ID A0A1P8B8M5_ARATH Unreviewed; 282 AA. AC A0A1P8B8M5; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 03-AUG-2022, entry version 27. DE RecName: Full=Nudix hydrolase {ECO:0000256|RuleBase:RU368106}; DE Short=AtNUDT {ECO:0000256|RuleBase:RU368106}; DE EC=3.6.1.13 {ECO:0000256|RuleBase:RU368106}; DE EC=3.6.1.22 {ECO:0000256|RuleBase:RU368106}; DE AltName: Full=ADP-ribose pyrophosphatase {ECO:0000256|RuleBase:RU368106}; DE AltName: Full=NADH pyrophosphatase {ECO:0000256|RuleBase:RU368106}; GN Name=NUDT10 {ECO:0000313|EMBL:ANM67948.1}; GN Synonyms=ATNUDT10 {ECO:0000313|EMBL:ANM67948.1}, nudix hydrolase GN homolog 10 {ECO:0000313|EMBL:ANM67948.1}; GN OrderedLocusNames=At4g25434 {ECO:0000313|Araport:AT4G25434, GN ECO:0000313|EMBL:ANM67948.1}; 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 {ECO:0000313|EMBL:ANM67948.1, ECO:0000313|Proteomes:UP000006548}; RN [1] {ECO:0000313|EMBL:ANM67948.1, ECO:0000313|Proteomes:UP000006548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; RX PubMed=10617198; DOI=10.1038/47134; RG EU; RG CSHL and WU Arabidopsis Sequencing Project; 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] {ECO:0000313|Proteomes:UP000006548} RP GENOME REANNOTATION. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; 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). CC -!- FUNCTION: Mediates the hydrolysis of some nucleoside diphosphate CC derivatives, possibly using both NADH and ADP-ribose as substrates. CC {ECO:0000256|RuleBase:RU368106}. 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:0000256|RuleBase:RU368106}; 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:0000256|RuleBase:RU368106}; 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:0000256|RuleBase:RU368106}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU368106}; CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. CC {ECO:0000256|ARBA:ARBA00005582, ECO:0000256|RuleBase:RU368106}. 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; CP002687; ANM67948.1; -; Genomic_DNA. DR RefSeq; NP_001329739.1; NM_001341732.1. DR SMR; A0A1P8B8M5; -. DR ProteomicsDB; 203879; -. DR DNASU; 828648; -. DR EnsemblPlants; AT4G25434.10; AT4G25434.10; AT4G25434. DR GeneID; 828648; -. DR Gramene; AT4G25434.10; AT4G25434.10; AT4G25434. DR Araport; AT4G25434; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; A0A1P8B8M5; baseline and differential. DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule. DR GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-UniRule. 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 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368106}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU368106}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU368106}; KW Reference proteome {ECO:0000313|Proteomes:UP000006548}. FT DOMAIN 110..240 FT /note="Nudix hydrolase" FT /evidence="ECO:0000259|PROSITE:PS51462" SQ SEQUENCE 282 AA; 32369 MW; D99472EA3D67B075 CRC64; MSDQEAPLRN GVEHKIFEVL PFVDDDYGGV IVEMKTPMDT KNFVAALRDS FEQWRLQGKK GVWLNLPLSH VNLVEPAVKE GFRYHHAEPT YLMLVYWIPE AESTIPLNAS HRVRVGAVVL NHNKEILVVQ EKYGSLCGSG IWKIPTGVVD EGEEIFAAAI REVKEETGID TEFLEILAFC QTHESFFAKS DLFFVCLLRP TSFDIQKQDL EIEAAQWMRF EDSASQPITH KNDLFKDIHH ICSMKMEKSY SGFSKKPITT FFDDKLGYLY LNKQEDMEQP IS //