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Q9SU14

- NUDT7_ARATH

UniProt

Q9SU14 - NUDT7_ARATH

Protein

Nudix hydrolase 7

Gene

NUDT7

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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-ribose2 Publications

    Vmax=3.681 nmol/min/mg enzyme with NADH as substrate2 Publications

    Vmax=2678 nmol/min/mg enzyme with ADP-ribose as substrate2 Publications

    pH dependencei

    Optimum pH is 8.5.2 Publications

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius.2 Publications

    Sites

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

    GO - Molecular functioni

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

    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 1 Publication. Cytoplasm 1 Publication. Cell membrane 1 Publication
    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.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB
    3. plasma membrane Source: UniProtKB

    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 7PRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini101 – 233133Nudix hydrolasePROSITE-ProRule annotationAdd
    BLAST

    Motif

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

    Sequence similaritiesi

    Belongs to the Nudix hydrolase family.Curated
    Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

    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.

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    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

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 100 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