NUD10_ARATH
ID NUD10_ARATH Reviewed; 277 AA.
AC Q6NPD7; O65616; Q2V3F2;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Nudix hydrolase 10;
DE Short=AtNUDT10 {ECO:0000303|PubMed:15878881};
DE EC=3.6.1.-;
DE AltName: Full=ADP-ribose pyrophosphatase;
DE EC=3.6.1.13 {ECO:0000305|PubMed:15878881};
DE AltName: Full=NADH pyrophosphatase;
DE EC=3.6.1.22;
GN Name=NUDT10; Synonyms=NUDX10; OrderedLocusNames=At4g25434;
GN ORFNames=T30C3.4;
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=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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION IN VITRO, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP 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: May mediate the hydrolysis of some nucleoside diphosphate
CC derivatives. In vitro, uses both ADP-ribose and NADH as substrates;
CC however the relevance of such substrates in vivo is unclear.
CC {ECO:0000305|PubMed:15878881}.
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:0000305|PubMed:15878881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10413;
CC Evidence={ECO:0000305|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;
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; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=27.4 uM for ADP-ribose {ECO:0000269|PubMed:15878881};
CC Vmax=0.10 umol/min/mg enzyme with ADP-ribose as substrate
CC {ECO:0000269|PubMed:15878881};
CC Note=kcat is 0.06 sec(-1) with ADP-ribose as substrate.
CC {ECO:0000269|PubMed:15878881};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NPD7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NPD7-2; Sequence=VSP_037557;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and, at lower level,
CC leaves. {ECO:0000269|PubMed:15878881}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18182.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL022197; CAA18182.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85058.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85059.1; -; Genomic_DNA.
DR EMBL; BT010987; AAR24765.1; -; mRNA.
DR EMBL; BT010765; AAR23735.1; -; mRNA.
DR PIR; T05803; T05803.
DR RefSeq; NP_001031713.1; NM_001036636.2. [Q6NPD7-2]
DR RefSeq; NP_849443.2; NM_179112.3. [Q6NPD7-1]
DR AlphaFoldDB; Q6NPD7; -.
DR SMR; Q6NPD7; -.
DR STRING; 3702.AT4G25434.2; -.
DR ProteomicsDB; 248849; -. [Q6NPD7-1]
DR DNASU; 828648; -.
DR EnsemblPlants; AT4G25434.1; AT4G25434.1; AT4G25434. [Q6NPD7-1]
DR EnsemblPlants; AT4G25434.2; AT4G25434.2; AT4G25434. [Q6NPD7-2]
DR GeneID; 828648; -.
DR Gramene; AT4G25434.1; AT4G25434.1; AT4G25434. [Q6NPD7-1]
DR Gramene; AT4G25434.2; AT4G25434.2; AT4G25434. [Q6NPD7-2]
DR KEGG; ath:AT4G25434; -.
DR Araport; AT4G25434; -.
DR TAIR; locus:1005716200; AT4G25434.
DR eggNOG; KOG0648; Eukaryota.
DR InParanoid; Q6NPD7; -.
DR PhylomeDB; Q6NPD7; -.
DR BioCyc; ARA:AT4G25434-MON; -.
DR SABIO-RK; Q6NPD7; -.
DR PRO; PR:Q6NPD7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q6NPD7; baseline and differential.
DR Genevisible; Q6NPD7; 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 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 Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding; NAD;
KW Reference proteome.
FT CHAIN 1..277
FT /note="Nudix hydrolase 10"
FT /id="PRO_0000057130"
FT DOMAIN 97..235
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 142..163
FT /note="Nudix box"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 163
FT /note="G -> GVRRSIYLNVNQSTINIYNLTFSYIYLQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037557"
SQ SEQUENCE 277 AA; 31816 MW; A609D65AB5D2EE3F CRC64;
MSDQEAPLRN GVEHKIFEVL PFVDDDYGGV IVEMKTPMDT KNFVAALRDS FEQWRLQGKK
GVWLNLPLSH VNLVEPAVKE GFRYHHAEPT YLMLVYWIPE AESTIPLNAS HRVRVGAVVL
NHNKEEKYGS LCGSGIWKIP TGVVDEGEEI FAAAIREVKE ETGIDTEFLE ILAFCQTHES
FFAKSDLFFV CLLRPTSFDI QKQDLEIEAA QWMRFEDSAS QPITHKNDLF KDIHHICSMK
MEKSYSGFSK KPITTFFDDK LGYLYLNKQE DMEQPIS
