ID   NUDT4_ARATH             Reviewed;         207 AA.
AC   Q9LE73; Q0WU23;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   04-NOV-2026, entry version 137.
DE   RecName: Full=Nudix hydrolase 4;
DE            Short=AtNUDT4;
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;
GN   Name=NUDT4; Synonyms=NUDX4; OrderedLocusNames=At1g18300;
GN   ORFNames=F15H18.18;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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).
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. {ECO:0000269|PubMed:15878881}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-D-ribose + H2O = D-ribose 5-phosphate + AMP + 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=NAD(+) + H2O = beta-nicotinamide D-ribonucleotide + AMP + 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=NADH + H2O = reduced beta-nicotinamide D-ribonucleotide + AMP
CC         + 2 H(+); Xref=Rhea:RHEA:48868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:90832, ChEBI:CHEBI:456215;
CC         EC=3.6.1.22;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems and leaves.
CC       {ECO:0000269|PubMed:15878881}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR   EMBL; AC013354; AAF25994.1; -; Genomic_DNA.
DR   EMBL; AC069551; AAF78378.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29699.1; -; Genomic_DNA.
DR   EMBL; OZ408683; CAO7027805.1; -; Genomic_DNA.
DR   EMBL; BT003060; AAO23625.1; -; mRNA.
DR   EMBL; AK227367; BAE99375.1; -; mRNA.
DR   RefSeq; NP_173266.1; NM_101688.3.
DR   AlphaFoldDB; Q9LE73; -.
DR   SMR; Q9LE73; -.
DR   FunCoup; Q9LE73; 1404.
DR   STRING; 3702.Q9LE73; -.
DR   PaxDb; 3702-Q9LE73; -.
DR   GeneID; 838410; -.
DR   KEGG; ath:AT1G18300; -.
DR   Araport; AT1G18300; -.
DR   TAIR; AT1G18300; NUDT4.
DR   eggNOG; KOG2839; Eukaryota.
DR   HOGENOM; CLU_037162_5_2_1; -.
DR   InParanoid; Q9LE73; -.
DR   OMA; ACKFFYP; -.
DR   OrthoDB; 2011998at2759; -.
DR   PhylomeDB; Q9LE73; -.
DR   BioCyc; ARA:AT1G18300-MONOMER; -.
DR   PRO; PR:Q9LE73; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   Proteomes; UP001984100; Chromosome 1.
DR   ExpressionAtlas; Q9LE73; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; ISM:TAIR.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISM:TAIR.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052745; F:inositol phosphate phosphatase activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0052845; F:inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity; IBA:GO_Central.
DR   GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:RHEA.
DR   GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:RHEA.
DR   GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR   GO; GO:0016036; P:cellular response to phosphate starvation; IEA:UniProtKB-ARBA.
DR   GO; GO:1901909; P:diadenosine hexaphosphate catabolic process; IBA:GO_Central.
DR   GO; GO:0071544; P:diphosphoinositol polyphosphate catabolic process; IBA:GO_Central.
DR   CDD; cd04666; NUDIX_DIPP2_like_Nudt4; 1.
DR   FunFam; 3.90.79.10:FF:000022; Nudix hydrolase 17, mitochondrial; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR047198; DDP-like_NUDIX.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   PANTHER; PTHR12629; DIPHOSPHOINOSITOL POLYPHOSPHATE PHOSPHOHYDROLASE; 1.
DR   PANTHER; PTHR12629:SF15; NUDIX HYDROLASE 4; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; NAD; Reference proteome.
FT   CHAIN           1..207
FT                   /note="Nudix hydrolase 4"
FT                   /id="PRO_0000057124"
FT   DOMAIN          58..194
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           101..122
FT                   /note="Nudix box"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   207 AA;  23701 MW;  0E266BF7519129E1 CRC64;
     MTGFSVSLFV SNLSNVASYL SPIFENIPST KVVPAQIEKV VSLVSRTGRD LQRYDHAGYR
     QVVGCVPYRY KKQEVNGVET QVIQVLLVSA QKGKGMLFPK GGWETDESME EAALRETIEE
     AGVTGELEEK LGKWQYKSKR HSIIHDGYMF ALLVSQEFER WPEAEMRQRR WVSLDEAREV
     CQNWWMREAL EAFINLKCLA DDDESGN
//