NADC_ARATH
ID NADC_ARATH Reviewed; 348 AA.
AC Q9ZU32; Q8LC11; Q93ZA4;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Nicotinate-nucleotide pyrophosphorylase [carboxylating], chloroplastic {ECO:0000305};
DE EC=2.4.2.19 {ECO:0000269|PubMed:16698895};
DE AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] {ECO:0000303|PubMed:16698895};
DE Flags: Precursor;
GN Name=QPT {ECO:0000303|PubMed:16698895};
GN OrderedLocusNames=At2g01350 {ECO:0000312|Araport:AT2G01350};
GN ORFNames=F10A8.23 {ECO:0000312|EMBL:AAD14535.2};
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 [LARGE SCALE MRNA].
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16698895; DOI=10.1104/pp.106.081091;
RA Katoh A., Uenohara K., Akita M., Hashimoto T.;
RT "Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate
RT and occur in the plastid.";
RL Plant Physiol. 141:851-857(2006).
RN [7]
RP FUNCTION.
RX PubMed=22268572; DOI=10.1111/j.1365-313x.2012.04920.x;
RA Petriacq P., de Bont L., Hager J., Didierlaurent L., Mauve C., Guerard F.,
RA Noctor G., Pelletier S., Renou J.P., Tcherkez G., Gakiere B.;
RT "Inducible NAD overproduction in Arabidopsis alters metabolic pools and
RT gene expression correlated with increased salicylate content and resistance
RT to Pst-AvrRpm1.";
RL Plant J. 70:650-665(2012).
CC -!- FUNCTION: Involved in the biosynthesis of NAD(+) (PubMed:16698895).
CC Catalyzes the conversion of quinolate to nicotinate to nicotinate beta-
CC D-ribonucleotide (PubMed:16698895). {ECO:0000269|PubMed:16698895}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CO2 + diphosphate + nicotinate beta-D-ribonucleotide = 5-
CC phospho-alpha-D-ribose 1-diphosphate + 2 H(+) + quinolinate;
CC Xref=Rhea:RHEA:12733, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:29959, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502,
CC ChEBI:CHEBI:58017; EC=2.4.2.19;
CC Evidence={ECO:0000269|PubMed:16698895};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12735;
CC Evidence={ECO:0000269|PubMed:16698895};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from quinolinate: step 1/1. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16698895}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9ZU32-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC {ECO:0000269|PubMed:16698895}.
CC -!- MISCELLANEOUS: Accumulation of NAD by over-expression of the bacterial
CC nadC gene in Arabidopsis stimulates plant resistance probably via
CC salicylic acid (SA)-dependent signaling. {ECO:0000305|PubMed:22268572}.
CC -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM63914.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC006200; AAD14535.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC05440.1; -; Genomic_DNA.
DR EMBL; AK117875; BAC42515.1; -; mRNA.
DR EMBL; AY057685; AAL15316.1; -; mRNA.
DR EMBL; AY116955; AAM51589.1; -; mRNA.
DR EMBL; AY086867; AAM63914.1; ALT_INIT; mRNA.
DR PIR; F84423; F84423.
DR RefSeq; NP_565259.1; NM_126196.3. [Q9ZU32-1]
DR AlphaFoldDB; Q9ZU32; -.
DR SMR; Q9ZU32; -.
DR BioGRID; 67; 3.
DR STRING; 3702.AT2G01350.1; -.
DR PaxDb; Q9ZU32; -.
DR PRIDE; Q9ZU32; -.
DR ProteomicsDB; 251197; -. [Q9ZU32-1]
DR EnsemblPlants; AT2G01350.1; AT2G01350.1; AT2G01350. [Q9ZU32-1]
DR GeneID; 814663; -.
DR Gramene; AT2G01350.1; AT2G01350.1; AT2G01350. [Q9ZU32-1]
DR KEGG; ath:AT2G01350; -.
DR Araport; AT2G01350; -.
DR TAIR; locus:2038791; AT2G01350.
DR eggNOG; KOG3008; Eukaryota.
DR InParanoid; Q9ZU32; -.
DR PhylomeDB; Q9ZU32; -.
DR BioCyc; ARA:AT2G01350-MON; -.
DR UniPathway; UPA00253; UER00331.
DR PRO; PR:Q9ZU32; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZU32; baseline and differential.
DR Genevisible; Q9ZU32; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IMP:TAIR.
DR GO; GO:0009435; P:NAD biosynthetic process; IMP:TAIR.
DR GO; GO:0034213; P:quinolinate catabolic process; IBA:GO_Central.
DR CDD; cd01572; QPRTase; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.90.1170.20; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR004393; NadC.
DR InterPro; IPR027277; NadC/ModD.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR InterPro; IPR037128; Quinolinate_PRibosylTase_N_sf.
DR InterPro; IPR002638; Quinolinate_PRibosylTrfase_C.
DR InterPro; IPR022412; Quinolinate_PRibosylTrfase_N.
DR PANTHER; PTHR32179; PTHR32179; 1.
DR Pfam; PF01729; QRPTase_C; 1.
DR Pfam; PF02749; QRPTase_N; 1.
DR SUPFAM; SSF51690; SSF51690; 1.
DR TIGRFAMs; TIGR00078; nadC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Glycosyltransferase; Plastid;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..41
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 42..348
FT /note="Nicotinate-nucleotide pyrophosphorylase
FT [carboxylating], chloroplastic"
FT /id="PRO_0000423480"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 170..172
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 296..298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 317..319
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT CONFLICT 56
FT /note="A -> D (in Ref. 5; AAM63914)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 37955 MW; 7D41CE0CC39ADB72 CRC64;
MISVSRFLSP QFYAIPRSFV KMSASATQTA GEVSMGIKPP SHPTYDLKAV IKLALAEDAG
HTGDVTCMAT IPFDMEVEAY FLAKEDGIVA GVALADMIFE HVDPSLKVEW MRKDGDYVHK
GLKFGKVSGN AHKIVVAERV LLNFMQRMSG IATLTKLMAD AASPACILET RKTAPGLRLV
DKWAVLIGGG RNHRMGLFDM VMIKDNHISA AGGIVNAVKS VDEYLKQKNL EMDVEVETRT
LEEVKEVLEY ASGSETRLTR IMLDNMVVPL ENGDVDVTML KDAVELINGR FETEASGNVT
LETVHKIGQS GVTFISSGAL THSVKALDIS LKIDTELALE VGRRTKRA
