ID   NUDB_HAEIN              Reviewed;         158 AA.
AC   P44635;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 114.
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; Synonyms=ntpA; OrderedLocusNames=HI_0316;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC21980.1; -; Genomic_DNA.
DR   PIR; H64147; H64147.
DR   RefSeq; NP_438482.2; NC_000907.1.
DR   AlphaFoldDB; P44635; -.
DR   SMR; P44635; -.
DR   STRING; 71421.HI_0316; -.
DR   EnsemblBacteria; AAC21980; AAC21980; HI_0316.
DR   KEGG; hin:HI_0316; -.
DR   PATRIC; fig|71421.8.peg.333; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_128620_0_0_6; -.
DR   OrthoDB; 7066556at2; -.
DR   PhylomeDB; P44635; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0008828; F:dATP diphosphatase activity; IEA:InterPro.
DR   GO; GO:0019177; F:dihydroneopterin triphosphate pyrophosphohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd04664; Nudix_Hydrolase_7; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
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   PANTHER; PTHR43736; ADP-RIBOSE PYROPHOSPHATASE; 1.
DR   PANTHER; PTHR43736:SF4; DIHYDRONEOPTERIN TRIPHOSPHATE DIPHOSPHATASE; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR01404; NPPPHYDRLASE.
DR   SUPFAM; SSF55811; Nudix; 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..158
FT                   /note="Dihydroneopterin triphosphate diphosphatase"
FT                   /id="PRO_0000056955"
FT   DOMAIN          14..153
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           48..69
FT                   /note="Nudix box"
FT   BINDING         14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         88..91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         124
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   158 AA;  18826 MW;  A82B3750A5631553 CRC64;
     MRSDLTAFLM MQYKNNQSVL VVIYTKDTNR VLMLQRQDDP DFWQSVTGTI ESDETPKKTA
     IRELWEEVRL DISENSTALF DCNESIEFEI FPHFRYKYAP NITHCKEHWF LCEVEKEFIP
     VLSEHLDFCW VSAKKAVEMT KSQNNAEAIK KYLFNLRR
//