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Protein

ADP-sugar pyrophosphatase

Gene

Nudt5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Enzyme that can either act as an ADP-sugar pyrophosphatase in absence of diphosphate or catalyze the synthesis of ATP in presence of diphosphate (By similarity). In absence of diphosphate, hydrolyzes with similar activities various modified nucleoside diphosphates such as ADP-ribose, ADP-mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP (PubMed:10722730). Can also hydrolyze other nucleotide sugars with low activity (PubMed:10722730). In presence of diphosphate, mediates the synthesis of ATP in the nucleus by catalyzing the conversion of ADP-ribose to ATP and ribose 5-phosphate (By similarity). Nuclear ATP synthesis takes place when dephosphorylated at Thr-44 (By similarity). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (By similarity). Does not play a role in U8 snoRNA decapping activity (PubMed:21070968). Binds U8 snoRNA (PubMed:21070968).By similarity2 Publications

Catalytic activityi

ATP + D-ribose 5-phosphate = diphosphate + ADP-D-ribose.By similarity
ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate.By similarity
8-oxo-dGDP + H2O = 8-oxo-dGMP + phosphate.By similarity

Cofactori

Mg2+By similarityNote: Binds 3 Mg2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei27SubstrateBy similarity1
Binding sitei83SubstrateBy similarity1
Metal bindingi95Magnesium 1; via carbonyl oxygenBy similarity1
Binding sitei97Substrate; via amide nitrogenBy similarity1
Metal bindingi111Magnesium 2By similarity1
Metal bindingi111Magnesium 3By similarity1
Metal bindingi115Magnesium 1By similarity1
Metal bindingi115Magnesium 3By similarity1
Binding sitei132SubstrateBy similarity1
Metal bindingi165Magnesium 3By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-2393930. Phosphate bond hydrolysis by NUDT proteins.
SABIO-RKQ9JKX6.

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-sugar pyrophosphataseBy similarity (EC:3.6.1.13By similarity)
Alternative name(s):
8-oxo-dGDP phosphataseBy similarity (EC:3.6.1.58By similarity)
Nuclear ATP-synthesis protein NUDIX5By similarity (EC:2.7.7.-By similarity)
Nucleoside diphosphate-linked moiety X motif 5Curated
Short name:
Nudix motif 5Curated
Gene namesi
Name:Nudt5Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1858232. Nudt5.

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000570491 – 218ADP-sugar pyrophosphataseAdd BLAST218

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei10PhosphoserineCombined sources1
Modified residuei44PhosphothreonineBy similarity1
Modified residuei209N6-acetyllysineBy similarity1
Modified residuei217N6-acetyllysineBy similarity1

Post-translational modificationi

Phosphorylation at Thr-44 is required for homodimer stability; dephosphorylation results in destabilization of the homodimer. Dephosphorylation at Thr-44 promotes the ATP-synthesis activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9JKX6.
MaxQBiQ9JKX6.
PaxDbiQ9JKX6.
PeptideAtlasiQ9JKX6.
PRIDEiQ9JKX6.

2D gel databases

REPRODUCTION-2DPAGEQ9JKX6.

PTM databases

iPTMnetiQ9JKX6.
PhosphoSitePlusiQ9JKX6.
SwissPalmiQ9JKX6.

Miscellaneous databases

PMAP-CutDBQ9JKX6.

Expressioni

Tissue specificityi

Widely expressed. Most abundant in liver.1 Publication

Gene expression databases

BgeeiENSMUSG00000025817.
ExpressionAtlasiQ9JKX6. baseline and differential.
GenevisibleiQ9JKX6. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with PARG.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207516. 1 interactor.
IntActiQ9JKX6. 2 interactors.
MINTiMINT-4104265.
STRINGi10090.ENSMUSP00000026927.

Structurei

3D structure databases

ProteinModelPortaliQ9JKX6.
SMRiQ9JKX6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini56 – 196Nudix hydrolasePROSITE-ProRule annotationAdd BLAST141

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni45 – 46Substrate binding; shared with dimeric partner2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi96 – 117Nudix boxAdd BLAST22

