GenomeNet

Database: UniProt
Entry: P0AFC0
LinkDB: P0AFC0
Original site: P0AFC0 
ID   NUDB_ECOLI              Reviewed;         150 AA.
AC   P0AFC0; P24236;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Dihydroneopterin triphosphate diphosphatase;
DE            EC=3.6.1.67 {ECO:0000269|PubMed:8798731};
DE   AltName: Full=Dihydroneopterin triphosphate pyrophosphatase;
DE   AltName: Full=dATP pyrophosphohydrolase;
GN   Name=nudB; Synonyms=ntpA; OrderedLocusNames=b1865, JW1854;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1657895; DOI=10.1128/jb.173.23.7711-7715.1991;
RA   Sharples G.J., Lloyd R.G.;
RT   "Resolution of Holliday junctions in Escherichia coli: identification of
RT   the ruvC gene product as a 19-kilodalton protein.";
RL   J. Bacteriol. 173:7711-7715(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1885548; DOI=10.1128/jb.173.18.5747-5753.1991;
RA   Takahagi M., Iwasaki H., Nakata A., Shinagawa H.;
RT   "Molecular analysis of the Escherichia coli ruvC gene, which encodes a
RT   Holliday junction-specific endonuclease.";
RL   J. Bacteriol. 173:5747-5753(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   CHARACTERIZATION.
RX   PubMed=8163538; DOI=10.1016/s0021-9258(17)32721-7;
RA   Bullions L.C., Mejean V., Claverys J.-P., Bessman M.J.;
RT   "Purification of the MutX protein of Streptococcus pneumoniae, a homologue
RT   of Escherichia coli MutT. Identification of a novel catalytic domain for
RT   nucleoside triphosphate pyrophosphohydrolase activity.";
RL   J. Biol. Chem. 269:12339-12344(1994).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND COFACTOR.
RX   PubMed=8798731; DOI=10.1074/jbc.271.40.24649;
RA   O'Handley S.F., Frick D.N., Bullions L.C., Mildvan A.S., Bessman M.J.;
RT   "Escherichia coli orf17 codes for a nucleoside triphosphate
RT   pyrophosphohydrolase member of the MutT family of proteins. Cloning,
RT   purification, and characterization of the enzyme.";
RL   J. Biol. Chem. 271:24649-24654(1996).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH PYROPHOSPHATE AND
RP   SAMARIUM IONS, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=17698004; DOI=10.1016/j.str.2007.06.018;
RA   Gabelli S.B., Bianchet M.A., Xu W., Dunn C.A., Niu Z.-D., Amzel L.M.,
RA   Bessman M.J.;
RT   "Structure and function of the E. coli dihydroneopterin triphosphate
RT   pyrophosphatase: a Nudix enzyme involved in folate biosynthesis.";
RL   Structure 15:1014-1022(2007).
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. {ECO:0000269|PubMed:17698004,
CC       ECO:0000269|PubMed:8798731}.
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:0000269|PubMed:8798731};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:8798731};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:8798731};
CC   -!- ACTIVITY REGULATION: Subject to product inhibition by pyrophosphate.
CC       {ECO:0000269|PubMed:8798731}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.27 mM for dihydroneopterin triphosphate
CC         {ECO:0000269|PubMed:17698004, ECO:0000269|PubMed:8798731};
CC         KM=0.79 mM for dATP {ECO:0000269|PubMed:17698004,
CC         ECO:0000269|PubMed:8798731};
CC       pH dependence:
CC         Optimum pH is 8.5-9. {ECO:0000269|PubMed:17698004,
CC         ECO:0000269|PubMed:8798731};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X59551; CAA42124.1; -; Genomic_DNA.
DR   EMBL; D10165; BAA01029.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74935.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15676.1; -; Genomic_DNA.
DR   PIR; B38113; B38113.
DR   RefSeq; NP_416379.1; NC_000913.3.
DR   RefSeq; WP_001300367.1; NZ_SSZK01000001.1.
DR   PDB; 2O1C; X-ray; 1.80 A; A/B/C/D=1-150.
DR   PDB; 2O5W; X-ray; 2.60 A; A/B/C/D=1-150.
