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 22-APR-2020, entry version 136. 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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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., Pohl T., RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., RA Johnson D., 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., Du H., RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., RA Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."; RL Nature 402:769-777(1999). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). 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., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA 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 hydrolase RT 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., Bautor J., RA Parker J.E.; RT "Salicylic acid-independent ENHANCED DISEASE SUSCEPTIBILITY1 signaling in RT Arabidopsis immunity and cell death is regulated by the monooxygenase FMO1 RT and the Nudix hydrolase NUDT7."; RL Plant Cell 18:1038-1051(2006). RN [8] RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND RP 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, modulates RT two distinct defense response pathways and is involved in maintaining redox RT 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 transducing RT 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 not 8- CC oxo-dGTP, cyclic ADP-ribose, GDP-manose, UDP-glucose, ATP, or GTP. CC 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: CC Reaction=ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+); CC Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; CC EC=3.6.1.13; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + NAD(+) = AMP + beta-nicotinamide D-ribonucleotide + 2 CC H(+); Xref=Rhea:RHEA:11800, ChEBI:CHEBI:14649, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:456215; CC EC=3.6.1.22; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + NADH = AMP + 2 H(+) + reduced beta-nicotinamide D- CC ribonucleotide; Xref=Rhea:RHEA:48868, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57945, ChEBI:CHEBI:90832, CC ChEBI:CHEBI:456215; EC=3.6.1.22; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- ACTIVITY 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}. Cytoplasm CC {ECO:0000269|PubMed:22068106}. Cell membrane CC {ECO:0000269|PubMed:22068106}. Note=Localized at the plasma membrane CC when in complex with GG2, but present in the cytoplasm when associated CC with GG1. Detected in the cytoplasm and nucleus when interacting with CC 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, 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 species CC and NADH. {ECO:0000269|PubMed:16328543, ECO:0000269|PubMed:16531493, CC ECO:0000269|PubMed:17660350}. CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}. 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_117341.5. [Q9SU14-1] DR RefSeq; NP_849367.1; NM_179036.4. [Q9SU14-1] DR RefSeq; NP_849368.1; NM_179037.3. [Q9SU14-1] 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 SMR; Q9SU14; -. 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 Gramene; AT4G12720.1; AT4G12720.1; AT4G12720. [Q9SU14-1] DR Gramene; AT4G12720.2; AT4G12720.2; AT4G12720. [Q9SU14-1] DR Gramene; AT4G12720.3; AT4G12720.3; AT4G12720. [Q9SU14-1] DR KEGG; ath:AT4G12720; -. DR Araport; AT4G12720; -. DR HOGENOM; CLU_054299_1_2_1; -. DR InParanoid; Q9SU14; -. DR PhylomeDB; Q9SU14; -. DR BioCyc; ARA:AT4G12720-MONOMER; -. DR BRENDA; 3.6.1.13; 399. DR SABIO-RK; Q9SU14; -. 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; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IBA:GO_Central. DR GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0035529; F:NADH pyrophosphatase activity; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf. DR InterPro; IPR003293; Nudix_hydrolase6-like. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR040618; Pre-Nudix. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF18290; Nudix_hydro; 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; Cytoplasm; Hydrolase; KW Magnesium; Membrane; Metal-binding; NAD; Nucleus; Reference proteome. FT CHAIN 1..282 FT /note="Nudix hydrolase 7" FT /id="PRO_0000057127" FT DOMAIN 101..233 FT /note="Nudix hydrolase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794" FT MOTIF 139..160 FT /note="Nudix box" FT METAL 154 FT /note="Magnesium" FT /evidence="ECO:0000250" FT METAL 158 FT /note="Magnesium" FT /evidence="ECO:0000250" FT MUTAGEN 154 FT /note="E->Q: Loss of hydrolase activity." FT /evidence="ECO:0000269|PubMed:17660350" FT CONFLICT 6 FT /note="Q -> L (in Ref. 4; AAM62604)" FT /evidence="ECO:0000305" FT CONFLICT 217 FT /note="V -> I (in Ref. 4; AAM62604)" FT /evidence="ECO:0000305" FT STRAND 21..24 FT /evidence="ECO:0000244|PDB:4ZB3" FT HELIX 31..47 FT /evidence="ECO:0000244|PDB:4ZB3" FT STRAND 52..58 FT /evidence="ECO:0000244|PDB:4ZB3" FT HELIX 59..64 FT /evidence="ECO:0000244|PDB:4ZB3" FT HELIX 65..70 FT /evidence="ECO:0000244|PDB:4ZB3" FT STRAND 74..79 FT /evidence="ECO:0000244|PDB:4ZB3" FT STRAND 82..88 FT /evidence="ECO:0000244|PDB:4ZB3" FT STRAND 90..92 FT /evidence="ECO:0000244|PDB:4ZB3" FT STRAND 102..112 FT /evidence="ECO:0000244|PDB:4ZB3" FT TURN 113..116 FT /evidence="ECO:0000244|PDB:4ZB3" FT STRAND 117..126 FT /evidence="ECO:0000244|PDB:4ZB3" FT TURN 127..132 FT /evidence="ECO:0000244|PDB:4ZB3" FT STRAND 138..140 FT /evidence="ECO:0000244|PDB:4ZB3" FT HELIX 147..159 FT /evidence="ECO:0000244|PDB:4ZB3" FT STRAND 163..174 FT /evidence="ECO:0000244|PDB:4ZB3" FT STRAND 183..194 FT /evidence="ECO:0000244|PDB:4ZB3" FT STRAND 202..212 FT /evidence="ECO:0000244|PDB:4ZB3" FT HELIX 213..218 FT /evidence="ECO:0000244|PDB:4ZB3" FT HELIX 220..223 FT /evidence="ECO:0000244|PDB:4ZB3" FT HELIX 226..239 FT /evidence="ECO:0000244|PDB:4ZB3" FT STRAND 246..252 FT /evidence="ECO:0000244|PDB:4ZB3" FT STRAND 254..256 FT /evidence="ECO:0000244|PDB:4ZBP" FT STRAND 258..263 FT /evidence="ECO:0000244|PDB:4ZB3" FT HELIX 265..273 FT /evidence="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 //