ID NUDB_ECO57 Reviewed; 150 AA.
AC P0AFC1; P24236;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 02-NOV-2016, entry version 66.
DE RecName: Full=Dihydroneopterin triphosphate diphosphatase;
DE EC=3.6.1.67;
DE AltName: Full=Dihydroneopterin triphosphate pyrophosphatase;
DE AltName: Full=dATP pyrophosphohydrolase;
GN Name=nudB; OrderedLocusNames=Z2917, ECs2575;
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 dihydroneopterin
CC triphosphate to dihydroneopterin monophosphate and pyrophosphate.
CC Required for efficient folate biosynthesis. Can also hydrolyze
CC nucleoside triphosphates with a preference for dATP.
CC {ECO:0000250|UniProtKB:P0AFC0}.
CC -!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin 3'-triphosphate + H(2)O =
CC 7,8-dihydroneopterin 3'-phosphate + diphosphate.
CC {ECO:0000250|UniProtKB:P0AFC0}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0AFC0};
CC Note=Binds 1 Mg(2+) ion per subunit.
CC {ECO:0000250|UniProtKB:P0AFC0};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 nudix hydrolase domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00794}.
DR EMBL; AE005174; AAG56855.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35998.1; -; Genomic_DNA.
DR PIR; C85799; C85799.
DR PIR; G90950; G90950.
DR RefSeq; NP_310602.1; NC_002695.1.
DR ProteinModelPortal; P0AFC1; -.
DR SMR; P0AFC1; -.
DR STRING; 155864.Z2917; -.
DR EnsemblBacteria; AAG56855; AAG56855; Z2917.
DR EnsemblBacteria; BAB35998; BAB35998; BAB35998.
DR GeneID; 914189; -.
DR KEGG; ece:Z2917; -.
DR KEGG; ecs:ECs2575; -.
DR PATRIC; 18354522; VBIEscCol44059_2472.
DR eggNOG; ENOG4108TIT; Bacteria.
DR eggNOG; COG0494; LUCA.
DR HOGENOM; HOG000264405; -.
DR KO; K08310; -.
DR OMA; VTRNTEH; -.
DR BioCyc; ECOO157:Z2917-MONOMER; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0008828; F:dATP pyrophosphohydrolase activity; IEA:InterPro.
DR GO; GO:0019177; F:dihydroneopterin triphosphate pyrophosphohydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.79.10; -; 1.
DR InterPro; IPR003564; DHNTPase.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR015797; NUDIX_hydrolase_dom-like.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR01404; NPPPHYDRLASE.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Complete proteome; Folate biosynthesis; Hydrolase; Magnesium;
KW Metal-binding.
FT CHAIN 1 150 Dihydroneopterin triphosphate
FT diphosphatase.
FT /FTId=PRO_0000056953.
FT DOMAIN 5 146 Nudix hydrolase. {ECO:0000255|PROSITE-
FT ProRule:PRU00794}.
FT REGION 81 84 Substrate binding. {ECO:0000255}.
FT MOTIF 41 62 Nudix box.
FT METAL 56 56 Magnesium. {ECO:0000250}.
FT METAL 60 60 Magnesium. {ECO:0000250}.
FT METAL 117 117 Magnesium. {ECO:0000250}.
FT BINDING 7 7 Substrate. {ECO:0000250}.
FT BINDING 29 29 Substrate. {ECO:0000250}.
FT BINDING 40 40 Substrate. {ECO:0000250}.
FT BINDING 135 135 Substrate. {ECO:0000255}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 8 144 ipfam:NUDIX [T]
FT MYHIT 5 146 iprf:NUDIX [T]
FT MYHIT 41 62 ipat:NUDIX_BOX [T]
SQ SEQUENCE 150 AA; 17306 MW; B4F05FA056F3BA07 CRC64;
MKDKVYKRPV SILVVIYAQD TKRVLMLQRR DDPDFWQSVT GSVEEGETAP QAAMREVKEE
VTIDVVAEQL TLIDCQRTVE FEIFSHLRHR YAPGVTRNTE SWFCLALPHE RQIVFTEHLA
YKWLDAPAAA ALTKSWSNRQ AIEQFVINAA
//
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