Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9SU14 (NUDT7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nudix hydrolase 7

Short name=AtNUDT7
EC=3.6.1.-
Alternative name(s):
ADP-ribose pyrophosphatase
EC=3.6.1.13
NADH pyrophosphatase
EC=3.6.1.22
Protein GROWTH FACTOR GENE 1
Gene names
Name:NUDT7
Synonyms:GFG1, NUDX7
Ordered Locus Names:At4g12720
ORF Names:T20K18.70
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates the hydrolysis of some nucleoside diphosphate derivatives. Can use both NADH and ADP-ribose as substrates, but not 8-oxo-dGTP, cyclic ADP-ribose, GDP-manose, UDP-glucose, ATP, or GTP. Exerts negative control of EDS1 signaling. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Catalytic activity

ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate.

NAD+ + H2O = AMP + NMN.

Cofactor

Magnesium.

Enzyme regulation

Not inhibited by fluoride.

Subunit structure

Homodimer. Interacts with RACK1A, GG1 and GG2. Ref.6 Ref.10

Subcellular location

Nucleus. Cytoplasm. Cell membrane. Note: Localized at the plasma membrane when in complex with GG2, but present in the cytoplasm when associated with GG1. Detected in the cytoplasm and nucleus when interacting with RACK1A. Ref.10

Tissue specificity

Expressed in stems, leaves, roots, flowers and siliques. Ref.5 Ref.8

Induction

Rapid and transient induction by biotic and abiotic stresses. Not induced by H2O2. Ref.8 Ref.9

Disruption phenotype

Growth retardation, constitutive pathogen resistance phenotype and increased levels of reactive oxygen species and NADH. Ref.7 Ref.8 Ref.9

Sequence similarities

Belongs to the Nudix hydrolase family.

Contains 1 nudix hydrolase domain.

Biophysicochemical properties

Kinetic parameters:

KM=26.23 µM for NADH Ref.6 Ref.8

KM=25.8 µM for ADP-ribose

Vmax=3.681 nmol/min/mg enzyme with NADH as substrate

Vmax=2678 nmol/min/mg enzyme with ADP-ribose as substrate

pH dependence:

Optimum pH is 8.5.

Temperature dependence:

Optimum temperature is 50 degrees Celsius.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9SU14-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 282282Nudix hydrolase 7
PRO_0000057127

Regions

Domain101 – 233133Nudix hydrolase
Motif139 – 16022Nudix box

Sites

Metal binding1541Magnesium By similarity
Metal binding1581Magnesium By similarity

Experimental info

Mutagenesis1541E → Q: Loss of hydrolase activity. Ref.9
Sequence conflict61Q → L in AAM62604. Ref.4
Sequence conflict2171V → I in AAM62604. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: EA37FC0F1C2FDCB7

FASTA28231,884
        10         20         30         40         50         60 
MGTRAQQIPL LEGETDNYDG VTVTMVEPMD SEVFTESLRA SLSHWREEGK KGIWIKLPLG 

        70         80         90        100        110        120 
LANLVEAAVS EGFRYHHAEP EYLMLVSWIS ETPDTIPANA SHVVGAGALV INKNTKEVLV 

       130        140        150        160        170        180 
VQERSGFFKD KNVWKLPTGV INEGEDIWTG VAREVEEETG IIADFVEVLA FRQSHKAILK 

       190        200        210        220        230        240 
KKTDMFFLCV LSPRSYDITE QKSEILQAKW MPIQEYVDQP WNKKNEMFKF MANICQKKCE 

       250        260        270        280 
EEYLGFAIVP TTTSSGKESF IYCNADHAKR LKVSRDQASA SL 

« Hide

References

« Hide '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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN VITRO, TISSUE SPECIFICITY.
[6]"Cloning and characterization of an Arabidopsis thaliana Nudix hydrolase homologous to the mammalian GFG protein."
Olejnik K., Kraszewska E.
Biochim. Biophys. Acta 1752:133-141(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
[7]"Salicylic acid-independent ENHANCED DISEASE SUSCEPTIBILITY1 signaling in Arabidopsis immunity and cell death is regulated by the monooxygenase FMO1 and the Nudix hydrolase NUDT7."
Bartsch M., Gobbato E., Bednarek P., Debey S., Schultze J.L., Bautor J., Parker J.E.
Plant Cell 18:1038-1051(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[8]"Analysis of Arabidopsis growth factor gene 1 (GFG1) encoding a nudix hydrolase during oxidative signaling."
Jambunathan N., Mahalingam R.
Planta 224:1-11(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
[9]"AtNUDT7, a negative regulator of basal immunity in Arabidopsis, modulates two distinct defense response pathways and is involved in maintaining redox homeostasis."
Ge X., Li G.-J., Wang S.-B., Zhu H., Zhu T., Wang X., Xia Y.
Plant Physiol. 145:204-215(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLU-154, INDUCTION, DISRUPTION PHENOTYPE.
[10]"Arabidopsis thaliana Nudix hydrolase AtNUDT7 forms complexes with the regulatory RACK1A protein and Ggamma subunits of the signal transducing heterotrimeric G protein."
Olejnik K., Bucholc M., Anielska-Mazur A., Lipko A., Kujawa M., Modzelan M., Augustyn A., Kraszewska E.
Acta Biochim. Pol. 58:609-616(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RACK1A; GG1 AND GG2, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL049640 Genomic DNA. Translation: CAB40989.1.
AL161534 Genomic DNA. Translation: CAB78314.1.
CP002687 Genomic DNA. Translation: AEE83167.1.
CP002687 Genomic DNA. Translation: AEE83168.1.
CP002687 Genomic DNA. Translation: AEE83169.1.
AF325104 mRNA. Translation: AAK17172.1.
AF370209 mRNA. Translation: AAK44024.1.
AY056344 mRNA. Translation: AAL07193.1.
AY085375 mRNA. Translation: AAM62604.1.
PIRT06630.
RefSeqNP_193008.1. NM_117341.4. [Q9SU14-1]
NP_849367.1. NM_179036.3. [Q9SU14-1]
NP_849368.1. NM_179037.3. [Q9SU14-1]
UniGeneAt.23449.

3D structure databases

ProteinModelPortalQ9SU14.
SMRQ9SU14. Positions 11-91, 104-215.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid12181. 7 interactions.

Proteomic databases

PaxDbQ9SU14.
PRIDEQ9SU14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G12720.1; AT4G12720.1; AT4G12720. [Q9SU14-1]
AT4G12720.2; AT4G12720.2; AT4G12720. [Q9SU14-1]
AT4G12720.3; AT4G12720.3; AT4G12720. [Q9SU14-1]
GeneID826884.
KEGGath:AT4G12720.

Organism-specific databases

TAIRAT4G12720.

Phylogenomic databases

eggNOGNOG137117.
HOGENOMHOG000240943.
InParanoidQ9SU14.
PhylomeDBQ9SU14.

Enzyme and pathway databases

BioCycARA:AT4G12720-MONOMER.
ARA:GQT-2313-MONOMER.
ARA:GQT-2314-MONOMER.
ARA:GQT-2315-MONOMER.

Gene expression databases

ArrayExpressQ9SU14.
GenevestigatorQ9SU14.

Family and domain databases

Gene3D3.90.79.10. 1 hit.
InterProIPR003293. Nudix_hydrolase6-like.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSPR01356. GFGPROTEIN.
SUPFAMSSF55811. SSF55811. 1 hit.
PROSITEPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNUDT7_ARATH
AccessionPrimary (citable) accession number: Q9SU14
Secondary accession number(s): Q8LEK5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names