ID A0A1V9V6J0_9PSED Unreviewed; 205 AA.
AC A0A1V9V6J0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 Name=nudF {ECO:0000313|EMBL:OQR37756.1};
GN ORFNames=BWR59_01280 {ECO:0000313|EMBL:OQR37756.1};
OS Pseudomonas sp. Bc-h.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1943632 {ECO:0000313|EMBL:OQR37756.1, ECO:0000313|Proteomes:UP000192462};
RN [1] {ECO:0000313|EMBL:OQR37756.1, ECO:0000313|Proteomes:UP000192462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bc-h {ECO:0000313|EMBL:OQR37756.1,
RC ECO:0000313|Proteomes:UP000192462};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR37756.1}.
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DR EMBL; MUIN01000001; OQR37756.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9V6J0; -.
DR STRING; 1943632.BWR59_01280; -.
DR OrthoDB; 5292471at2; -.
DR Proteomes; UP000192462; Unassembled WGS sequence.
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 Magnesium {ECO:0000256|PIRSR:PIRSR604385-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604385-2}.
FT DOMAIN 51..189
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT MOTIF 93..115
FT /note="Nudix box"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-3"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
SQ SEQUENCE 205 AA; 23166 MW; 9B2F85608B19501C CRC64;
MTDSNKSTPT KHEIIRRDTC FKGFYQLDRL TLRHELFDGG MGPEINRELF VRHDAVCVLP
YDAKRDEVVL IEQFRVGVVG KHPNPWLIEM VAGLIDKEEQ PEEVAHREGE EEAELVFSAL
WPITKYFPSP GGSNEFVHLY LGKCESEGAG GVHGLEEEAE DIRVSVWSFD DAMQAVKDGR
IVNAATIIAI QWLALNRAEI MGLWS
//
