NUDB_SHIFL
ID NUDB_SHIFL Reviewed; 150 AA.
AC P0AFC2; P24236;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=SF1875, S1941;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN43431.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP17255.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN43431.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP17255.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_707724.2; NC_004337.2.
DR RefSeq; WP_001300367.1; NZ_UIQL01000048.1.
DR AlphaFoldDB; P0AFC2; -.
DR SMR; P0AFC2; -.
DR STRING; 198214.SF1875; -.
DR EnsemblBacteria; AAN43431; AAN43431; SF1875.
DR EnsemblBacteria; AAP17255; AAP17255; S1941.
DR GeneID; 1025022; -.
DR GeneID; 58389836; -.
DR KEGG; sfl:SF1875; -.
DR KEGG; sfx:S1941; -.
DR PATRIC; fig|198214.7.peg.2235; -.
DR HOGENOM; CLU_128620_0_0_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000056954"
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
