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Q9SU14

- NUDT7_ARATH

UniProt

Q9SU14 - NUDT7_ARATH

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Protein
Nudix hydrolase 7
Gene
NUDT7, GFG1, NUDX7, At4g12720, T20K18.70
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

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

Cofactori

Magnesium.

Enzyme regulationi

Not inhibited by fluoride.

Kineticsi

  1. KM=26.23 µM for NADH2 Publications
  2. 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 dependencei

Optimum pH is 8.5.

Temperature dependencei

Optimum temperature is 50 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi154 – 1541Magnesium By similarity
Metal bindingi158 – 1581Magnesium By similarity

GO - Molecular functioni

  1. ADP-ribose diphosphatase activity Source: UniProtKB-EC
  2. NAD+ diphosphatase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
  4. protein binding Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, NAD

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Nudix hydrolase 7 (EC:3.6.1.-)
Short name:
AtNUDT7
Alternative name(s):
ADP-ribose pyrophosphatase (EC:3.6.1.13)
NADH pyrophosphatase (EC:3.6.1.22)
Protein GROWTH FACTOR GENE 1
Gene namesi
Name:NUDT7
Synonyms:GFG1, NUDX7
Ordered Locus Names:At4g12720
ORF Names:T20K18.70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G12720.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Growth retardation, constitutive pathogen resistance phenotype and increased levels of reactive oxygen species and NADH.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi154 – 1541E → Q: Loss of hydrolase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 282282Nudix hydrolase 7
PRO_0000057127Add
BLAST

Proteomic databases

PaxDbiQ9SU14.
PRIDEiQ9SU14.

Expressioni

Tissue specificityi

Expressed in stems, leaves, roots, flowers and siliques.2 Publications

Inductioni

Rapid and transient induction by biotic and abiotic stresses. Not induced by H2O2.2 Publications

Gene expression databases

ArrayExpressiQ9SU14.
GenevestigatoriQ9SU14.

Interactioni

Subunit structurei

Homodimer. Interacts with RACK1A, GG1 and GG2.2 Publications

Protein-protein interaction databases

BioGridi12181. 7 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9SU14.
SMRiQ9SU14. Positions 11-91, 104-215.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini101 – 233133Nudix hydrolase
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi139 – 16022Nudix box
Add
BLAST

Sequence similaritiesi

Belongs to the Nudix hydrolase family.

Phylogenomic databases

eggNOGiNOG137117.
HOGENOMiHOG000240943.
InParanoidiQ9SU14.
PhylomeDBiQ9SU14.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR003293. Nudix_hydrolase6-like.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR01356. GFGPROTEIN.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9SU14-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MGTRAQQIPL LEGETDNYDG VTVTMVEPMD SEVFTESLRA SLSHWREEGK    50
KGIWIKLPLG LANLVEAAVS EGFRYHHAEP EYLMLVSWIS ETPDTIPANA 100
SHVVGAGALV INKNTKEVLV VQERSGFFKD KNVWKLPTGV INEGEDIWTG 150
VAREVEEETG IIADFVEVLA FRQSHKAILK KKTDMFFLCV LSPRSYDITE 200
QKSEILQAKW MPIQEYVDQP WNKKNEMFKF MANICQKKCE EEYLGFAIVP 250
TTTSSGKESF IYCNADHAKR LKVSRDQASA SL 282
Length:282
Mass (Da):31,884
Last modified:May 1, 2000 - v1
Checksum:iEA37FC0F1C2FDCB7
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61Q → L in AAM62604. 1 Publication
Sequence conflicti217 – 2171V → I in AAM62604. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiT06630.
RefSeqiNP_193008.1. NM_117341.4. [Q9SU14-1]
NP_849367.1. NM_179036.3. [Q9SU14-1]
NP_849368.1. NM_179037.3. [Q9SU14-1]
UniGeneiAt.23449.

Genome annotation databases

EnsemblPlantsiAT4G12720.1; AT4G12720.1; AT4G12720. [Q9SU14-1]
AT4G12720.2; AT4G12720.2; AT4G12720. [Q9SU14-1]
AT4G12720.3; AT4G12720.3; AT4G12720. [Q9SU14-1]
GeneIDi826884.
KEGGiath:AT4G12720.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi T06630.
RefSeqi NP_193008.1. NM_117341.4. [Q9SU14-1 ]
NP_849367.1. NM_179036.3. [Q9SU14-1 ]
NP_849368.1. NM_179037.3. [Q9SU14-1 ]
UniGenei At.23449.

3D structure databases

ProteinModelPortali Q9SU14.
SMRi Q9SU14. Positions 11-91, 104-215.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 12181. 7 interactions.

Proteomic databases

PaxDbi Q9SU14.
PRIDEi Q9SU14.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G12720.1 ; AT4G12720.1 ; AT4G12720 . [Q9SU14-1 ]
AT4G12720.2 ; AT4G12720.2 ; AT4G12720 . [Q9SU14-1 ]
AT4G12720.3 ; AT4G12720.3 ; AT4G12720 . [Q9SU14-1 ]
GeneIDi 826884.
KEGGi ath:AT4G12720.

Organism-specific databases

TAIRi AT4G12720.

Phylogenomic databases

eggNOGi NOG137117.
HOGENOMi HOG000240943.
InParanoidi Q9SU14.
PhylomeDBi Q9SU14.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressi Q9SU14.
Genevestigatori Q9SU14.

Family and domain databases

Gene3Di 3.90.79.10. 1 hit.
InterProi IPR003293. Nudix_hydrolase6-like.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view ]
Pfami PF00293. NUDIX. 1 hit.
[Graphical view ]
PRINTSi PR01356. GFGPROTEIN.
SUPFAMi SSF55811. SSF55811. 1 hit.
PROSITEi PS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [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.
    , 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.

Entry informationi

Entry nameiNUDT7_ARATH
AccessioniPrimary (citable) accession number: Q9SU14
Secondary accession number(s): Q8LEK5
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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