NUDT9_ARATH
ID NUDT9_ARATH Reviewed; 311 AA.
AC Q8VYR2; Q8GXK4; Q9LX75;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Nudix hydrolase 9;
DE Short=AtNUDT9;
DE EC=3.6.1.-;
GN Name=NUDT9; Synonyms=NUDX9; OrderedLocusNames=At3g46200;
GN ORFNames=F12M12.170;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-311.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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: Probably mediates the hydrolysis of some nucleoside
CC diphosphate derivatives. {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC42814.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB90947.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL355775; CAB90947.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78127.1; -; Genomic_DNA.
DR EMBL; AY070078; AAL49773.1; -; mRNA.
DR EMBL; AY117353; AAM51428.1; -; mRNA.
DR EMBL; AK118191; BAC42814.1; ALT_INIT; mRNA.
DR PIR; T49261; T49261.
DR RefSeq; NP_190206.2; NM_114489.5.
DR AlphaFoldDB; Q8VYR2; -.
DR SMR; Q8VYR2; -.
DR STRING; 3702.AT3G46200.1; -.
DR PaxDb; Q8VYR2; -.
DR ProteomicsDB; 250555; -.
DR DNASU; 823765; -.
DR EnsemblPlants; AT3G46200.1; AT3G46200.1; AT3G46200.
DR GeneID; 823765; -.
DR Gramene; AT3G46200.1; AT3G46200.1; AT3G46200.
DR KEGG; ath:AT3G46200; -.
DR Araport; AT3G46200; -.
DR TAIR; locus:2075336; AT3G46200.
DR eggNOG; ENOG502QRSW; Eukaryota.
DR HOGENOM; CLU_061819_0_0_1; -.
DR InParanoid; Q8VYR2; -.
DR OMA; PEPQAVC; -.
DR OrthoDB; 1587403at2759; -.
DR PhylomeDB; Q8VYR2; -.
DR PRO; PR:Q8VYR2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VYR2; baseline and differential.
DR Genevisible; Q8VYR2; AT.
DR GO; GO:0005829; C:cytosol; ISM:TAIR.
DR GO; GO:0052751; F:GDP-mannose hydrolase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071242; P:cellular response to ammonium ion; IMP:TAIR.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..311
FT /note="Nudix hydrolase 9"
FT /id="PRO_0000057129"
FT DOMAIN 131..298
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 192..213
FT /note="Nudix box"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 311 AA; 34717 MW; 373A8FEF3842BDD5 CRC64;
MAKLAEEMNP EGSRYQLLLS CPSGLSPSQV SVDFSKSHDR IPRQDPGLED SISQVWEQRS
QGNSSLFNGQ KFRYGGYCLD DDDGSTNEVP HVCLRLGLTD YRTFVGTNLS SLWEKFLVTS
EDDSVRCRHT SSPLGNGAVI ETSDKKIIVL RRSNNVGEFP GHYVFPGGHP EPTAVGIDYH
QLENNVQTGE VLNKKVTQEM FDSIICEVVE ETGIPASSLS SPLFIGISRR ELNVRPAMFF
YLKCSHHSDD IQRLYSSAED GFESTQLHTV SLDELKMMTS RMPGCHHGGF ALYELMLQRL
KNTKETSLIA T
