QPT2A_TOBAC
ID QPT2A_TOBAC Reviewed; 351 AA.
AC A0A1S4DFD3; I0J224; Q0WX54; Q9SMB7;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] 2a, mitochondrial {ECO:0000303|PubMed:22525250};
DE Short=NtQPT2a {ECO:0000303|PubMed:22525250};
DE Short=QPRtase 2a {ECO:0000303|PubMed:11198422};
DE EC=2.4.2.19 {ECO:0000305|PubMed:22525250, ECO:0000305|PubMed:23953973, ECO:0000305|PubMed:25582664};
DE Flags: Precursor;
GN Name=QPT2a {ECO:0000303|PubMed:22525250};
GN ORFNames=LOC107829122 {ECO:0000312|RefSeq:XP_016512046.1};
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 [MRNA].
RC STRAIN=cv. NC95, and cv. SC58; TISSUE=Root;
RX PubMed=11198422; DOI=10.1023/a:1026590521318;
RA Sinclair S.J., Murphy K.J., Birch C.D., Hamill J.D.;
RT "Molecular characterization of quinolinate phosphoribosyltransferase
RT (QPRtase) in Nicotiana.";
RL Plant Mol. Biol. 44:603-617(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP INDUCTION BY WOUNDING AND JASMONATE, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND GENE FAMILY.
RC STRAIN=cv. Xanthi; 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 [3]
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 [4]
RP CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND REVIEW ON ALKALOID
RP 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 [5]
RP 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 [6]
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 ECO:0000305|PubMed:23953973, 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:22525250, ECO:0000305|PubMed:23953973,
CC ECO:0000305|PubMed:25582664};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12735;
CC Evidence={ECO:0000305|PubMed:22525250, ECO:0000305|PubMed:23953973,
CC ECO:0000305|PubMed:25582664};
CC -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC {ECO:0000305|PubMed:22525250, ECO:0000305|PubMed:23953973,
CC ECO:0000305|PubMed:25582664}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from quinolinate: step 1/1.
CC {ECO:0000305|PubMed:22525250, ECO:0000305|PubMed:23953973,
CC ECO:0000305|PubMed:25582664}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and flowers.
CC {ECO:0000269|PubMed:22525250, ECO:0000269|PubMed:23953973}.
CC -!- DEVELOPMENTAL STAGE: In flowers, expressed in anthers, upper region of
CC style, stigma and pollen from dehisced anthers.
CC {ECO:0000269|PubMed:22525250}.
CC -!- INDUCTION: Triggered by wounding and jasmonic acid (MeJA).
CC {ECO:0000269|PubMed:22525250}.
CC -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
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DR EMBL; AJ243437; CAB59430.1; -; mRNA.
DR EMBL; AJ748263; CAH04307.1; -; Genomic_DNA.
DR EMBL; FR852382; CCA65515.1; -; Genomic_DNA.
DR RefSeq; NP_001313145.1; NM_001326216.1.
DR RefSeq; XP_016512046.1; XM_016656560.1.
DR SMR; A0A1S4DFD3; -.
DR GeneID; 107829122; -.
DR KEGG; nta:107829122; -.
DR OMA; EMINGRF; -.
DR OrthoDB; 1263431at2759; -.
DR BioCyc; MetaCyc:MON-12622; -.
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 GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
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; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..351
FT /note="Quinolinate phosphoribosyltransferase
FT [decarboxylating] 2a, mitochondrial"
FT /id="PRO_0000455790"
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"
FT CONFLICT 5
FT /note="L -> I (in Ref. 2; CAH04307)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="V -> L (in Ref. 2; CAH04307)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="E -> D (in Ref. 2; CAH04307)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="H -> Q (in Ref. 1; CAB59430)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="R -> Q (in Ref. 1; CAB59430)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 38200 MW; 1CCE7F3C28BACB43 CRC64;
MFRALPFTAT VHPYAITAPR LVVKMSAIAT KNTRVESLEV KPPAHPTYDL KGVMQLALSE
DAGNLGDVTC KATIPVDMES DAHFLAKEDG IIAGIALAEM IFAEVDPSLK VEWYVNDGDK
VHKGLKFGKV QGNAYNIVIA ERVVLNFMQR MSGIATLTKE MADAAHPAYI LETRKTAPGL
RLVDKWAVLI GGGKNHRMGL FDMVMIKDNH ISAAGGVGKA LKSVDQYLEQ NKLQIGVEVE
TRTIAEVREV LEYASQTKTS LTRIMLDNMV VPLSNGDIDV SMLKEAVELI NGRFDTEASG
NVTLETVHKI GQTGVTYISS GALTHSVKAL DISLKIDTEL ALEVGRRTKR A
