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Reviewed, UniProtKB/Swiss-Prot Q9SU14 (NUDT7_ARATH)

Last modified July 7, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

NAD+ + H2O = AMP + NMN.

Cofactor

Magnesium.

Enzyme regulation

Not inhibited by fluoride.

Subunit structure

Homodimer.

Tissue specificity

Expressed in stems, leaves, roots, flowers and siliques.

Induction

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

Disruption phenotype

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

Sequence similarities

Belongs to the Nudix hydrolase family.

Contains 1 nudix hydrolase domain.

Biophysicochemical properties

Kinetic parameters:

KM=26.23 µM for NADH

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 282282Nudix hydrolase 7
PRO_0000057127

Regions

Domain102 – 237136Nudix hydrolase
Motif139 – 16022Nudix box

Sites

Metal binding1541Magnesium By similarity
Metal binding1581Magnesium By similarity

Experimental info

Mutagenesis1541E → Q: Loss of hydrolase acitvity.
Sequence conflict61Q → L in AAM62604. Ref.3
Sequence conflict2171V → I in AAM62604. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9SU14-1 [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: 10617198] [Abstract]
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. 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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[3]"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].
[4]"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.
[5]"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: 16154395] [Abstract]
Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"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: 16531493] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]"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: 16328543] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
[8]"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: 17660350] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLU-154, INDUCTION, DISRUPTION PHENOTYPE.

Cross-references

Sequence databases

AL049640 Genomic DNA. Translation: CAB40989.1.
AL161534 Genomic DNA. Translation: CAB78314.1.
AF325104 mRNA. Translation: AAK17172.1.
AF370209 mRNA. Translation: AAK44024.1.
AY056344 mRNA. Translation: AAL07193.1.
AY085375 mRNA. Translation: AAM62604.1.
IPIIPI00537463.
PIRT06630.
RefSeqNP_193008.1.
NP_849367.1.
NP_849368.1.
UniGeneAt.23449

3D structure databases

ModBaseSearch...

Proteomic databases

PRIDEQ9SU14.
ProMEXQ9SU14.

Genome annotation databases

GeneID826884.
GenomeReviewsGene locus AT4G12720 in contig CT486007_GR.
KEGGath:AT4G12720.
NMPDRfig|3702.1.peg.18947.

Organism-specific databases

TAIRAt4g12720.

Phylogenomic databases

OMAQ9SU14. ANASHIV.

Enzyme and pathway databases

BRENDA3.6.1.13. 302.
3.6.1.22. 302.

Gene expression databases

GermOnlineAT4G12720. Arabidopsis thaliana.

Family and domain databases

InterProIPR003293. GFG_antis.
IPR000086. NUDIX_hydrolase_core.
[Graphical view]
Gene3DG3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
PfamPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSPR01356. GFGPROTEIN.
PROSITEPS00893. NUDIX. 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: July 7, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents