ID   B6IMI8_RHOCS            Unreviewed;       213 AA.
AC   B6IMI8;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=ADP-ribose pyrophosphatase {ECO:0000256|ARBA:ARBA00013297};
DE            EC=3.6.1.13 {ECO:0000256|ARBA:ARBA00012453};
DE   AltName: Full=ADP-ribose diphosphatase {ECO:0000256|ARBA:ARBA00030162};
DE   AltName: Full=ADP-ribose phosphohydrolase {ECO:0000256|ARBA:ARBA00033056};
DE   AltName: Full=Adenosine diphosphoribose pyrophosphatase {ECO:0000256|ARBA:ARBA00030308};
GN   OrderedLocusNames=RC1_1151 {ECO:0000313|EMBL:ACI98567.1};
OS   Rhodospirillum centenum (strain ATCC 51521 / SW).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=414684 {ECO:0000313|EMBL:ACI98567.1, ECO:0000313|Proteomes:UP000001591};
RN   [1] {ECO:0000313|Proteomes:UP000001591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RA   Touchman J.W., Bauer C., Blankenship R.E.;
RT   "Genome sequence of Rhodospirillum centenum.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACI98567.1, ECO:0000313|Proteomes:UP000001591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RX   PubMed=20500872; DOI=10.1186/1471-2164-11-325;
RA   Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D., Chowdhury S.R.,
RA   Hao J., Helmy T., Kim S., Kurdoglu A.A., Matthies H.J., Rollo D.,
RA   Stothard P., Blankenship R.E., Bauer C.E., Touchman J.W.;
RT   "Metabolic flexibility revealed in the genome of the cyst-forming alpha-1
RT   proteobacterium Rhodospirillum centenum.";
RL   BMC Genomics 11:325-325(2010).
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.
CC       {ECO:0000256|ARBA:ARBA00025164}.
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; Evidence={ECO:0000256|ARBA:ARBA00001454};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRSR:PIRSR604385-2};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudF subfamily.
CC       {ECO:0000256|ARBA:ARBA00007482}.
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DR   EMBL; CP000613; ACI98567.1; -; Genomic_DNA.
DR   RefSeq; WP_012566356.1; NC_011420.2.
DR   AlphaFoldDB; B6IMI8; -.
DR   STRING; 414684.RC1_1151; -.
DR   KEGG; rce:RC1_1151; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_062658_6_1_5; -.
DR   OrthoDB; 5292471at2; -.
DR   Proteomes; UP000001591; Chromosome.
DR   GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd03424; ADPRase_NUDT5; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR004385; NDP_pyrophosphatase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   NCBIfam; TIGR00052; nudix-type nucleoside diphosphatase, YffH/AdpP family; 1.
DR   PANTHER; PTHR11839:SF5; ADP-RIBOSE PYROPHOSPHATASE; 1.
DR   PANTHER; PTHR11839; UDP/ADP-SUGAR PYROPHOSPHATASE; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR604385-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR604385-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001591}.
FT   DOMAIN          58..196
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
FT   BINDING         99
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT   BINDING         115
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT   BINDING         119
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT   BINDING         167
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
SQ   SEQUENCE   213 AA;  23569 MW;  3A7EDDD7363E2042 CRC64;
     MTDQPSSPPA EAPFGRDDVQ VLERRQAYRG YFRVDVFRLR HRLFAGGWSG EMSRELFDRG
     HAAAILLYDP LRDAVVLVEQ FRVGALAADQ EPWLVEAVAG IVDPGETPEQ VVRRESVEEA
     GCTVSDLVLI GEFLPSPGGC SEVITLYCGR VDSAGAGGLH GLAEENEDIR VLVLPADDAI
     TRADRNEIRN GVTLVALHWL ARHRLSLRRR WAD
//