(data stored in ACNUC7421 zone)

SWISSPROT: COF_ECODH

ID   COF_ECODH               Reviewed;         272 AA.
AC   B1XFN4;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 61.
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=ECDH10B_0402;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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}.
DR   EMBL; CP000948; ACB01574.1; -; Genomic_DNA.
DR   RefSeq; WP_001336137.1; NC_010473.1.
DR   ProteinModelPortal; B1XFN4; -.
DR   SMR; B1XFN4; -.
DR   EnsemblBacteria; ACB01574; ACB01574; ECDH10B_0402.
DR   KEGG; ecd:ECDH10B_0402; -.
DR   eggNOG; ENOG4108AZI; Bacteria.
DR   eggNOG; COG0561; LUCA.
DR   HOGENOM; HOG000184784; -.
DR   KO; K11938; -.
DR   OMA; MPDHRLG; -.
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; B1XFN4.
DR   SWISS-2DPAGE; B1XFN4.
KW   Hydrolase; Magnesium; Metal-binding.
FT   CHAIN         1    272       HMP-PP phosphatase.
FT                                /FTId=PRO_0000342978.
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;  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
//

If you have problems or comments...

PBIL Back to PBIL home page