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QPT1B_TOBAC
ID   QPT1B_TOBAC             Reviewed;         350 AA.
AC   A0A1S4DF18; A0A1S4DFD0;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] 1b {ECO:0000305};
DE            Short=NtQPT1b {ECO:0000305};
DE            EC=2.4.2.19 {ECO:0000305|PubMed:23953973, ECO:0000305|PubMed:25582664};
GN   Name=QPT1b {ECO:0000305};
GN   ORFNames=LOC107829123 {ECO:0000312|RefSeq:XP_016512047.1};
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 [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   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND REVIEW ON ALKALOID BIOSYNTHESIS
RP   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   [3]
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   [4]
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A0A1S4DF18-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A0A1S4DF18-2; Sequence=VSP_061528;
CC   -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
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DR   RefSeq; XP_016512047.1; XM_016656561.1.
DR   RefSeq; XP_016512048.1; XM_016656562.1.
DR   SMR; A0A1S4DF18; -.
DR   GeneID; 107829123; -.
DR   KEGG; nta:107829123; -.
DR   OMA; CPRKAIP; -.
DR   OrthoDB; 1263431at2759; -.
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   PIRSF; PIRSF006250; NadC_ModD; 1.
DR   SUPFAM; SSF51690; SSF51690; 1.
DR   TIGRFAMs; TIGR00078; nadC; 1.
PE   1: Evidence at protein level;
KW   Alkaloid metabolism; Alternative splicing; Glycosyltransferase;
KW   Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..350
FT                   /note="Quinolinate phosphoribosyltransferase
FT                   [decarboxylating] 1b"
FT                   /id="PRO_0000455794"
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   VAR_SEQ         1..24
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_061528"
SQ   SEQUENCE   350 AA;  37819 MW;  98EB6816B54AB3F9 CRC64;
     MFKVLPFTAI VHPNAITAPR LVVKMSAIAT KNAVESFVVK PPAHPTYDLK GVIQLALSED
     AGDIGDVTCK ATIPIDMESE AHFLAKEDGI VAGIALAEMI FAEVDPSLKM EWSINDGDKV
     HKGLKFGKVQ GKAHSIVIAE RVVLNFMQRM SGIATLTKAM ADAAHPATIL ETRKTAPGLR
     LVDKWAVLIG GGKNHRMGLF DMVMIKDNHI SAAGGVSKAL NSVDQYLEQN KLQMGVEVET
     RTIAEVHEVL EYASQTKTSL TRIMLDNMVV PLSNGDIEVS MLEEAVDLIN GRFETEASGN
     VTLETVHKIG QTGVTYISSG ALTHSVKALD ISLKIDTELA LEVGRRTKRA
 
 
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