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QPT2B_TOBAC
ID   QPT2B_TOBAC             Reviewed;         351 AA.
AC   A0A1S4CL59; Q9MB29;
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] 2b, mitochondrial {ECO:0000303|PubMed:22525250};
DE            Short=NtQPT2b {ECO:0000303|PubMed:22525250};
DE            Short=QPRtase 2b {ECO:0000305};
DE            EC=2.4.2.19 {ECO:0000305|PubMed:22525250, ECO:0000305|PubMed:23953973, ECO:0000305|PubMed:25582664};
DE   Flags: Precursor;
GN   Name=QPT2b {ECO:0000303|PubMed:22525250};
GN   Synonyms=MC212 {ECO:0000303|PubMed:18001808}, QAPRT {ECO:0000303|Ref.1},
GN   QPRT {ECO:0000303|PubMed:18001808};
GN   ORFNames=LOC107820078 {ECO:0000312|RefSeq:XP_016501781.1};
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. Bright Yellow 2;
RA   Kojima H.;
RT   "Characterization of a cDNA encoding quinolinate phosphoribosyltransferase
RT   from Nicotiana tabacum.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
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   REVIEW.
RC   TISSUE=Protoplast;
RX   PubMed=18001808; DOI=10.1016/j.phytochem.2007.09.010;
RA   Haekkinen S.T., Tilleman S., Swiatek A., De Sutter V., Rischer H.,
RA   Vanhoutte I., Van Onckelen H., Hilson P., Inze D., Oksman-Caldentey K.-M.,
RA   Goossens A.;
RT   "Functional characterisation of genes involved in pyridine alkaloid
RT   biosynthesis in tobacco.";
RL   Phytochemistry 68:2773-2785(2007).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INDUCTION BY WOUNDING AND JASMONATE,
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND GENE FAMILY.
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   [5]
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   [6]
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   [7]
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; AB038494; BAA92153.1; -; mRNA.
DR   RefSeq; NP_001312987.1; NM_001326058.1.
DR   RefSeq; XP_016501781.1; XM_016646295.1.
DR   SMR; A0A1S4CL59; -.
DR   ProMEX; Q9MB29; -.
DR   GeneID; 107820078; -.
DR   KEGG; nta:107820078; -.
DR   OMA; LCGQPWF; -.
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   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] 2b, mitochondrial"
FT                   /id="PRO_0000455791"
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        344
FT                   /note="V -> D (in Ref. 1; BAA92153)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   351 AA;  38330 MW;  8180F624507092BB CRC64;
     MFRAIPFTAT VHPYAITAPR LVVKMSAIAT KNTRVESLEV KPPAHPTYDL KEVMKLALSE
     DAGNLGDVTC KATIPLDMES DAHFLAKEDG IIAGIALAEM IFAEVDPSLK VEWYVNDGDK
     VHKGLKFGKV QGNAYNIVIA ERVVLNFMQR MSGIATLTKE MADAAHPAYI LETRKTAPGL
     RLVDKWAVLI GGGKNHRMGL FDMVMIKDNH ISAAGGVGKA LKSVDQYLEQ NKLQIGVEVE
     TRTIEEVREV LDYASQTKTS LTRIMLDNMV VPLSNGDIDV SMLKEAVELI NGRFDTEASG
     NVTLETVHKI GQTGVTYISS GALTHSVKAL DISLKIDTEL ALEVGRRTKR A
 
 
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