NUD13_ARATH
ID NUD13_ARATH Reviewed; 202 AA.
AC Q52K88; Q29PY9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Nudix hydrolase 13, mitochondrial;
DE Short=AtNUDT13;
DE EC=3.6.1.-;
DE Flags: Precursor;
GN Name=NUDT13; Synonyms=NUDX13; OrderedLocusNames=At3g26690;
GN ORFNames=MLJ15.8;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17824959; DOI=10.1111/j.1742-4658.2007.06009.x;
RA Olejnik K., Murcha M.W., Whelan J., Kraszewska E.;
RT "Cloning and characterization of AtNUDT13, a novel mitochondrial
RT Arabidopsis thaliana Nudix hydrolase specific for long-chain diadenosine
RT polyphosphates.";
RL FEBS J. 274:4877-4885(2007).
RN [6]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 diadenosine 5',5'''-P(1)P(6) hexaphosphate
CC (Ap(6)A), diadenosine 5',5'''-P(1)P(5) pentaphosphate (Ap(5)A) and
CC adenosine tetraphosphate (p(4)A) as substrates, but not diadenosine
CC 5',5'''-P(1)P(4) tetraphosphate (Ap(4)A), diadenosine 5',5'''-P(1)P(3)
CC triphosphate (Ap(3)A), deoxyribonucleoside triphosphates,
CC ribonucleoside triphosphates, diphosphoinositol pentakisphosphate (PP-
CC InsP(5)) and 5-phospho-alpha-D-ribosyl diphosphate (PRPP).
CC {ECO:0000269|PubMed:17824959}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Inhibited by fluoride.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.61 mM for diadenosine 5',5'''-P(1)P(6) hexaphosphate
CC {ECO:0000269|PubMed:17824959};
CC Vmax=26.5 umol/min/mg enzyme with diadenosine 5',5'''-P(1)P(6)
CC hexaphosphate as substrate {ECO:0000269|PubMed:17824959};
CC Note=Reducing conditions are required for the hydrolytic activity.;
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:17824959};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:17824959};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17824959}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17824959}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and
CC inflorescences. {ECO:0000269|PubMed:18815383}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:18815383}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AB026648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE77199.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77200.1; -; Genomic_DNA.
DR EMBL; BT021980; AAY17417.1; -; mRNA.
DR EMBL; BT024767; ABD59105.1; -; mRNA.
DR RefSeq; NP_189303.1; NM_113580.2.
DR RefSeq; NP_850636.1; NM_180305.2.
DR AlphaFoldDB; Q52K88; -.
DR SMR; Q52K88; -.
DR STRING; 3702.AT3G26690.2; -.
DR PaxDb; Q52K88; -.
DR PRIDE; Q52K88; -.
DR ProteomicsDB; 234942; -.
DR EnsemblPlants; AT3G26690.1; AT3G26690.1; AT3G26690.
DR EnsemblPlants; AT3G26690.2; AT3G26690.2; AT3G26690.
DR GeneID; 822281; -.
DR Gramene; AT3G26690.1; AT3G26690.1; AT3G26690.
DR Gramene; AT3G26690.2; AT3G26690.2; AT3G26690.
DR KEGG; ath:AT3G26690; -.
DR Araport; AT3G26690; -.
DR TAIR; locus:2090842; AT3G26690.
DR eggNOG; KOG2839; Eukaryota.
DR HOGENOM; CLU_037162_5_2_1; -.
DR OMA; GERQIDP; -.
DR OrthoDB; 1324716at2759; -.
DR PhylomeDB; Q52K88; -.
DR BioCyc; ARA:AT3G26690-MON; -.
DR BRENDA; 3.6.1.60; 399.
DR PRO; PR:Q52K88; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q52K88; baseline and differential.
DR Genevisible; Q52K88; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0034432; F:bis(5'-adenosyl)-pentaphosphatase activity; IDA:TAIR.
DR GO; GO:0016787; F:hydrolase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT CHAIN ?..202
FT /note="Nudix hydrolase 13, mitochondrial"
FT /id="PRO_0000019956"
FT DOMAIN 18..167
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 65..86
FT /note="Nudix box"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 202 AA; 23187 MW; C8B20342322B8297 CRC64;
MSNLSARTGR DHQRYDNNFR LVSGCIPYRL VKDEEEDSTS VDFENKLQVL MISSPNRHDL
VFPKGGWEDD ETVLEAASRE AMEEAGVKGI LREDPLGVWE FRSKSSSVEA DCCLGGGCKG
YMFALEVKEE LAIWPEQDDR ERRWLNVKEA LELCRYEWMQ SALEEFLRVM AEEGSTKEDS
LAISSISNRG ERQIDPRYCF VV
