Q9LE73 (NUDT4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nudix hydrolase 4
Short name=AtNUDT4
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:	NUDT4
Synonyms:	NUDX4
Ordered Locus Names:	At1g18300
ORF Names:	F15H18.18

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	207 AA.
Sequence status	Complete.
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.5
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.5
Sequence similarities	Belongs to the Nudix hydrolase family. Contains 1 nudix hydrolase domain.

Ontologies

Keywords
Ligand	Magnesium Manganese Metal-binding NAD
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	ADP-ribose diphosphatase activity Inferred from electronic annotation. Source: EC NAD+ diphosphatase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred 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 – 207	207	Nudix hydrolase 4		PRO_0000057124
Regions
	Domain	58 – 194	137	Nudix hydrolase
	Motif	101 – 122	22	Nudix box
Sites
	Metal binding	116	1	Magnesium or manganese By similarity
	Metal binding	120	1	Magnesium or manganese By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9LE73 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 0E266BF7519129E1	FASTA	207	23,701
	10 20 30 40 50 60 MTGFSVSLFV SNLSNVASYL SPIFENIPST KVVPAQIEKV VSLVSRTGRD LQRYDHAGYR 70 80 90 100 110 120 QVVGCVPYRY KKQEVNGVET QVIQVLLVSA QKGKGMLFPK GGWETDESME EAALRETIEE 130 140 150 160 170 180 AGVTGELEEK LGKWQYKSKR HSIIHDGYMF ALLVSQEFER WPEAEMRQRR WVSLDEAREV 190 200 CQNWWMREAL EAFINLKCLA DDDESGN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"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. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"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, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC013354 Genomic DNA. Translation: AAF25994.1. AC069551 Genomic DNA. Translation: AAF78378.1. CP002684 Genomic DNA. Translation: AEE29699.1. BT003060 mRNA. Translation: AAO23625.1. AK227367 mRNA. Translation: BAE99375.1.
IPI	IPI00525170.
RefSeq	NP_173266.1. NM_101688.2.
UniGene	At.22732.
3D structure databases
ProteinModelPortal	Q9LE73.
SMR	Q9LE73. Positions 52-194.
ModBase	Search...
Proteomic databases
PRIDE	Q9LE73.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G18300.1; AT1G18300.1; AT1G18300.
GeneID	838410.
GenomeReviews	Gene locus AT1G18300 in contig CT485782_GR.
KEGG	ath:AT1G18300.
NMPDR	fig|3702.1.peg.2163.
Organism-specific databases
TAIR	At1g18300.
Phylogenomic databases
GeneTree	EPGT00050000017749.
HOGENOM	HBG713158.
InParanoid	Q9LE73.
OMA	SPIFENI.
PhylomeDB	Q9LE73.
ProtClustDB	CLSN2914542.
Gene expression databases
Genevestigator	Q9LE73.
Family and domain databases
InterPro	IPR020084. NUDIX_hydrolase_CS. IPR000086. NUDIX_hydrolase_dom. IPR015797. NUDIX_hydrolase_dom-like. [Graphical view]
Gene3D	G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
Pfam	PF00293. NUDIX. 1 hit. [Graphical view]
SUPFAM	SSF55811. NUDIX_hydrolase. 1 hit.
PROSITE	PS51462. NUDIX. 1 hit. PS00893. NUDIX_BOX. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NUDT4_ARATH

Accession

Primary (citable) accession number: Q9LE73
Secondary accession number(s): Q0WU23

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	October 1, 2000
Last modified:	September 21, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program