Sequence similaritiesi

Belongs to the Nudix hydrolase family.Curated
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3041. Eukaryota.
COG0494. LUCA.
GeneTreeiENSGT00390000006280.
HOGENOMiHOG000174302.
HOVERGENiHBG052691.
InParanoidiQ9JKX6.
KOiK13987.
OMAiSYCLEFP.
OrthoDBiEOG091G0LL6.
PhylomeDBiQ9JKX6.
TreeFamiTF106347.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020476. Nudix_hydrolase.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR00502. NUDIXFAMILY.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JKX6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METRESTESS PGKHLVTSEE LISEGKWVKF EKTTYMDPTG KTRTWETVKL
60 70 80 90 100
TTRKGKSADA VSVIPVLQRT LHHECVILVK QFRPPMGSYC LEFPAGFIED
110 120 130 140 150
GESPEAAALR ELEEETGYKG EVAECSPAVC MDPGLSNCTT HVVTVTINGD
160 170 180 190 200
DAGNVRPKPK PGDGEFMEVI SLPKNDLLTR LDALGAEQHL TVDAKVYAYG
210
LALKHANSKP FEVPFLKF
Length:218
Mass (Da):23,984
Last modified:October 1, 2000 - v1
Checksum:iE831852919F85DFE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti103S → N in AAH04571 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF222786 mRNA. Translation: AAF44630.1.
AK088222 mRNA. Translation: BAC40220.1.
AL928924 Genomic DNA. Translation: CAM20348.1.
BC004571 mRNA. Translation: AAH04571.1.
BC049595 mRNA. Translation: AAH49595.1.
CCDSiCCDS15667.1.
RefSeqiNP_058614.1. NM_016918.3.
XP_006497575.1. XM_006497512.3.
XP_006497576.1. XM_006497513.3.
UniGeneiMm.251904.

Genome annotation databases

EnsembliENSMUST00000026927; ENSMUSP00000026927; ENSMUSG00000025817.
ENSMUST00000179748; ENSMUSP00000136233; ENSMUSG00000025817.
GeneIDi53893.
KEGGimmu:53893.
UCSCiuc033hlj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF222786 mRNA. Translation: AAF44630.1.
AK088222 mRNA. Translation: BAC40220.1.
AL928924 Genomic DNA. Translation: CAM20348.1.
BC004571 mRNA. Translation: AAH04571.1.
BC049595 mRNA. Translation: AAH49595.1.
CCDSiCCDS15667.1.
RefSeqiNP_058614.1. NM_016918.3.
XP_006497575.1. XM_006497512.3.
XP_006497576.1. XM_006497513.3.
UniGeneiMm.251904.

3D structure databases

ProteinModelPortaliQ9JKX6.
SMRiQ9JKX6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207516. 1 interactor.
IntActiQ9JKX6. 2 interactors.
MINTiMINT-4104265.
STRINGi10090.ENSMUSP00000026927.

PTM databases

iPTMnetiQ9JKX6.
PhosphoSitePlusiQ9JKX6.
SwissPalmiQ9JKX6.

2D gel databases

REPRODUCTION-2DPAGEQ9JKX6.

Proteomic databases

EPDiQ9JKX6.
MaxQBiQ9JKX6.
PaxDbiQ9JKX6.
PeptideAtlasiQ9JKX6.
PRIDEiQ9JKX6.

Protocols and materials databases

DNASUi53893.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026927; ENSMUSP00000026927; ENSMUSG00000025817.
ENSMUST00000179748; ENSMUSP00000136233; ENSMUSG00000025817.
GeneIDi53893.
KEGGimmu:53893.
UCSCiuc033hlj.1. mouse.

Organism-specific databases

CTDi11164.
MGIiMGI:1858232. Nudt5.

Phylogenomic databases

eggNOGiKOG3041. Eukaryota.
COG0494. LUCA.
GeneTreeiENSGT00390000006280.
HOGENOMiHOG000174302.
HOVERGENiHBG052691.
InParanoidiQ9JKX6.
KOiK13987.
OMAiSYCLEFP.
OrthoDBiEOG091G0LL6.
PhylomeDBiQ9JKX6.
TreeFamiTF106347.

Enzyme and pathway databases

ReactomeiR-MMU-2393930. Phosphate bond hydrolysis by NUDT proteins.
SABIO-RKQ9JKX6.

Miscellaneous databases

PMAP-CutDBQ9JKX6.
PROiQ9JKX6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000025817.
ExpressionAtlasiQ9JKX6. baseline and differential.
GenevisibleiQ9JKX6. MM.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020476. Nudix_hydrolase.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR00502. NUDIXFAMILY.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNUDT5_MOUSE
AccessioniPrimary (citable) accession number: Q9JKX6
Secondary accession number(s): A2ATT6, Q99KM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.