIR; F64774; F64774.
DR RefSeq; NP_414980.2; NC_000913.3.
DR RefSeq; WP_001336137.1; NZ_LN832404.1.
DR AlphaFoldDB; P46891; -.
DR SMR; P46891; -.
DR BioGRID; 4260651; 7.
DR IntAct; P46891; 1.
DR STRING; 511145.b0446; -.
DR PaxDb; P46891; -.
DR PRIDE; P46891; -.
DR DNASU; 945089; -.
DR EnsemblBacteria; AAC73549; AAC73549; b0446.
DR EnsemblBacteria; BAE76226; BAE76226; BAE76226.
DR GeneID; 945089; -.
DR KEGG; ecj:JW0436; -.
DR KEGG; eco:b0446; -.
DR PATRIC; fig|1411691.4.peg.1830; -.
DR EchoBASE; EB3007; -.
DR eggNOG; COG0561; Bacteria.
DR HOGENOM; CLU_044146_5_2_6; -.
DR InParanoid; P46891; -.
DR OMA; MPDHRLG; -.
DR PhylomeDB; P46891; -.
DR BioCyc; EcoCyc:G6246-MON; -.
DR BioCyc; MetaCyc:G6246-MON; -.
DR PRO; PR:P46891; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0002145; F:4-amino-5-hydroxymethyl-2-methylpyrimidine diphosphatase activity; IEA:RHEA.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IDA:EcoliWiki.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR GO; GO:0017001; P:antibiotic catabolic process; IDA:UniProtKB.
DR GO; GO:0009228; P:thiamine biosynthetic process; IMP:EcoliWiki.
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 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..272
FT /note="HMP-PP phosphatase"
FT /id="PRO_0000054418"
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"
FT CONFLICT 173
FT /note="C -> S (in Ref. 2; BAA11650)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 272 AA; 30371 MW; D8FC034BF81E41AC CRC64;
MARLAAFDMD GTLLMPDHHL GEKTLSTLAR LRERDITLTF ATGRHALEMQ HILGALSLDA
YLITGNGTRV HSLEGELLHR DDLPADVAEL VLYQQWDTRA SMHIFNDDGW FTGKEIPALL
QAFVYSGFRY QIIDVKKMPL GSVTKICFCG DHDDLTRLQI QLYEALGERA HLCFSATDCL
EVLPVGCNKG AALTVLTQHL GLSLRDCMAF GDAMNDREML VSVGSGFIMG NAMPQLRAEL
PHLPVIGHCR NQAVSHYLTH WLDYPHLPYS PE