DR   PDB; 5U7E; X-ray; 1.94 A; A=1-150.
DR   PDB; 5U7F; X-ray; 1.79 A; A=1-150.
DR   PDB; 5U7H; X-ray; 2.00 A; A=1-150.
DR   PDBsum; 2O1C; -.
DR   PDBsum; 2O5W; -.
DR   PDBsum; 5U7E; -.
DR   PDBsum; 5U7F; -.
DR   PDBsum; 5U7H; -.
DR   AlphaFoldDB; P0AFC0; -.
DR   SMR; P0AFC0; -.
DR   BioGRID; 4260348; 315.
DR   DIP; DIP-10372N; -.
DR   IntAct; P0AFC0; 7.
DR   STRING; 511145.b1865; -.
DR   PaxDb; 511145-b1865; -.
DR   EnsemblBacteria; AAC74935; AAC74935; b1865.
DR   GeneID; 75202729; -.
DR   GeneID; 946383; -.
DR   KEGG; ecj:JW1854; -.
DR   KEGG; eco:b1865; -.
DR   PATRIC; fig|511145.12.peg.1944; -.
DR   EchoBASE; EB1128; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_128620_0_0_6; -.
DR   InParanoid; P0AFC0; -.
DR   OMA; VTRNTEH; -.
DR   OrthoDB; 7066556at2; -.
DR   PhylomeDB; P0AFC0; -.
DR   BioCyc; EcoCyc:H2NEOPTERINP3PYROPHOSPHOHYDRO-MONOMER; -.
DR   BioCyc; MetaCyc:H2NEOPTERINP3PYROPHOSPHOHYDRO-MONOMER; -.
DR   BRENDA; 3.6.1.67; 2026.
DR   EvolutionaryTrace; P0AFC0; -.
DR   PRO; PR:P0AFC0; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0008828; F:dATP diphosphatase activity; IDA:EcoCyc.
DR   GO; GO:0019177; F:dihydroneopterin triphosphate pyrophosphohydrolase activity; IDA:EcoCyc.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IMP:EcoCyc.
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   1: Evidence at protein level;
KW   3D-structure; Folate biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..150
FT                   /note="Dihydroneopterin triphosphate diphosphatase"
FT                   /id="PRO_0000056952"
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   BINDING         29
FT                   /ligand="substrate"
FT   BINDING         40
FT                   /ligand="substrate"
FT   BINDING         56
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         60
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   STRAND          9..18
FT                   /evidence="ECO:0007829|PDB:5U7F"
FT   TURN            19..21
FT                   /evidence="ECO:0007829|PDB:5U7F"
FT   STRAND          23..32
FT                   /evidence="ECO:0007829|PDB:5U7F"
FT   STRAND          36..42
FT                   /evidence="ECO:0007829|PDB:5U7F"
FT   HELIX           49..61
FT                   /evidence="ECO:0007829|PDB:5U7F"
FT   TURN            65..69
FT                   /evidence="ECO:0007829|PDB:5U7F"
FT   STRAND          72..82
FT                   /evidence="ECO:0007829|PDB:5U7F"
FT   HELIX           85..90
FT                   /evidence="ECO:0007829|PDB:5U7F"
FT   STRAND          97..109
FT                   /evidence="ECO:0007829|PDB:5U7F"
FT   STRAND          116..125
FT                   /evidence="ECO:0007829|PDB:5U7F"
FT   HELIX           126..132
FT                   /evidence="ECO:0007829|PDB:5U7F"
FT   HELIX           136..145
FT                   /evidence="ECO:0007829|PDB:5U7F"
SQ   SEQUENCE   150 AA;  17306 MW;  B4F05FA056F3BA07 CRC64;
     MKDKVYKRPV SILVVIYAQD TKRVLMLQRR DDPDFWQSVT GSVEEGETAP QAAMREVKEE
     VTIDVVAEQL TLIDCQRTVE FEIFSHLRHR YAPGVTRNTE SWFCLALPHE RQIVFTEHLA
     YKWLDAPAAA ALTKSWSNRQ AIEQFVINAA
//
DBGET integrated database retrieval system