NUDT6_ARATH
ID NUDT6_ARATH Reviewed; 283 AA.
AC Q9SJC4;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Nudix hydrolase 6 {ECO:0000303|PubMed:15878881};
DE Short=AtNUDT6 {ECO:0000303|PubMed:15878881};
DE EC=3.6.1.- {ECO:0000269|PubMed:15878881};
DE AltName: Full=ADP-ribose pyrophosphatase {ECO:0000305};
DE EC=3.6.1.13 {ECO:0000269|PubMed:15878881};
DE AltName: Full=NADH pyrophosphatase {ECO:0000305};
DE EC=3.6.1.22 {ECO:0000269|PubMed:15878881};
GN Name=NUDT6 {ECO:0000303|PubMed:15878881}; Synonyms=NUDX6 {ECO:0000305};
GN OrderedLocusNames=At2g04450 {ECO:0000312|Araport:AT2G04450};
GN ORFNames=T1O3.14 {ECO:0000312|EMBL:AAD25833.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 [MRNA] OF 136-283.
RA Gomez-Buitrago A.M., Lindsrtom L., Raina R.;
RT "Identification of Arabidopsis genes differentially expressed in response
RT to virulent and avirulent strains of Pseudomonas syringae and salicylic
RT acid.";
RL Submitted (FEB-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: Probably mediates the hydrolysis of some nucleoside
CC diphosphate derivatives. In vitro, it can use both NADH and ADP-ribose
CC as substrates; however the relevance of such substrates in vivo is
CC unclear. {ECO:0000269|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 -!- 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:0000305|PubMed:15878881};
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:0000305|PubMed:15878881};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P32664};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P32664};
CC Note=Divalent metal cations. Mg(2+) or Mn(2+).
CC {ECO:0000250|UniProtKB:P32664};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23.0 uM for ADP-ribose {ECO:0000269|PubMed:15878881};
CC KM=13.7 uM for NADH {ECO:0000269|PubMed:15878881};
CC Vmax=0.18 umol/min/mg enzyme with ADP-ribose as substrate
CC {ECO:0000269|PubMed:15878881};
CC Vmax=0.32 umol/min/mg enzyme with NADPH as substrate
CC {ECO:0000269|PubMed:15878881};
CC -!- TISSUE SPECIFICITY: Expressed in stems and leaves. Weakly or not
CC expressed in roots. {ECO:0000269|PubMed:15878881}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AC006951; AAD25833.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05837.1; -; Genomic_DNA.
DR EMBL; CB185816; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; G84457; G84457.
DR RefSeq; NP_178526.1; NM_126478.4.
DR AlphaFoldDB; Q9SJC4; -.
DR SMR; Q9SJC4; -.
DR BioGRID; 386; 1.
DR STRING; 3702.AT2G04450.1; -.
DR PaxDb; Q9SJC4; -.
DR PRIDE; Q9SJC4; -.
DR ProteomicsDB; 248624; -.
DR DNASU; 814985; -.
DR EnsemblPlants; AT2G04450.1; AT2G04450.1; AT2G04450.
DR GeneID; 814985; -.
DR Gramene; AT2G04450.1; AT2G04450.1; AT2G04450.
DR KEGG; ath:AT2G04450; -.
DR Araport; AT2G04450; -.
DR TAIR; locus:2058334; AT2G04450.
DR eggNOG; KOG0648; Eukaryota.
DR HOGENOM; CLU_054299_1_0_1; -.
DR InParanoid; Q9SJC4; -.
DR OMA; FRFMANI; -.
DR OrthoDB; 835461at2759; -.
DR PhylomeDB; Q9SJC4; -.
DR BioCyc; ARA:AT2G04450-MON; -.
DR BioCyc; MetaCyc:AT2G04450-MON; -.
DR SABIO-RK; Q9SJC4; -.
DR PRO; PR:Q9SJC4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJC4; baseline and differential.
DR Genevisible; Q9SJC4; 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; IDA:TAIR.
DR GO; GO:0080151; P:positive regulation of salicylic acid mediated signaling pathway; IEP:TAIR.
DR GO; GO:0051707; P:response to other organism; IEP:TAIR.
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 Hydrolase; Magnesium; Manganese; Metal-binding; NAD; Reference proteome.
FT CHAIN 1..283
FT /note="Nudix hydrolase 6"
FT /id="PRO_0000057126"
FT DOMAIN 101..233
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 139..160
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT BINDING 154
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32664"
FT BINDING 158
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32664"
FT BINDING 204
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32664"
SQ SEQUENCE 283 AA; 31913 MW; B8140657498E57B4 CRC64;
MDNEDQESLL LQGVPDNYGG VKVNLTEPMT IEDFVPKLRA SLVYWSNQGT KGIWLKLADG
LDNLIAPAKA EGFVCHHAER EYTMLTSWIA DVPSTLPANA SHRIGVGAFV LNKKTKEVLV
VQEIDGHFKG TGVWKLPTGV VKEGENIWEG ALREVEEETG IKTKFVEVLA FRESHQAFLE
IKTDIFFLCE LEPTTFEIKK QDSEILAAKW MPIEEYVNQP WNQKKELFRF MANICLKRLQ
EMEYMGFSKV LTTTSSGKES YLYCNTDHAN LLNATRGLAS TSG
