(data stored in ACNUC7421 zone)

SWISSPROT: COF_ECO57

ID   COF_ECO57               Reviewed;         272 AA.
AC   Q8XE50; Q7AGZ5;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   05-JUL-2017, entry version 99.
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=Z0553, ECs0500;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the hydrolysis of 4-amino-2-methyl-5-
CC       hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2-
CC       methyl-5-hydroxymethylpyrimidine phosphate (HMP-P).
CC       {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
CC       family. {ECO:0000255|HAMAP-Rule:MF_01847}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG54796.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=BAB33923.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; AE005174; AAG54796.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB33923.1; ALT_INIT; Genomic_DNA.
DR   PIR; D90691; D90691.
DR   PIR; H85541; H85541.
DR   RefSeq; NP_308527.1; NC_002695.1.
DR   RefSeq; WP_001301796.1; NZ_MWVM01000009.1.
DR   ProteinModelPortal; Q8XE50; -.
DR   SMR; Q8XE50; -.
DR   STRING; 155864.Z0553; -.
DR   EnsemblBacteria; AAG54796; AAG54796; Z0553.
DR   EnsemblBacteria; BAB33923; BAB33923; BAB33923.
DR   GeneID; 914602; -.
DR   KEGG; ece:Z0553; -.
DR   KEGG; ecs:ECs0500; -.
DR   PATRIC; fig|386585.9.peg.603; -.
DR   eggNOG; ENOG4108AZI; Bacteria.
DR   eggNOG; COG0561; LUCA.
DR   HOGENOM; HOG000184784; -.
DR   KO; K11938; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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; 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; IPR023214; HAD-like_dom.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023938; HMP-PP_phosphatase.
DR   PANTHER; PTHR10000:SF35; PTHR10000:SF35; 1.
DR   Pfam; PF08282; Hydrolase_3; 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;
DR   PRODOM; Q8XE50.
DR   SWISS-2DPAGE; Q8XE50.
KW   Complete proteome; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN         1    272       HMP-PP phosphatase.
FT                                /FTId=PRO_0000342982.
FT   ACT_SITE      8      8       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_01847}.
FT   METAL         8      8       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01847}.
FT   METAL        10     10       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01847}.
FT   METAL       212    212       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01847}.
SQ   SEQUENCE   272 AA;  30303 MW;  C6B3B2E5A845BEAD CRC64;
     MARLAAFDMD GTLLMPDHHL GEKTLSTLAR LRERDITLTF ATGRHALEMQ HILGAISLDA
     YLITGNGTRV HSLEGELLHR DDLPADVAEL VLYQQWDTRA SMHIFNDDGW FTGKEIPALL
     QAFVYSGFRY QIIDVKKMPL GSVTKICFCG DHDDLTRLQI QLHEALGERA HLCFSATDCL
     EVLPVGCNKG AALTVLTQHL GLSLRDCMAF GDAMNDREML GSVGSGFIMG NAMPQLRAEL
     PHLPVIGHCR NQAVSHYLTH WLDYPHLPYS PE
//

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