NUDT5_PONAB
ID NUDT5_PONAB Reviewed; 216 AA.
AC Q5RCY2; H2N9S2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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:0000250|UniProtKB:Q9UKK9};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR858136; CAH90375.1; -; mRNA.
DR EMBL; ABGA01256085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001125182.1; NM_001131710.1.
DR AlphaFoldDB; Q5RCY2; -.
DR SMR; Q5RCY2; -.
DR STRING; 9601.ENSPPYP00000002427; -.
DR PRIDE; Q5RCY2; -.
DR Ensembl; ENSPPYT00000037059; ENSPPYP00000040737; ENSPPYG00000002091.
DR GeneID; 100172071; -.
DR KEGG; pon:100172071; -.
DR CTD; 11164; -.
DR eggNOG; KOG3041; Eukaryota.
DR GeneTree; ENSGT00940000154045; -.
DR HOGENOM; CLU_062658_0_2_1; -.
DR InParanoid; Q5RCY2; -.
DR TreeFam; TF106347; -.
DR Proteomes; UP000001595; Chromosome 10.
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:0000287; F:magnesium ion binding; ISS:UniProtKB.
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:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0019303; P:D-ribose catabolic process; ISS:UniProtKB.
DR GO; GO:0009191; P:ribonucleoside diphosphate catabolic process; ISS:UniProtKB.
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 Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; SSF55811; 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..216
FT /note="ADP-sugar pyrophosphatase"
FT /id="PRO_0000250702"
FT DOMAIN 57..194
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 51
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 163
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 3
FT /note="Phosphoserine"
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 74
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT MOD_RES 207
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK9"
FT MOD_RES 215
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"
FT CONFLICT 162
FT /note="P -> PGDG (in Ref. 2; ABGA01256085)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24070 MW; 9C88CC433D3CC3A9 CRC64;
MESQEPTESS QNGKQYIISE ELISEGKWVK LEKTTYMDPT GKTRTWESVK RTTRKEQTAD
GVAVIPVLQR TLHYECIVLV KQFRPPMGGY CIEFPAGLID DGETPEAAAL RELEEETGYK
GDVAECSPAV CMDPGLSNCT VHIVTVTING DDAENARPKP KPEFVEVISL PKNDLLQRLD
ALVAEEHLTV DARVYSYALA LKHANAKPFE VPFLKF
