NUDT2_ARATH
ID NUDT2_ARATH Reviewed; 278 AA.
AC Q94B74; Q9FGJ2;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Nudix hydrolase 2 {ECO:0000303|PubMed:15878881};
DE Short=AtNUDT2 {ECO:0000303|PubMed:15878881};
DE EC=3.6.1.- {ECO:0000269|PubMed:15878881};
DE AltName: Full=ADP-ribose pyrophosphatase {ECO:0000303|PubMed:15878881};
DE EC=3.6.1.13 {ECO:0000269|PubMed:15878881};
DE AltName: Full=NADH pyrophosphatase {ECO:0000303|PubMed:15878881};
DE EC=3.6.1.22 {ECO:0000269|PubMed:15878881};
GN Name=NUDT2 {ECO:0000303|PubMed:15878881}; Synonyms=NUDX2;
GN OrderedLocusNames=At5g47650 {ECO:0000312|Araport:AT5G47650};
GN ORFNames=MNJ7.24 {ECO:0000312|EMBL:BAB09091.1};
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION IN VITRO, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
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 [5]
RP FUNCTION, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=18798872; DOI=10.1111/j.1365-313x.2008.03686.x;
RA Ogawa T., Ishikawa K., Harada K., Fukusaki E., Yoshimura K., Shigeoka S.;
RT "Overexpression of an ADP-ribose pyrophosphatase, AtNUDX2, confers enhanced
RT tolerance to oxidative stress in Arabidopsis plants.";
RL Plant J. 57:289-301(2009).
CC -!- FUNCTION: Probably mediates the hydrolysis of some nucleoside
CC diphosphate derivatives. In vitro, it can use both NADH and ADP-ribose
CC as substrates; however the relevance of such substrates in vivo is
CC unclear. Confers tolerance to oxidative stress (PubMed:18798872).
CC {ECO:0000269|PubMed:15878881, ECO:0000269|PubMed:18798872}.
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; Evidence={ECO:0000269|PubMed:15878881};
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; Evidence={ECO:0000269|PubMed:15878881};
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 Evidence={ECO:0000269|PubMed:15878881};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8IU60};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8IU60};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16.9 uM for ADP-ribose (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:15878881};
CC KM=22.3 uM for NADH (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:15878881};
CC Vmax=0.20 umol/min/mg enzyme with ADP-ribose as substrate (at pH 8
CC and 37 degrees Celsius) {ECO:0000269|PubMed:15878881};
CC Vmax=0.16 umol/min/mg enzyme with NADH as substrate (at pH 8 and 37
CC degrees Celsius) {ECO:0000269|PubMed:15878881};
CC Note=kcat is 0.12 sec(-1) with ADP-ribose as substrate (at pH 8 and
CC 37 degrees Celsius) (PubMed:15878881). kcat is 0.01 sec(-1) with NADH
CC as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15878881).
CC {ECO:0000269|PubMed:15878881};
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and leaves.
CC {ECO:0000269|PubMed:15878881}.
CC -!- INDUCTION: By paraquat, drought and high salinity.
CC {ECO:0000269|PubMed:18798872}.
CC -!- MISCELLANEOUS: Overexpression of NUTD2 confers enhanced tolerance to
CC oxidative stress. {ECO:0000269|PubMed:18798872}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09091.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB025628; BAB09091.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED95546.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70008.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70010.1; -; Genomic_DNA.
DR EMBL; AY042806; AAK68746.1; -; mRNA.
DR EMBL; AY064646; AAL47357.1; -; mRNA.
DR RefSeq; NP_001331650.1; NM_001344739.1.
DR RefSeq; NP_001331652.1; NM_001344737.1.
DR RefSeq; NP_568687.1; NM_124139.4.
DR AlphaFoldDB; Q94B74; -.
DR SMR; Q94B74; -.
DR BioGRID; 20064; 1.
DR STRING; 3702.AT5G47650.1; -.
DR PaxDb; Q94B74; -.
DR PRIDE; Q94B74; -.
DR ProteomicsDB; 248851; -.
DR EnsemblPlants; AT5G47650.1; AT5G47650.1; AT5G47650.
DR EnsemblPlants; AT5G47650.3; AT5G47650.3; AT5G47650.
DR EnsemblPlants; AT5G47650.5; AT5G47650.5; AT5G47650.
DR GeneID; 834816; -.
DR Gramene; AT5G47650.1; AT5G47650.1; AT5G47650.
DR Gramene; AT5G47650.3; AT5G47650.3; AT5G47650.
DR Gramene; AT5G47650.5; AT5G47650.5; AT5G47650.
DR KEGG; ath:AT5G47650; -.
DR Araport; AT5G47650; -.
DR TAIR; locus:2168993; AT5G47650.
DR eggNOG; KOG0648; Eukaryota.
DR HOGENOM; CLU_054299_1_0_1; -.
DR InParanoid; Q94B74; -.
DR PhylomeDB; Q94B74; -.
DR BioCyc; ARA:AT5G47650-MON; -.
DR BRENDA; 3.6.1.13; 399.
DR SABIO-RK; Q94B74; -.
DR PRO; PR:Q94B74; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94B74; baseline and differential.
DR Genevisible; Q94B74; AT.
DR GO; GO:0005829; C:cytosol; ISM:TAIR.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IDA:TAIR.
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:0006979; P:response to oxidative stress; IMP:TAIR.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR003293; Nudix_hydrolase6-like.
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.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; NAD; Reference proteome.
FT CHAIN 1..278
FT /note="Nudix hydrolase 2"
FT /id="PRO_0000057122"
FT DOMAIN 110..242
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 147..168
FT /note="Nudix box"
FT /evidence="ECO:0000305"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT CONFLICT 125
FT /note="E -> EK (in Ref. 1; BAB09091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 278 AA; 31611 MW; C0907A87DD5D2A7D CRC64;
MSASSSSTNP MSREDATTLL PSVQDKYGGV MTEMTHPMDP SLFSTLLRSS LSTWTLQGKK
GVWIKLPKQL IGLAETAVKE GFWFHHAEKD YLMLVYWIPK EDDTLPANAS HRVGIGAFVI
NHNKEVLVVQ EKTGRFQGQG IWKFPTGVVN EGEDIHDGSV REVKEETGVD TEFDQILAFR
QTHKAFFGKS DLFFVCMLKP LSLEINAQES EIEAAQWMPW EEYINQPFVQ NYELLRYMTD
ICSAKTNGDY EGFTPLRVSA PDQQGNLYYN TRDLHSRN
