QPT1_NICGL
ID QPT1_NICGL Reviewed; 350 AA.
AC B2RFT0;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] 1 {ECO:0000303|PubMed:22525250};
DE Short=NgQPT1 {ECO:0000303|PubMed:22525250};
DE EC=2.4.2.19 {ECO:0000305|PubMed:22525250};
GN Name=QPT1 {ECO:0000303|PubMed:22525250};
OS Nicotiana glauca (Glaucous tobacco) (Tree 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=4090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC TISSUE=Leaf;
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 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:22525250}.
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:22525250};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12735;
CC Evidence={ECO:0000305|PubMed:22525250};
CC -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC {ECO:0000305|PubMed:22525250}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from quinolinate: step 1/1.
CC {ECO:0000305|PubMed:22525250}.
CC -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
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DR EMBL; AM922108; CAP57999.1; -; Genomic_DNA.
DR UniPathway; UPA00107; -.
DR UniPathway; UPA00253; UER00331.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
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 Transferase.
FT CHAIN 1..350
FT /note="Quinolinate phosphoribosyltransferase
FT [decarboxylating] 1"
FT /id="PRO_0000455795"
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"
SQ SEQUENCE 350 AA; 37719 MW; 2E4FB2C51CF3E589 CRC64;
MFKVFPFTAI GHPHAITAPR LVVKMSAIAT KNAVESLVVK PPAHPTYDLK GVIQLALSED
AGDLGDVTCK ATIPVVMESE AHFLAKEDGI VAGIALAEMI FAEVDPSLKM EWSISDGDKV
HKGLKFGKVQ GKAHSIVIAE RVVLNFMQRM SGIATLTKAM ADAAHPATIL ETRKTAPGLR
LVDKWAVLIG GGKNHRMGLF DMVMIKDNHI SAAGGVSKAL NSVDQYLEQN KLQMGVEVET
RTIAEVLEVL DYASRTKTSL TRIMLDNMVV PLSDGDIEVS MLNEAVDLIN GRFETEASGN
VTLETVHKIG QTGVTYISSG ALTHSVKALD ISLKIDTELA LEVGRRTKRA
