Reviewed, UniProtKB/Swiss-Prot Q6NPD7 (NUD10_ARATH)

Names and origin

Protein names

Recommended name:
    Nudix hydrolase 10
      Short name=AtNUDT10
    EC=3.6.1.-
Alternative name(s):
    ADP-ribose pyrophosphatase
    EC=3.6.1.13
    NADH pyrophosphatase
    EC=3.6.1.22

Gene names

Name:	NUDT10
Synonyms:	NUDX10
Ordered Locus Names:	At4g25434
ORF Names:	T30C3.4

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	277 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, at lower level, leaves. Ref.3
Sequence similarities	Belongs to the Nudix hydrolase family. Contains 1 nudix hydrolase domain.
Biophysicochemical properties	Kinetic parameters: KM=27.4 µM for ADP-ribose Vmax=0.10 µmol/min/mg enzyme with ADP-ribose as substrate
Sequence caution	The sequence CAA18182.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	Magnesium Manganese Metal-binding NAD
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	ADP-ribose diphosphatase activity Ref.3 Inferred from direct assay. Source: TAIR NAD or NADH binding Ref.3 Inferred from direct assay. Source: TAIR NAD+ diphosphatase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q6NPD7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q6NPD7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     163-163: G → GVRRSIYLNVNQSTINIYNLTFSYIYLQ

Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 277	277	Nudix hydrolase 10		PRO_0000057130
Regions
	Domain	111 – 239	129	Nudix hydrolase
	Motif	142 – 163	22	Nudix box
Sites
	Metal binding	157	1	Magnesium or manganese By similarity
	Metal binding	161	1	Magnesium or manganese By similarity
Natural variations
	Alternative sequence	163	1	G → GVRRSIYLNVNQSTINIYNL TFSYIYLQ in isoform 2.		VSP_037557

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: A609D65AB5D2EE3F	FASTA	277	31,816
	10 20 30 40 50 60 MSDQEAPLRN GVEHKIFEVL PFVDDDYGGV IVEMKTPMDT KNFVAALRDS FEQWRLQGKK 70 80 90 100 110 120 GVWLNLPLSH VNLVEPAVKE GFRYHHAEPT YLMLVYWIPE AESTIPLNAS HRVRVGAVVL 130 140 150 160 170 180 NHNKEEKYGS LCGSGIWKIP TGVVDEGEEI FAAAIREVKE ETGIDTEFLE ILAFCQTHES 190 200 210 220 230 240 FFAKSDLFFV CLLRPTSFDI QKQDLEIEAA QWMRFEDSAS QPITHKNDLF KDIHHICSMK 250 260 270 MEKSYSGFSK KPITTFFDDK LGYLYLNKQE DMEQPIS
	Isoform 2. Checksum: 35DFD0ED17293278	FASTA	304	35,095
	10 20 30 40 50 60 MSDQEAPLRN GVEHKIFEVL PFVDDDYGGV IVEMKTPMDT KNFVAALRDS FEQWRLQGKK 70 80 90 100 110 120 GVWLNLPLSH VNLVEPAVKE GFRYHHAEPT YLMLVYWIPE AESTIPLNAS HRVRVGAVVL 130 140 150 160 170 180 NHNKEEKYGS LCGSGIWKIP TGVVDEGEEI FAAAIREVKE ETGVRRSIYL NVNQSTINIY 190 200 210 220 230 240 NLTFSYIYLQ IDTEFLEILA FCQTHESFFA KSDLFFVCLL RPTSFDIQKQ DLEIEAAQWM 250 260 270 280 290 300 RFEDSASQPI THKNDLFKDI HHICSMKMEK SYSGFSKKPI TTFFDDKLGY LYLNKQEDME QPIS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R. Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL022197 Genomic DNA. Translation: CAA18182.1. Sequence problems. BT010987 mRNA. Translation: AAR24765.1. BT010765 mRNA. Translation: AAR23735.1.
IPI	IPI00538855.
PIR	T05803.
RefSeq	NP_849443.2.
UniGene	At.47131
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	828648.
GenomeReviews	Gene locus AT4G25434 in contig CT486007_GR.
Organism-specific databases
TAIR	At4g25434.
Enzyme and pathway databases
BRENDA	3.6.1.13. 302. 3.6.1.22. 302.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NUD10_ARATH

Accession

Primary (citable) accession number: Q6NPD7
Secondary accession number(s): O65616, Q2V3F2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	July 5, 2004
Last modified:	July 7, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)