ID B3PCJ9_CELJU Unreviewed; 209 AA.
AC B3PCJ9;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=CJA_2908 {ECO:0000313|EMBL:ACE85856.1};
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE85856.1, ECO:0000313|Proteomes:UP000001036};
RN [1] {ECO:0000313|EMBL:ACE85856.1, ECO:0000313|Proteomes:UP000001036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE85856.1,
RC ECO:0000313|Proteomes:UP000001036};
RX PubMed=18556790; DOI=10.1128/JB.01701-07;
RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
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; CP000934; ACE85856.1; -; Genomic_DNA.
DR RefSeq; WP_012488492.1; NC_010995.1.
DR AlphaFoldDB; B3PCJ9; -.
DR STRING; 498211.CJA_2908; -.
DR KEGG; cja:CJA_2908; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_062658_6_1_6; -.
DR OrthoDB; 5292471at2; -.
DR Proteomes; UP000001036; 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:UP000001036}.
FT DOMAIN 52..195
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT MOTIF 94..116
FT /note="Nudix box"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-3"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
SQ SEQUENCE 209 AA; 23622 MW; 2CC229A4506BB1EB CRC64;
MAIDKPVFTR GDVEIIRREQ LYKRFFRVEK VFLRHRLFGG GWGKEIGREL FVRGEAVAVV
LYDPEHDLIG MVEQFRVGAM DEINGPWCYE VVAGMLEPGE SPEEVARREL IEEANVEPCR
MEYICNYLSS PGGSDEKLHL FCGLCDLSQA GGVYGLPEEG EDIRVHVFTA GDVFAELYSG
AFNNAAALIC LQWLQANRPR LRTQMTGQE
//
