NUDT7_ARATH
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 03-AUG-2022, entry version 142.
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}.
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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 AlphaFoldDB; Q9SU14; -.
DR SMR; Q9SU14; -.
DR BioGRID; 12181; 9.
DR PRIDE; Q9SU14; -.
DR ProteomicsDB; 248853; -. [Q9SU14-1]
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-MON; -.
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 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 PANTHER; PTHR13994; PTHR13994; 1.
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 BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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:0007829|PDB:4ZB3"
FT HELIX 31..47
FT /evidence="ECO:0007829|PDB:4ZB3"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:4ZB3"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:4ZB3"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:4ZB3"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:4ZB3"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:4ZB3"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:4ZB3"
FT STRAND 102..112
FT /evidence="ECO:0007829|PDB:4ZB3"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:4ZB3"
FT STRAND 117..126
FT /evidence="ECO:0007829|PDB:4ZB3"
FT TURN 127..132
FT /evidence="ECO:0007829|PDB:4ZB3"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:4ZB3"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:4ZB3"
FT STRAND 163..174
FT /evidence="ECO:0007829|PDB:4ZB3"
FT STRAND 183..194
FT /evidence="ECO:0007829|PDB:4ZB3"
FT STRAND 202..212
FT /evidence="ECO:0007829|PDB:4ZB3"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:4ZB3"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:4ZB3"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:4ZB3"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:4ZB3"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:4ZBP"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:4ZB3"
FT HELIX 265..273
FT /evidence="ECO:0007829|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
