ID   ADPP_BACSU              Reviewed;         185 AA.
AC   P54570;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 152.
DE   RecName: Full=ADP-ribose pyrophosphatase;
DE            EC=3.6.1.13;
DE   AltName: Full=ADP-ribose diphosphatase;
DE   AltName: Full=ADP-ribose phosphohydrolase;
DE            Short=ASPPase;
DE   AltName: Full=Adenosine diphosphoribose pyrophosphatase;
DE            Short=ADPR-PPase;
GN   Name=nudF; Synonyms=yqkG; OrderedLocusNames=BSU23610;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=10542272; DOI=10.1074/jbc.274.45.32318;
RA   Dunn C.A., O'Handley S.F., Frick D.N., Bessman M.J.;
RT   "Studies on the ADP-ribose pyrophosphatase subfamily of the nudix
RT   hydrolases and tentative identification of trgB, a gene associated with
RT   tellurite resistance.";
RL   J. Biol. Chem. 274:32318-32324(1999).
CC   -!- FUNCTION: Acts on ADP-mannose and ADP-glucose as well as ADP-ribose.
CC       Prevents glycogen biosynthesis. The reaction catalyzed by this enzyme
CC       is a limiting step of the gluconeogenic process (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-D-ribose + H2O = D-ribose 5-phosphate + AMP + 2 H(+);
CC         Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215;
CC         EC=3.6.1.13;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudF subfamily.
CC       {ECO:0000305}.
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DR   EMBL; D84432; BAA12639.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14293.1; -; Genomic_DNA.
DR   PIR; A69967; A69967.
DR   RefSeq; NP_390242.1; NC_000964.3.
DR   RefSeq; WP_004398600.1; NC_000964.3.
DR   AlphaFoldDB; P54570; -.
DR   SMR; P54570; -.
DR   FunCoup; P54570; 536.
DR   STRING; 224308.BSU23610; -.
DR   PaxDb; 224308-BSU23610; -.
DR   EnsemblBacteria; CAB14293; CAB14293; BSU_23610.
DR   GeneID; 938719; -.
DR   KEGG; bsu:BSU23610; -.
DR   PATRIC; fig|224308.179.peg.2573; -.
DR   eggNOG; COG0494; Bacteria.
DR   InParanoid; P54570; -.
DR   OrthoDB; 9806150at2; -.
DR   PhylomeDB; P54570; -.
DR   BioCyc; BSUB:BSU23610-MONOMER; -.
DR   BRENDA; 3.6.1.13; 658.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P54570; -.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019693; P:ribose phosphate metabolic process; IBA:GO_Central.
DR   CDD; cd03424; NUDIX_ADPRase_Nudt5_UGPPase_Nudt14; 1.
DR   FunFam; 3.90.79.10:FF:000024; ADP-ribose pyrophosphatase; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR020476; Nudix_hydrolase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   PANTHER; PTHR11839:SF18; NUDIX HYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11839; UDP/ADP-SUGAR PYROPHOSPHATASE; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..185
FT                   /note="ADP-ribose pyrophosphatase"
FT                   /id="PRO_0000057041"
FT   DOMAIN          40..171
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           77..98
FT                   /note="Nudix box"
FT   ACT_SITE        140
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         14..15
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         37..38
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         113..115
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   185 AA;  20980 MW;  E9C7088B525813A3 CRC64;
     MKSLEEKTIA KEQIFSGKVI DLYVEDVELP NGKASKREIV KHPGAVAVLA VTDEGKIIMV
     KQFRKPLERT IVEIPAGKLE KGEEPEYTAL RELEEETGYT AKKLTKITAF YTSPGFADEI
     VHVFLAEELS VLEEKRELDE DEFVEVMEVT LEDALKLVES REVYDAKTAY AIQYLQLKEA
     LQAQK
//