QPT1A_TOBAC
ID QPT1A_TOBAC Reviewed; 350 AA.
AC A0A1S4D475; Q0WX55;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] 1a {ECO:0000303|PubMed:23953973, ECO:0000303|PubMed:25582664};
DE Short=NtQPT1a {ECO:0000305};
DE EC=2.4.2.19 {ECO:0000305|PubMed:23953973, ECO:0000305|PubMed:25582664};
GN Name=QPT1a {ECO:0000303|PubMed:23953973, ECO:0000303|PubMed:25582664};
GN ORFNames=LOC107825849 {ECO:0000312|RefSeq:XP_016508245.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GENE FAMILY.
RC STRAIN=cv. Xanthi;
RX PubMed=22525250; DOI=10.1016/j.plantsci.2012.02.008;
RA Ryan S.M., Cane K.A., DeBoer K.D., Sinclair S.J., Brimblecombe R.,
RA Hamill J.D.;
RT "Structure and expression of the quinolinate phosphoribosyltransferase
RT (QPT) gene family in Nicotiana.";
RL Plant Sci. 188:102-110(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90;
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND REVIEW ON
RP ALKALOID BIOSYNTHESIS IN NICOTIANA TABACUM.
RX PubMed=23953973; DOI=10.1016/j.phytochem.2013.06.002;
RA Dewey R.E., Xie J.;
RT "Molecular genetics of alkaloid biosynthesis in Nicotiana tabacum.";
RL Phytochemistry 94:10-27(2013).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND REVIEW ON NICOTINE BIOSYNTHESIS.
RX PubMed=25582664; DOI=10.1007/s00438-015-0989-7;
RA Wang X., Bennetzen J.L.;
RT "Current status and prospects for the study of Nicotiana genomics,
RT genetics, and nicotine biosynthesis genes.";
RL Mol. Genet. Genomics 290:11-21(2015).
RN [5]
RP FUNCTION.
RC STRAIN=cv. Burley Stella, cv. Burley TN90, cv. Virginia ITB 683, and
RC cv. Virginia K326;
RX PubMed=31276744; DOI=10.1016/j.fct.2019.110660;
RA Schorderet Weber S., Kaminski K.P., Perret J.-L., Leroy P., Mazurov A.,
RA Peitsch M.C., Ivanov N.V., Hoeng J.;
RT "Antiparasitic properties of leaf extracts derived from selected Nicotiana
RT species and Nicotiana tabacum varieties.";
RL Food Chem. Toxicol. 132:110660-110660(2019).
CC -!- FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural
CC products, leading mainly to the production of anabasine, anatabine,
CC nicotine and nornicotine, effective deterrents against herbivores with
CC antiparasitic and pesticide properties (neurotoxins); nornicotine
CC serves as the precursor in the synthesis of the carcinogen compound N'-
CC nitrosonornicotine (NNN) (Probable) (PubMed:31276744). Involved in the
CC catabolism of quinolinic acid (QA) (Probable).
CC {ECO:0000269|PubMed:31276744, ECO:0000305|PubMed:23953973,
CC ECO:0000305|PubMed:25582664}.
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:0000305|PubMed:23953973, ECO:0000305|PubMed:25582664};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12735;
CC Evidence={ECO:0000305|PubMed:23953973, ECO:0000305|PubMed:25582664};
CC -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC {ECO:0000305|PubMed:23953973, ECO:0000305|PubMed:25582664}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from quinolinate: step 1/1.
CC {ECO:0000305|PubMed:23953973, ECO:0000305|PubMed:25582664}.
CC -!- TISSUE SPECIFICITY: Ubiquitously present at low levels with higher
CC levels at the apical meristem. {ECO:0000269|PubMed:23953973}.
CC -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
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; AJ748262; CAH04306.1; -; mRNA.
DR RefSeq; XP_016508245.1; XM_016652759.1.
DR SMR; A0A1S4D475; -.
DR GeneID; 107825849; -.
DR KEGG; nta:107825849; -.
DR OMA; DMIMLKD; -.
DR OrthoDB; 1263431at2759; -.
DR BRENDA; 2.4.2.19; 3645.
DR UniPathway; UPA00107; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IBA:GO_Central.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
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 Alkaloid metabolism; Glycosyltransferase; Pyridine nucleotide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..350
FT /note="Quinolinate phosphoribosyltransferase
FT [decarboxylating] 1a"
FT /id="PRO_0000455793"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 172..174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 298..300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 319..321
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT CONFLICT 225
FT /note="Q -> H (in Ref. 1; CAH04306)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="D -> E (in Ref. 1; CAH04306)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="E -> D (in Ref. 1; CAH04306)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="S -> R (in Ref. 1; CAH04306)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 37832 MW; 7F787C82F7C18DF1 CRC64;
MFKVFPFTAI VHPHAITAPR LVVKMSAIAT KNAVESLVVK PPAHPTYDLK GVIQLALSED
AGDLGDVTCK ATIPIDMESE AHFLAKEDGI VAGIALAEMI FAEVDPSLKM EWSINDGDKV
HKGLKFGKVQ GKAHSIVIAE RVVLNFMQRM SGIATLTKAM ADAAHPATIL ETRKTAPGLR
LVDKWAVLIG GGKNHRMGLF DMVMIKDNHI SAAGGVSKAL NSVDQYLEQN KLQMGVEVET
RTIAEVREVL DYASQTKTSL TRIMLDNMVV PLSNGDIDVS MLKEAVDLIN GRFETEASGN
VTLETVHKIG QTGVTYISSG ALTHSVKALD ISLKIDTELA LEVGRRTKRA
