NUD14_ARATH
ID NUD14_ARATH Reviewed; 309 AA.
AC Q9SZ63; Q4R0T9; Q941C3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Nudix hydrolase 14, chloroplastic;
DE Short=AtNUDT14;
DE EC=3.6.1.21;
DE AltName: Full=ADP-sugar diphosphatase;
DE Short=AtASPP;
DE Flags: Precursor;
GN Name=NUDT14; Synonyms=ASPP, NUDX14; OrderedLocusNames=At4g11980;
GN ORFNames=F16J13.50;
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 [MRNA], FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=16774931; DOI=10.1093/pcp/pcj065;
RA Munoz F.J., Baroja-Fernandez E., Moran-Zorzano M.T., Alonso-Casajus N.,
RA Pozueta-Romero J.;
RT "Cloning, expression and characterization of a Nudix hydrolase that
RT catalyzes the hydrolytic breakdown of ADP-glucose linked to starch
RT biosynthesis in Arabidopsis thaliana.";
RL Plant Cell Physiol. 47:926-934(2006).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP 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 ADP-glucose, ADP-mannose and ADP-ribose as
CC substrates. Regulates the intracellular ADP-glucose levels linked to
CC starch biosynthesis. {ECO:0000269|PubMed:16774931}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-sugar + H2O = AMP + alpha-D-aldose 1-phosphate.;
CC EC=3.6.1.21;
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=13.0 uM for ADP-ribose {ECO:0000269|PubMed:18815383};
CC KM=1235 uM for ADP-glucose {ECO:0000269|PubMed:18815383};
CC Vmax=12.5 umol/min/mg enzyme with ADP-ribose as substrate
CC {ECO:0000269|PubMed:18815383};
CC Vmax=30.0 umol/min/mg enzyme with ADP-glucose as substrate
CC {ECO:0000269|PubMed:18815383};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16774931}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16774931, ECO:0000269|PubMed:18815383}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB40939.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78241.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ748742; CAG38620.1; -; mRNA.
DR EMBL; AL049638; CAB40939.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161533; CAB78241.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83079.1; -; Genomic_DNA.
DR EMBL; AY052271; AAK96464.1; -; mRNA.
DR EMBL; BT001146; AAN64537.1; -; mRNA.
DR PIR; T06605; T06605.
DR RefSeq; NP_567384.1; NM_117268.3.
DR AlphaFoldDB; Q9SZ63; -.
DR SMR; Q9SZ63; -.
DR STRING; 3702.AT4G11980.1; -.
DR PaxDb; Q9SZ63; -.
DR PRIDE; Q9SZ63; -.
DR ProteomicsDB; 248735; -.
DR EnsemblPlants; AT4G11980.1; AT4G11980.1; AT4G11980.
DR GeneID; 826805; -.
DR Gramene; AT4G11980.1; AT4G11980.1; AT4G11980.
DR KEGG; ath:AT4G11980; -.
DR Araport; AT4G11980; -.
DR TAIR; locus:2118061; AT4G11980.
DR eggNOG; KOG3041; Eukaryota.
DR HOGENOM; CLU_070130_1_1_1; -.
DR InParanoid; Q9SZ63; -.
DR OMA; GCDEFIP; -.
DR OrthoDB; 957911at2759; -.
DR PhylomeDB; Q9SZ63; -.
DR BioCyc; ARA:AT4G11980-MON; -.
DR SABIO-RK; Q9SZ63; -.
DR PRO; PR:Q9SZ63; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZ63; baseline and differential.
DR Genevisible; Q9SZ63; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0080042; F:ADP-glucose pyrophosphohydrolase activity; IDA:TAIR.
DR GO; GO:0080041; F:ADP-ribose pyrophosphohydrolase activity; IDA:TAIR.
DR GO; GO:0019144; F:ADP-sugar diphosphatase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006753; P:nucleoside phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0019693; P:ribose phosphate metabolic process; IBA:GO_Central.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Magnesium; Manganese; Metal-binding; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 61..309
FT /note="Nudix hydrolase 14, chloroplastic"
FT /id="PRO_0000019957"
FT DOMAIN 139..292
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 179..200
FT /note="Nudix box"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 309 AA; 34254 MW; 4454120E3B7998AF CRC64;
MAGFTLLPSR LLAFPSRALP RRLHHHHAKL ILRCKMSSSS SSLTQSITLP SQPNEPVLVS
ATAGISSSDF RDAIDSSLFR NWLRNLESES GILADGSMTL KQVLIQGVDM FGKRIGFLKF
KADIFDKETG QKVPGIVFAR GPAVAVLILL ESDGETYAVL TEQVRVPTGK IVLELPAGML
DDDKGDFVGT AVREVEEEIG IKLKKEDMVD LTAFLDPSTG YRIFPSPGGC DEEMSVFLYR
GQVEKETIRQ LQGKETGLRE HGEFIKVRLI PYRELWRKTA DAKVLMSIGL YEMAQREGLV
SSQRLKPNS
