ID NUDT7_ARATH Reviewed; 282 AA. AC Q9SU14; Q8LEK5; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 08-JUN-2016, entry version 112. DE RecName: Full=Nudix hydrolase 7; DE Short=AtNUDT7; DE EC=3.6.1.-; DE AltName: Full=ADP-ribose pyrophosphatase; DE EC=3.6.1.13; DE AltName: Full=NADH pyrophosphatase; DE EC=3.6.1.22; DE AltName: Full=Protein GROWTH FACTOR GENE 1; GN Name=NUDT7; Synonyms=GFG1, NUDX7; OrderedLocusNames=At4g12720; GN ORFNames=T20K18.70; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP FUNCTION IN VITRO, AND TISSUE SPECIFICITY. RX PubMed=15878881; DOI=10.1074/jbc.M503536200; RA Ogawa T., Ueda Y., Yoshimura K., Shigeoka S.; RT "Comprehensive analysis of cytosolic nudix hydrolases in Arabidopsis RT thaliana."; RL J. Biol. Chem. 280:25277-25283(2005). RN [6] RP FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=16154395; DOI=10.1016/j.bbapap.2005.07.021; RA Olejnik K., Kraszewska E.; RT "Cloning and characterization of an Arabidopsis thaliana Nudix RT hydrolase homologous to the mammalian GFG protein."; RL Biochim. Biophys. Acta 1752:133-141(2005). RN [7] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=16531493; DOI=10.1105/tpc.105.039982; RA Bartsch M., Gobbato E., Bednarek P., Debey S., Schultze J.L., RA Bautor J., Parker J.E.; RT "Salicylic acid-independent ENHANCED DISEASE SUSCEPTIBILITY1 signaling RT in Arabidopsis immunity and cell death is regulated by the RT monooxygenase FMO1 and the Nudix hydrolase NUDT7."; RL Plant Cell 18:1038-1051(2006). RN [8] RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, BIOPHYSICOCHEMICAL RP PROPERTIES, AND DISRUPTION PHENOTYPE. RX PubMed=16328543; DOI=10.1007/s00425-005-0183-y; RA Jambunathan N., Mahalingam R.; RT "Analysis of Arabidopsis growth factor gene 1 (GFG1) encoding a nudix RT hydrolase during oxidative signaling."; RL Planta 224:1-11(2006). RN [9] RP FUNCTION, MUTAGENESIS OF GLU-154, INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=17660350; DOI=10.1104/pp.107.103374; RA Ge X., Li G.-J., Wang S.-B., Zhu H., Zhu T., Wang X., Xia Y.; RT "AtNUDT7, a negative regulator of basal immunity in Arabidopsis, RT modulates two distinct defense response pathways and is involved in RT maintaining redox homeostasis."; RL Plant Physiol. 145:204-215(2007). RN [10] RP INTERACTION WITH RACK1A; GG1 AND GG2, AND SUBCELLULAR LOCATION. RX PubMed=22068106; RA Olejnik K., Bucholc M., Anielska-Mazur A., Lipko A., Kujawa M., RA Modzelan M., Augustyn A., Kraszewska E.; RT "Arabidopsis thaliana Nudix hydrolase AtNUDT7 forms complexes with the RT regulatory RACK1A protein and Ggamma subunits of the signal RT transducing heterotrimeric G protein."; RL Acta Biochim. Pol. 58:609-616(2011). CC -!- FUNCTION: Mediates the hydrolysis of some nucleoside diphosphate CC derivatives. Can use both NADH and ADP-ribose as substrates, but CC not 8-oxo-dGTP, cyclic ADP-ribose, GDP-manose, UDP-glucose, ATP, CC or GTP. Exerts negative control of EDS1 signaling. CC {ECO:0000269|PubMed:15878881, ECO:0000269|PubMed:16154395, CC ECO:0000269|PubMed:16328543, ECO:0000269|PubMed:16531493, CC ECO:0000269|PubMed:17660350}. CC -!