Reviewed,
UniProtKB/Swiss-Prot Q94B74 (NUDT2_ARATH)
Last modified
July 7, 2009.
Version 48.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Nudix hydrolase 2 Short name=AtNUDT2 EC=3.6.1.- Alternative name(s): ADP-ribose pyrophosphatase EC=3.6.1.13 NADH pyrophosphatase EC=3.6.1.22 | ||||||||
| Gene names |
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| Organism | Arabidopsis thaliana (Mouse-ear cress) [Complete proteome] | ||||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis |
Protein attributes
| Sequence length | 278 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. In vitro, it can use both NADH and ADP-ribose as substrates; however the relevance of such substrates in vivo is unclear. Ref.3 |
| Catalytic activity | ADP-ribose + H2O = AMP + D-ribose 5-phosphate. NAD+ + H2O = AMP + NMN. |
| Cofactor | Magnesium or manganese By similarity. |
| Tissue specificity | Expressed in roots, stems and leaves. Ref.3 |
| Induction | By paraquat, drought and high salinity. |
| Miscellaneous | Overexpression of NUTD2 confers enhanced tolerance to oxidative stress. |
| Sequence similarities | Belongs to the Nudix hydrolase family. Contains 1 nudix hydrolase domain. |
| Biophysicochemical properties | Kinetic parameters: KM=16.9 µM for ADP-ribose KM=23.1 µM for NADH Vmax=0.20 µmol/min/mg enzyme with ADP-ribose as substrate Vmax=0.16 µmol/min/mg enzyme with NADH as substrate |
Ontologies
| Keywords | |
|---|---|
| Ligand | Magnesium Manganese Metal-binding NAD |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | response to oxidative stress Ref.4 Inferred from mutant phenotype. Source: TAIR |
| Molecular function | ADP-ribose diphosphatase activity Ref.3 Inferred from direct assay. Source: TAIR NAD or NADH binding Ref.3Inferred from direct assay. Source: TAIR NAD+ diphosphatase activityInferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW manganese ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 278 | 278 | Nudix hydrolase 2 | PRO_0000057122 | |||||
Regions | |||||||||
| Domain | 111 – 240 | 130 | Nudix hydrolase | ||||||
| Motif | 147 – 168 | 22 | Nudix box | ||||||
Sites | |||||||||
| Metal binding | 162 | 1 | Magnesium or manganese By similarity | ||||||
| Metal binding | 166 | 1 | Magnesium or manganese By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 125 | 1 | E → EK in BAB09091. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Structural analysis of Arabidopsis thaliana chromosome 5. XI." Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [2] | "Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R.Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia. |
| [3] | "Comprehensive analysis of cytosolic nudix hydrolases in Arabidopsis thaliana." Ogawa T., Ueda Y., Yoshimura K., Shigeoka S. J. Biol. Chem. 280:25277-25283(2005) [PubMed: 15878881] [Abstract] Cited for: FUNCTION IN VITRO, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY. |
| [4] | "Overexpression of an ADP-ribose pyrophosphatase, AtNUDX2, confers enhanced tolerance to oxidative stress in Arabidopsis plants." Ogawa T., Ishikawa K., Harada K., Fukusaki E., Yoshimura K., Shigeoka S. Plant J. 57:289-301(2009) [PubMed: 18798872] [Abstract] Cited for: FUNCTION, INDUCTION. |
Cross-references
Sequence databases | |
|---|---|
| AB025628 Genomic DNA. Translation: BAB09091.1. Different initiation. AY042806 mRNA. Translation: AAK68746.1. AY064646 mRNA. Translation: AAL47357.1. | |
| IPI | IPI00532396. |
| RefSeq | NP_568687.1. |
| UniGene | At.71142 |
3D structure databases | |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q94B74. |
Genome annotation databases | |
| GeneID | 834816. |
| GenomeReviews | Gene locus AT5G47650 in contig BA000015_GR. |
| KEGG | ath:AT5G47650. |
| NMPDR | fig|3702.1.peg.26577. |
Organism-specific databases | |
| TAIR | At5g47650. |
Phylogenomic databases | |
| OMA | Q94B74. FVQKHEL. |
Enzyme and pathway databases | |
| BRENDA | 3.6.1.13. 302. 3.6.1.22. 302. |
Gene expression databases | |
| GermOnline | AT5G47650. Arabidopsis thaliana. |
Family and domain databases | |
| InterPro | IPR003293. GFG_antis. IPR000086. NUDIX_hydrolase_core. [Graphical view] |
| Gene3D | G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit. |
| Pfam | PF00293. NUDIX. 1 hit. [Graphical view] |
| PRINTS | PR01356. GFGPROTEIN. |
| PROSITE | PS00893. NUDIX. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NUDT2_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q94B74 Secondary accession number(s): Q9FGJ2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with


