NUDB_HAEIN
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 03-AUG-2022, entry version 108.
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; Proteobacteria; 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 RefSeq; WP_005694349.1; 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 OMA; NTEHVFG; -.
DR PhylomeDB; P44635; -.
DR Proteomes; UP000000579; 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..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