- CATALYTIC ACTIVITY: ADP-D-ribose + H(2)O = AMP + D-ribose 5- CC phosphate. CC -!- CATALYTIC ACTIVITY: NAD(H) + H(2)O = AMP + NMN(H). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- ENZYME REGULATION: Not inhibited by fluoride. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=26.23 uM for NADH {ECO:0000269|PubMed:16154395, CC ECO:0000269|PubMed:16328543}; CC KM=25.8 uM for ADP-ribose {ECO:0000269|PubMed:16154395, CC ECO:0000269|PubMed:16328543}; CC Vmax=3.681 nmol/min/mg enzyme with NADH as substrate CC {ECO:0000269|PubMed:16154395, ECO:0000269|PubMed:16328543}; CC Vmax=2678 nmol/min/mg enzyme with ADP-ribose as substrate CC {ECO:0000269|PubMed:16154395, ECO:0000269|PubMed:16328543}; CC pH dependence: CC Optimum pH is 8.5. {ECO:0000269|PubMed:16154395, CC ECO:0000269|PubMed:16328543}; CC Temperature dependence: CC Optimum temperature is 50 degrees Celsius. CC {ECO:0000269|PubMed:16154395, ECO:0000269|PubMed:16328543}; CC -!- SUBUNIT: Homodimer. Interacts with RACK1A, GG1 and GG2. CC {ECO:0000269|PubMed:16154395, ECO:0000269|PubMed:22068106}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22068106}. CC Cytoplasm {ECO:0000269|PubMed:22068106}. Cell membrane CC {ECO:0000269|PubMed:22068106}. Note=Localized at the plasma CC membrane when in complex with GG2, but present in the cytoplasm CC when associated with GG1. Detected in the cytoplasm and nucleus CC when interacting with RACK1A. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences.; CC Name=1; CC IsoId=Q9SU14-1; Sequence=Displayed; CC -!- TISSUE SPECIFICITY: Expressed in stems, leaves, roots, flowers and CC siliques. {ECO:0000269|PubMed:15878881, CC ECO:0000269|PubMed:16328543}. CC -!- INDUCTION: Rapid and transient induction by biotic and abiotic CC stresses. Not induced by H(2)O(2). {ECO:0000269|PubMed:16328543, CC ECO:0000269|PubMed:17660350}. CC -!- DISRUPTION PHENOTYPE: Growth retardation, constitutive pathogen CC resistance phenotype and increased levels of reactive oxygen CC species and NADH. {ECO:0000269|PubMed:16328543, CC ECO:0000269|PubMed:16531493, ECO:0000269|PubMed:17660350}. CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 nudix hydrolase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00794}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL049640; CAB40989.1; -; Genomic_DNA. DR EMBL; AL161534; CAB78314.1; -; Genomic_DNA. DR EMBL; CP002687; AEE83167.1; -; Genomic_DNA. DR EMBL; CP002687; AEE83168.1; -; Genomic_DNA. DR EMBL; CP002687; AEE83169.1; -; Genomic_DNA. DR EMBL; AF325104; AAK17172.1; -; mRNA. DR EMBL; AF370209; AAK44024.1; -; mRNA. DR EMBL; AY056344; AAL07193.1; -; mRNA. DR EMBL; AY085375; AAM62604.1; -; mRNA. DR PIR; T06630; T06630. DR RefSeq; NP_193008.1; NM_117341.4. [Q9SU14-1] DR RefSeq; NP_849367.1; NM_179036.3. [Q9SU14-1] DR RefSeq; NP_849368.1; NM_179037.3. [Q9SU14-1] DR UniGene; At.23449; -. DR PDB; 4ZB3; X-ray; 2.30 A; A=1-282. DR PDB; 4ZBP; X-ray; 2.60 A; A/B/C=1-282. DR PDBsum; 