ID A0A014MBS7_9GAMM Unreviewed; 211 AA.
AC A0A014MBS7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
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:EXU75544.1};
GN ORFNames=BG55_10245 {ECO:0000313|EMBL:EXU75544.1};
OS Erwinia mallotivora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU75544.1, ECO:0000313|Proteomes:UP000019918};
RN [1] {ECO:0000313|EMBL:EXU75544.1, ECO:0000313|Proteomes:UP000019918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU75544.1,
RC ECO:0000313|Proteomes:UP000019918};
RA Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA Mat Amin N.;
RT "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT pathogen.";
RL Submitted (FEB-2014) 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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:EXU75544.1}.
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DR EMBL; JFHN01000045; EXU75544.1; -; Genomic_DNA.
DR RefSeq; WP_034936932.1; NZ_JFHN01000045.1.
DR AlphaFoldDB; A0A014MBS7; -.
DR STRING; 69222.BG55_10245; -.
DR PATRIC; fig|69222.5.peg.2114; -.
DR OrthoDB; 5292471at2; -.
DR Proteomes; UP000019918; Unassembled WGS sequence.
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, ECO:0000313|EMBL:EXU75544.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR604385-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604385-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000019918}.
FT DOMAIN 55..193
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT MOTIF 97..119
FT /note="Nudix box"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-3"
FT BINDING 96
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 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604385-2"
SQ SEQUENCE 211 AA; 23978 MW; E266B626AC1681A1 CRC64;
MESDKKYPVT FTKNDVEIIA RETLYRGFFS LIRYHFRHRL FSGEMSGEVT RDVFERGHAA
AMLPYDPQRD EVVLIEQIRI PAFDSSATPW LLELVAGIIE PGETPEDVVR REAEEEAGLT
PGRVRPVLNY LASPGGTSER LAILVGEVDA SVAQGNHGLE EENEDILVHV VSRQQAYQWV
EEGKIDNAAS VIALQWLELH HKKLQEEWKN E
//
