NUD23_ARATH
ID NUD23_ARATH Reviewed; 280 AA.
AC P93740; Q1ECD1; Q8LAH1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Nudix hydrolase 23, chloroplastic;
DE Short=AtNUDT23;
DE EC=3.6.1.-;
DE AltName: Full=ADP-ribose pyrophosphatase;
DE EC=3.6.1.13 {ECO:0000269|PubMed:18815383};
DE AltName: Full=FAD diphosphatase;
DE EC=3.6.1.18 {ECO:0000269|PubMed:18815383};
DE Flags: Precursor;
GN Name=NUDT23; Synonyms=NUDX23; OrderedLocusNames=At2g42070;
GN ORFNames=T6D20.4;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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;
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NOMENCLATURE.
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18815383; DOI=10.1104/pp.108.128413;
RA Ogawa T., Yoshimura K., Miyake H., Ishikawa K., Ito D., Tanabe N.,
RA Shigeoka S.;
RT "Molecular characterization of organelle-type Nudix hydrolases in
RT Arabidopsis.";
RL Plant Physiol. 148:1412-1424(2008).
CC -!- FUNCTION: Mediates the hydrolysis of some nucleoside diphosphate
CC derivatives. Can use FAD and ADP-ribose as substrates.
CC {ECO:0000269|PubMed:18815383}.
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:18815383};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10413;
CC Evidence={ECO:0000269|PubMed:18815383};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FAD + H2O = AMP + FMN + 2 H(+); Xref=Rhea:RHEA:13889,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:456215; EC=3.6.1.18;
CC Evidence={ECO:0000269|PubMed:18815383};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13890;
CC Evidence={ECO:0000269|PubMed:18815383};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.1 uM for FAD {ECO:0000269|PubMed:18815383};
CC KM=386 uM for ADP-ribose {ECO:0000269|PubMed:18815383};
CC Vmax=2.1 umol/min/mg enzyme with ADP-ribose as substrate
CC {ECO:0000269|PubMed:18815383};
CC Vmax=0.19 umol/min/mg enzyme with FAD as substrate
CC {ECO:0000269|PubMed:18815383};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18815383}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and
CC inflorescences. {ECO:0000269|PubMed:18815383}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; U90439; AAB63537.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10067.1; -; Genomic_DNA.
DR EMBL; AK221588; BAD95098.1; -; mRNA.
DR EMBL; AY087819; AAM65373.1; -; mRNA.
DR EMBL; BT025803; ABF83693.1; -; mRNA.
DR PIR; E84849; E84849.
DR RefSeq; NP_565965.1; NM_129770.4.
DR AlphaFoldDB; P93740; -.
DR SMR; P93740; -.
DR STRING; 3702.AT2G42070.1; -.
DR PaxDb; P93740; -.
DR PRIDE; P93740; -.
DR ProteomicsDB; 250584; -.
DR EnsemblPlants; AT2G42070.1; AT2G42070.1; AT2G42070.
DR GeneID; 818807; -.
DR Gramene; AT2G42070.1; AT2G42070.1; AT2G42070.
DR KEGG; ath:AT2G42070; -.
DR Araport; AT2G42070; -.
DR TAIR; locus:2064632; AT2G42070.
DR eggNOG; KOG3084; Eukaryota.
DR HOGENOM; CLU_037162_16_0_1; -.
DR InParanoid; P93740; -.
DR OrthoDB; 1602447at2759; -.
DR PhylomeDB; P93740; -.
DR BioCyc; ARA:AT2G42070-MON; -.
DR SABIO-RK; P93740; -.
DR PRO; PR:P93740; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P93740; baseline and differential.
DR Genevisible; P93740; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0047884; F:FAD diphosphatase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042726; P:flavin-containing compound metabolic process; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR029401; Nudix_N.
DR Pfam; PF00293; NUDIX; 1.
DR Pfam; PF14803; Nudix_N_2; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW Chloroplast; FAD; Flavoprotein; FMN; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..75
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 76..280
FT /note="Nudix hydrolase 23, chloroplastic"
FT /id="PRO_0000019965"
FT DOMAIN 120..243
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 154..175
FT /note="Nudix box"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 28
FT /note="T -> S (in Ref. 4; AAM65373)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="S -> F (in Ref. 4; AAM65373)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 30794 MW; 0C813F6FB511CE45 CRC64;
MLKAVQILGW SSGLTISQRL TKTRKSSTVS FISSSLNLSS VTSSSPRRIF SFKPTRMSSS
LPGSDPVANS PTFVSVQSAG DVRKIKFCQW CGGPTKHEIP DGEEKLRAIC THCGKIAYQN
PKMVVGCLIE HEGKVLLCKR NIQPSHGLWT LPAGYLEVGE SAAQGAMRET WEEAGATVEV
ISPFAQLDIP LIGQTYVIFL AKLKNLHFAP GPESLECRLF ALDEIPFDSL AFSSIYVTLN
LYLEDLKKGK LKFHYGTINK RPGSSPSDIR AFSLDYHLQP