4ZB3; -. DR PDBsum; 4ZBP; -. DR ProteinModelPortal; Q9SU14; -. DR SMR; Q9SU14; 7-268. DR BioGrid; 12181; 9. DR PRIDE; Q9SU14; -. DR EnsemblPlants; AT4G12720.1; AT4G12720.1; AT4G12720. [Q9SU14-1] DR EnsemblPlants; AT4G12720.2; AT4G12720.2; AT4G12720. [Q9SU14-1] DR EnsemblPlants; AT4G12720.3; AT4G12720.3; AT4G12720. [Q9SU14-1] DR GeneID; 826884; -. DR KEGG; ath:AT4G12720; -. DR TAIR; AT4G12720; -. DR HOGENOM; HOG000240943; -. DR InParanoid; Q9SU14; -. DR PhylomeDB; Q9SU14; -. DR BioCyc; ARA:AT4G12720-MONOMER; -. DR BioCyc; ARA:GQT-2313-MONOMER; -. DR BioCyc; ARA:GQT-2314-MONOMER; -. DR BioCyc; ARA:GQT-2315-MONOMER; -. DR BRENDA; 3.6.1.13; 399. DR PRO; PR:Q9SU14; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q9SU14; baseline and differential. DR Genevisible; Q9SU14; AT. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:UniProtKB-EC. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR003293; Nudix_hydrolase6-like. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR Pfam; PF00293; NUDIX; 1. DR PRINTS; PR01356; GFGPROTEIN. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Complete proteome; KW Cytoplasm; Hydrolase; Magnesium; Membrane; Metal-binding; NAD; KW Nucleus; Reference proteome. FT CHAIN 1 282 Nudix hydrolase 7. FT /FTId=PRO_0000057127. FT DOMAIN 101 233 Nudix hydrolase. {ECO:0000255|PROSITE- FT ProRule:PRU00794}. FT MOTIF 139 160 Nudix box. FT METAL 154 154 Magnesium. {ECO:0000250}. FT METAL 158 158 Magnesium. {ECO:0000250}. FT MUTAGEN 154 154 E->Q: Loss of hydrolase activity. FT {ECO:0000269|PubMed:17660350}. FT CONFLICT 6 6 Q -> L (in Ref. 4; AAM62604). FT {ECO:0000305}. FT CONFLICT 217 217 V -> I (in Ref. 4; AAM62604). FT {ECO:0000305}. FT STRAND 21 24 {ECO:0000244|PDB:4ZB3}. FT HELIX 31 47 {ECO:0000244|PDB:4ZB3}. FT STRAND 52 58 {ECO:0000244|PDB:4ZB3}. FT HELIX 59 64 {ECO:0000244|PDB:4ZB3}. FT HELIX 65 70 {ECO:0000244|PDB:4ZB3}. FT STRAND 74 79 {ECO:0000244|PDB:4ZB3}. FT STRAND 82 88 {ECO:0000244|PDB:4ZB3}. FT STRAND 90 92 {ECO:0000244|PDB:4ZB3}. FT STRAND 102 112 {ECO:0000244|PDB:4ZB3}. FT TURN 113 116 {ECO:0000244|PDB:4ZB3}. FT STRAND 117 126 {ECO:0000244|PDB:4ZB3}. FT TURN 127 132 {ECO:0000244|PDB:4ZB3}. FT STRAND 138 140 {ECO:0000244|PDB:4ZB3}. FT HELIX 147 159 {ECO:0000244|PDB:4ZB3}. FT STRAND 163 174 {ECO:0000244|PDB:4ZB3}. FT STRAND 183 194 {ECO:0000244|PDB:4ZB3}. FT STRAND 202 212 {ECO:0000244|PDB:4ZB3}. FT HELIX 213 218 {ECO:0000244|PDB:4ZB3}. FT HELIX 220 223 {ECO:0000244|PDB:4ZB3}. FT HELIX 226 239 {ECO:0000244|PDB:4ZB3}. FT STRAND 246 252 {ECO:0000244|PDB:4ZB3}. FT STRAND 254 256 {ECO:0000244|PDB:4ZBP}. FT STRAND 258 263 {ECO:0000244|PDB:4ZB3}. FT HELIX 265 273 {ECO:0000244|PDB:4ZBP}. SQ SEQUENCE 282 AA; 31884 MW; EA37FC0F1C2FDCB7 CRC64; MGTRAQQIPL LEGETDNYDG VTVTMVEPMD SEVFTESLRA SLSHWREEGK KGIWIKLPLG LANLVEAAVS EGFRYHHAEP EYLMLVSWIS ETPDTIPANA SHVVGAGALV INKNTKEVLV VQERSGFFKD KNVWKLPTGV INEGEDIWTG VAREVEEETG IIADFVEVLA FRQSHKAILK KKTDMFFLCV LSPRSYDITE QKSEILQAKW MPIQEYVDQP WNKKNEMFKF MANICQKKCE EEYLGFAIVP TTTSSGKESF IYCNADHAKR LKVSRDQASA SL //