(data stored in SCRATCH zone)

SWISSPROT: ADPP_BACSU

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   11-DEC-2019, entry version 129.
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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 = AMP + D-ribose 5-phosphate + 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}.
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; NZ_JNCM01000036.1.
DR   SMR; P54570; -.
DR   STRING; 224308.BSU23610; -.
DR   PaxDb; P54570; -.
DR   PRIDE; P54570; -.
DR   EnsemblBacteria; CAB14293; CAB14293; BSU23610.
DR   GeneID; 938719; -.
DR   KEGG; bsu:BSU23610; -.
DR   PATRIC; fig|224308.179.peg.2573; -.
DR   eggNOG; ENOG4108YZ4; Bacteria.
DR   eggNOG; COG0494; LUCA.
DR   HOGENOM; HOG000045854; -.
DR   InParanoid; P54570; -.
DR   KO; K01515; -.
DR   OMA; LRQYRFA; -.
DR   PhylomeDB; P54570; -.
DR   BioCyc; BSUB:BSU23610-MONOMER; -.
DR   BRENDA; 3.6.1.13; 658.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006753; P:nucleoside phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0019693; P:ribose phosphate metabolic process; IBA:GO_Central.
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   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P54570.
DR   SWISS-2DPAGE; P54570.
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   REGION          14..15
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          37..38
FT                   /note="Substrate binding; shared with dimeric partner"
FT                   /evidence="ECO:0000250"
FT   REGION          113..115
FT                   /note="Substrate binding; shared with dimeric partner"
FT                   /evidence="ECO:0000250"
FT   MOTIF           77..98
FT                   /note="Nudix box"
FT   ACT_SITE        140
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   METAL           76
FT                   /note="Magnesium 1; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   METAL           92
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000250"
FT   METAL           92
FT                   /note="Magnesium 3"
FT                   /evidence="ECO:0000250"
FT   METAL           96
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000250"
FT   METAL           96
FT                   /note="Magnesium 3"
FT                   /evidence="ECO:0000250"
FT   METAL           142
FT                   /note="Magnesium 3"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /note="Substrate"
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
//

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