ID   A4WQQ8_CERS5            Unreviewed;       362 AA.
AC   A4WQQ8;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 67.
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=Rsph17025_0818 {ECO:0000313|EMBL:ABP69722.1};
OS   Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=349102 {ECO:0000313|EMBL:ABP69722.1};
RN   [1] {ECO:0000313|EMBL:ABP69722.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17025 {ECO:0000313|EMBL:ABP69722.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M.,
RA   Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000661; ABP69722.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WQQ8; -.
DR   STRING; 349102.Rsph17025_0818; -.
DR   KEGG; rsq:Rsph17025_0818; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_040290_0_0_5; -.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
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; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ABP69722.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR604385-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR604385-2}.
FT   DOMAIN          206..346
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
FT   MOTIF           249..271
FT                   /note="Nudix box"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604385-3"
FT   BINDING         248
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT   BINDING         264
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT   BINDING         317
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
SQ   SEQUENCE   362 AA;  38727 MW;  B877B7AD084A8847 CRC64;
     MRVFLCGPMA DEALRALVLG EEVAGVPARL EGHALRAAGA TVVPVPAGSD AVEGLLAEPG
     PEAAARLAYH QQAAGYQAVM HEIGGAPAVV FTADPDGAEA WDPVTWNAVW GPIVVATAGD
     VMALWPEVPA EQVGRRYRLM LVQGASRVRA AAPAPSRRRH AASPADVSVI RRRQPYANFF
     AVEEYDLSFR SFGGGMSPAV NRAVFISGDA VTVVPYDPVR DRVLLIEQFR PGPFGRGDGQ
     PWLLEPIAGR IDPGETPEGS ARREAVEEAG LALGELLPVA SYYPTPAAKA EYLYSYVALA
     ELPDGIEGVF GMEGEGEDIR GHLMAFDEMM ELVRSGEICN GPLLLTALWL ERERPGLRAA
     RR
//