ID NUDT5_RAT Reviewed; 219 AA.
AC Q6AY63;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 24-JAN-2024, entry version 124.
DE RecName: Full=ADP-sugar pyrophosphatase {ECO:0000250|UniProtKB:Q9UKK9};
DE EC=3.6.1.13 {ECO:0000250|UniProtKB:Q9UKK9};
DE AltName: Full=8-oxo-dGDP phosphatase {ECO:0000250|UniProtKB:Q9UKK9};
DE EC=3.6.1.58 {ECO:0000250|UniProtKB:Q9UKK9};
DE AltName: Full=Nuclear ATP-synthesis protein NUDIX5 {ECO:0000250|UniProtKB:Q9UKK9};
DE EC=2.7.7.96 {ECO:0000250|UniProtKB:Q9UKK9};
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 5 {ECO:0000305};
DE Short=Nudix motif 5 {ECO:0000305};
GN Name=Nudt5 {ECO:0000312|RGD:1359284};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Enzyme that can either act as an ADP-sugar pyrophosphatase in
CC absence of diphosphate or catalyze the synthesis of ATP in presence of
CC diphosphate. In absence of diphosphate, hydrolyzes with similar
CC activities various modified nucleoside diphosphates such as ADP-ribose,
CC ADP-mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP. Can also hydrolyze
CC other nucleotide sugars with low activity. In presence of diphosphate,
CC mediates the synthesis of ATP in the nucleus by catalyzing the
CC conversion of ADP-ribose to ATP and ribose 5-phosphate. Nuclear ATP
CC synthesis takes place when dephosphorylated at Thr-45. Nuclear ATP
CC generation is required for extensive chromatin remodeling events that
CC are energy-consuming. Does not play a role in U8 snoRNA decapping
CC activity. Binds U8 snoRNA. {ECO:0000250|UniProtKB:Q9JKX6,
CC ECO:0000250|UniProtKB:Q9UKK9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose 5-phosphate + H(+) = ADP-D-ribose +
CC diphosphate; Xref=Rhea:RHEA:50248, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57967,
CC ChEBI:CHEBI:78346; EC=2.7.7.96;
CC Evidence={ECO:0000250|UniProtKB:Q9UKK9};
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:0000250|UniProtKB:Q9UKK9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxo-dGDP + H2O = 8-oxo-dGMP + H(+) + phosphate;
CC Xref=Rhea:RHEA:32063, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:63224, ChEBI:CHEBI:63715; EC=3.6.1.58;
CC Evidence={ECO:0000250|UniProtKB:Q9UKK9};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9UKK9};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9UKK9};
CC -!- SUBUNIT: Homodimer. Interacts with PARG.
CC {ECO:0000250|UniProtKB:Q9UKK9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UKK9}.
CC -!- PTM: Phosphorylation at Thr-45 is required for homodimer stability;
CC dephosphorylation results in destabilization of the homodimer.
CC Dephosphorylation at Thr-45 promotes the ATP-synthesis activity.
CC {ECO:0000250|UniProtKB:Q9UKK9}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; BC079176; AAH79176.1; -; mRNA.
DR RefSeq; NP_001007734.1; NM_001007733.1.
DR AlphaFoldDB; Q6AY63; -.
DR SMR; Q6AY63; -.
DR BioGRID; 262565; 2.
DR STRING; 10116.ENSRNOP00000023893; -.
DR iPTMnet; Q6AY63; -.
DR PhosphoSitePlus; Q6AY63; -.
DR jPOST; Q6AY63; -.
DR PaxDb; 10116-ENSRNOP00000023893; -.
DR Ensembl; ENSRNOT00000082669.2; ENSRNOP00000075734.1; ENSRNOG00000017741.7.
DR Ensembl; ENSRNOT00055030240; ENSRNOP00055024309; ENSRNOG00055017867.
DR Ensembl; ENSRNOT00060014075; ENSRNOP00060010774; ENSRNOG00060008442.
DR Ensembl; ENSRNOT00065012077; ENSRNOP00065008815; ENSRNOG00065007710.
DR GeneID; 361274; -.
DR KEGG; rno:361274; -.
DR AGR; RGD:1359284; -.
DR CTD; 11164; -.
DR RGD; 1359284; Nudt5.
DR eggNOG; KOG3041; Eukaryota.
DR GeneTree; ENSGT00940000154045; -.
DR InParanoid; Q6AY63; -.
DR OMA; NDPGLCN; -.
DR OrthoDB; 991202at2759; -.
DR PhylomeDB; Q6AY63; -.
DR TreeFam; TF106347; -.
DR Reactome; R-RNO-2393930; Phosphate bond hydrolysis by NUDT proteins.
DR SABIO-RK; Q6AY63; -.
DR PRO; PR:Q6AY63; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000017741; Expressed in jejunum and 19 other cell types or tissues.
DR ExpressionAtlas; Q6AY63; baseline and differential.
DR Genevisible; Q6AY63; RN.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0044715; F:8-oxo-dGDP phosphatase activity; ISS:UniProtKB.
DR GO; GO:0044716; F:8-oxo-GDP phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0019144; F:ADP-sugar diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; ISO:RGD.
DR GO; GO:0016779; F:nucleotidyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0030515; F:snoRNA binding; ISS:UniProtKB.
DR GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISO:RGD.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0019303; P:D-ribose catabolic process; ISS:UniProtKB.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; ISO:RGD.
DR GO; GO:0006753; P:nucleoside phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0009191; P:ribonucleoside diphosphate catabolic process; ISS:UniProtKB.
DR GO; GO:0019693; P:ribose phosphate metabolic process; IBA:GO_Central.
DR CDD; cd03424; ADPRase_NUDT5; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR11839:SF1; ADP-SUGAR PYROPHOSPHATASE; 1.
DR PANTHER; PTHR11839; UDP/ADP-SUGAR PYROPHOSPHATASE; 1.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Hydrolase; Isopeptide bond; Magnesium; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Transferase;
KW Ubl conjugation.
FT CHAIN 1..219
FT /note="ADP-sugar pyrophosphatase"
FT /id="PRO_0000250703"
FT DOMAIN 57..197
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 97..118
FT /note="Nudix box"
FT BINDING 28
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 46..47
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 84
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 98
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 133
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT MOD_RES 45
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT MOD_RES 210
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT MOD_RES 218
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
SQ SEQUENCE 219 AA; 24117 MW; 87AFCD2BDD6E4B04 CRC64;
METQEPKDSS PPTEQRILSE ELISEGKWVK FEKTTYMDPT GKTRTWETVK LTTRKGKSAD
AVSVIPVLQR TLHHECIVLV KQFRPPMGGY CLEFPAGLIE DGESPEAAAL RELEEETGYK
GDIAECSPAV CMDPGLSNCT THVVTVTING DDAGNVRPKP KPGDGEFVEV ISLPKNDLLT
RLDALGAEDR LTVDARVYAY ALALKHANAK PFEVPFLKF
//
