ID   NTPNH_BIFLO             Reviewed;         482 AA.
AC   Q8G4U8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Nucleoside triphosphate pyrophosphatase/Nudix hydrolase fusion protein;
DE   Includes:
DE     RecName: Full=Nucleoside triphosphate pyrophosphatase {ECO:0000305};
DE              EC=3.6.1.9 {ECO:0000250|UniProtKB:P25536};
DE     AltName: Full=Nucleotide pyrophosphatase {ECO:0000305};
DE              Short=Nucleotide PPase {ECO:0000305};
DE   Includes:
DE     RecName: Full=Nudix hydrolase {ECO:0000305};
GN   OrderedLocusNames=BL1276;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
CC   -!- FUNCTION: Nucleoside triphosphate pyrophosphatase. May have a dual role
CC       in cell division arrest and in preventing the incorporation of modified
CC       nucleotides into cellular nucleic acids. {ECO:0000255|HAMAP-
CC       Rule:MF_00528}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-
CC         deoxyribonucleoside 5'-phosphate + diphosphate + H(+);
CC         Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00528,
CC       ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the Maf family.
CC       {ECO:0000305}.
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DR   EMBL; AE014295; AAN25077.1; -; Genomic_DNA.
DR   RefSeq; NP_696441.1; NC_004307.2.
DR   RefSeq; WP_011068714.1; NC_004307.2.
DR   AlphaFoldDB; Q8G4U8; -.
DR   SMR; Q8G4U8; -.
DR   STRING; 206672.BL1276; -.
DR   EnsemblBacteria; AAN25077; AAN25077; BL1276.
DR   KEGG; blo:BL1276; -.
DR   PATRIC; fig|206672.9.peg.1563; -.
DR   HOGENOM; CLU_040416_1_2_11; -.
DR   OMA; ECYGKPH; -.
DR   Proteomes; UP000000439; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0036218; F:dTTP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00555; Maf; 1.
DR   Gene3D; 3.90.950.10; -; 1.
DR   HAMAP; MF_00528; Maf; 1.
DR   InterPro; IPR029001; ITPase-like_fam.
DR   InterPro; IPR003697; Maf-like.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   PANTHER; PTHR43213; PTHR43213; 1.
DR   Pfam; PF02545; Maf; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF52972; SSF52972; 2.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Nucleotide metabolism; Reference proteome.
FT   CHAIN           1..482
FT                   /note="Nucleoside triphosphate pyrophosphatase/Nudix
FT                   hydrolase fusion protein"
FT                   /id="PRO_0000267256"
FT   DOMAIN          338..475
FT                   /note="Nudix hydrolase"
FT   REGION          1..299
FT                   /note="Maf-like"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
SQ   SEQUENCE   482 AA;  51515 MW;  2BF4859C7FC1FA17 CRC64;
     MSIPLILASK SKPRRDVLYS AGICPTIRVS HVDEPAALEA AAREEGVTVD DLSIKQRVMI
     LAVAKAEAVH RAYRDVADTA AAATGDRVIA YPLKAKEIKD SEREAAVEDL REAAAGKPID
     YSKAEIATTR DFSGIDMPTV TEPIATAIAG QPGLTEATVG PLILGCDSMF LLGGECYGKP
     HSEAVASERL KRMSGATGEL WTGHCLIDFA TGRTVRGASH AKVHFGEFTD ADVERYIATG
     EPLEVAGSFT LEGFGGAFID SIEGDPHGII GLSLPLARHL AGELGITWTD LWNVGRGELE
     PESKASGNQH AGILPPVENV HQPGDGWVDC ACGRKHWGTN GASGILLARR DPVSGKVTHV
     VMQHRAAWSA EGGTWGIPGG ATADGESPIE GALRESYEEA NITPEDIEVV GSYREDHGPW
     AYTTVFAFEK PGHTVEPKAN DDESMEICWV PIDDVPNRKL LTAMKTDWPR FAARLDELAT
     AQ