QPT2_NICGL
ID QPT2_NICGL Reviewed; 351 AA.
AC B2RFS9;
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] 2, mitochondrial {ECO:0000303|PubMed:22525250};
DE Short=NgQPT2 {ECO:0000303|PubMed:22525250};
DE EC=2.4.2.19 {ECO:0000305|PubMed:22525250};
DE Flags: Precursor;
GN Name=QPT2 {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 STRAIN=cv. Melbourne 1; 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 INDUCTION BY WOUNDING.
RX PubMed=32688942; DOI=10.1071/fp03242;
RA Sinclair S.J., Johnson R., Hamill J.D.;
RT "Analysis of wound-induced gene expression in Nicotiana species with
RT contrasting alkaloid profiles.";
RL Funct. Plant Biol. 31:721-729(2004).
RN [3]
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC -!- INDUCTION: Induced by wounding. {ECO:0000269|PubMed:32688942}.
CC -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
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DR EMBL; AM922107; CAP57998.1; -; 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 GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
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; Mitochondrion;
KW Pyridine nucleotide biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..351
FT /note="Quinolinate phosphoribosyltransferase
FT [decarboxylating] 2, mitochondrial"
FT /id="PRO_0000455792"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 173..175
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 299..301
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
FT BINDING 320..322
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ7"
SQ SEQUENCE 351 AA; 38330 MW; 072610E910FB1105 CRC64;
MFRAIPFTAT VHPYAITAPR LVVKMSAIAT KNTRVESLEV KPPAHPTYDL KEVMQLALSE
DAGNLGDVTC KATIPLDMES DAHFLAKEDG IVAGIALAEM IFAEVDPSLK VEWYVNDGDK
VHKGLKFGKV QGNAYNIVIA ERVVLNFMQR MSGIATLTKE MADAAHPAYI LETRKTAPGL
RLVDKWAVLI GGGKNHRMGL FDMVMIKDNH ISAAGGVGKA LKSVDQYLEQ NKLQIGVEVE
TRTIEEVREV LEYASQTKTS LTRIMLDNMV VPLSNGDIDV SMLKEAVELI NGRFDTEASG
NVTLETVHKI GQTGVTYISS GALTHSVKAL DISLKIDTEL ALEVGRRTKR A
