NUDB_ECO57
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 03-AUG-2022, entry version 90.
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., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA 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., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Catalyzes the hydrolysis of dihydroneopterin triphosphate to
CC dihydroneopterin monophosphate and pyrophosphate. Required for
CC efficient folate biosynthesis. Can also hydrolyze nucleoside
CC triphosphates with a preference for dATP.
CC {ECO:0000250|UniProtKB:P0AFC0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin 3'-triphosphate + H2O = 7,8-
CC dihydroneopterin 3'-phosphate + diphosphate + H(+);
CC Xref=Rhea:RHEA:25302, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58462, ChEBI:CHEBI:58762; EC=3.6.1.67;
CC Evidence={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. {ECO:0000250|UniProtKB:P0AFC0};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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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 RefSeq; WP_001300367.1; NZ_SDVX01000009.1.
DR AlphaFoldDB; P0AFC1; -.
DR SMR; P0AFC1; -.
DR STRING; 155864.EDL933_2839; -.
DR EnsemblBacteria; AAG56855; AAG56855; Z2917.
DR EnsemblBacteria; BAB35998; BAB35998; ECs_2575.
DR GeneID; 58389836; -.
DR GeneID; 914189; -.
DR KEGG; ece:Z2917; -.
DR KEGG; ecs:ECs_2575; -.
DR PATRIC; fig|386585.9.peg.2699; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_128620_0_0_6; -.
DR OMA; NTEHVFG; -.
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 InterPro; IPR003564; DHNTPase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
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 Folate biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..150
FT /note="Dihydroneopterin triphosphate diphosphatase"
FT /id="PRO_0000056953"
FT DOMAIN 5..146
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 41..62
FT /note="Nudix box"
FT BINDING 7
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 81..84
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 150 AA; 17306 MW; B4F05FA056F3BA07 CRC64;
MKDKVYKRPV SILVVIYAQD TKRVLMLQRR DDPDFWQSVT GSVEEGETAP QAAMREVKEE
VTIDVVAEQL TLIDCQRTVE FEIFSHLRHR YAPGVTRNTE SWFCLALPHE RQIVFTEHLA
YKWLDAPAAA ALTKSWSNRQ AIEQFVINAA
