ID   QS1_TOBAC               Reviewed;         721 AA.
AC   A0A1S4BZI5;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Quinolinate synthase, chloroplastic {ECO:0000250|UniProtKB:Q9FGS4};
DE            EC=2.5.1.72 {ECO:0000250|UniProtKB:Q9FGS4};
DE   Flags: Precursor;
GN   Name=QS {ECO:0000250|UniProtKB:Q9FGS4};
GN   ORFNames=LOC107813484 {ECO:0000312|RefSeq:XP_016494243.1};
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   REVIEW ON ALKALOID 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   [3]
RP   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, AND PATHWAY.
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) (PubMed:23953973, PubMed:31276744). Catalyzes
CC       the condensation of iminoaspartate with dihydroxyacetone phosphate to
CC       form quinolinate (By similarity). {ECO:0000250|UniProtKB:Q9FGS4,
CC       ECO:0000269|PubMed:31276744, ECO:0000303|PubMed:23953973}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O +
CC         phosphate + quinolinate; Xref=Rhea:RHEA:25888, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29959, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57642, ChEBI:CHEBI:77875; EC=2.5.1.72;
CC         Evidence={ECO:0000250|UniProtKB:Q9FGS4};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q9FGS4};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000250|UniProtKB:Q9FGS4};
CC   -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC       {ECO:0000269|PubMed:31276744}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       iminoaspartate: step 1/1. {ECO:0000250|UniProtKB:Q9FGS4}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9FGS4}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000250|UniProtKB:Q9FGS4}.
CC   -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 1
CC       subfamily. {ECO:0000305}.
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DR   RefSeq; XP_016494243.1; XM_016638757.1.
DR   SMR; A0A1S4BZI5; -.
DR   GeneID; 107813484; -.
DR   KEGG; nta:107813484; -.
DR   OMA; VSMQKKT; -.
DR   OrthoDB; 1016662at2759; -.
DR   UniPathway; UPA00107; -.
DR   UniPathway; UPA00253; UER00327.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008987; F:quinolinate synthetase A activity; IBA:GO_Central.
DR   GO; GO:0034628; P:'de novo' NAD biosynthetic process from aspartate; IBA:GO_Central.
DR   Gene3D; 3.40.50.10800; -; 3.
DR   InterPro; IPR003808; Fe-S_metab-assoc_dom.
DR   InterPro; IPR003473; NadA.
DR   InterPro; IPR036094; NadA_sf.
DR   PANTHER; PTHR30573; PTHR30573; 1.
DR   Pfam; PF02445; NadA; 1.
DR   Pfam; PF02657; SufE; 1.
DR   SUPFAM; SSF142754; SSF142754; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Alkaloid metabolism; Chloroplast; Iron; Iron-sulfur; Metal-binding;
KW   Plastid; Pyridine nucleotide biosynthesis; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..67
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           68..721
FT                   /note="Quinolinate synthase, chloroplastic"
FT                   /id="PRO_0000455788"
FT   ACT_SITE        133
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FGS4"
FT   BINDING         283
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000250|UniProtKB:O57767"
FT   BINDING         309
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000250|UniProtKB:O57767"
FT   BINDING         363
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:O57767"
FT   BINDING         392..394
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000250|UniProtKB:O57767"
FT   BINDING         414
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000250|UniProtKB:O57767"
FT   BINDING         487
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:O57767"
FT   BINDING         513..515
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000250|UniProtKB:O57767"
FT   BINDING         538
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000250|UniProtKB:O57767"
FT   BINDING         643
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:O57767"
SQ   SEQUENCE   721 AA;  78324 MW;  EC7FC2B1EA339382 CRC64;
     MDAANLVMKS SMFSKSPCPV FGSKLIPRAP PSVFTLPSTF RPLVKCIQAS FPQNPDSKIP
     SNNSTFTCSA VTSFPSQQSQ PHATSDAKLQ LLISEFQSLV EPMDRVKRLL HYSTLIPSMD
     ASLKTPENRV LGCTTQVWLH VSFDEAENRM KFVADSDSDI TKGFCACLVS LLDGATPDEV
     LALKTEDLNA LNVAGLNGKG SASRANTWHN VLVSMQKRTR ALVAEREGRP RNELFPSLVI
     TADGIQPQGS YAEAQARFLF PDESRVQELA SLLKEKKIGV VAHFYMDPEV QGVLTAAQKL
     WPHIHISDSL VMADKAVSMA KAGCEYISVL GVDFMSENVR AILDLAGFPE VGVYRMSDER
     IGCSLADAAA SPAYLDYLKT ASTSSPSLHV VYINTSLETK AYSHELVPTI TCTSSNVVQT
     ILQAFAEVPD LEVLYGPDTY MGSNIAELFT QMSTMTDEEI SEIHPLHNRS SIKSLLPRLH
     YFQDGTCIVH HLFGHEVVEN INEMYGDAFL TAHFEVPGEM FSLAMEAKKR GMGVVGSTSN
     ILDFIKERVE EALNRNVDEH LQFVLGTESG MITAIVAAVG KLLGSADTSS GGAKVSVEIV
     FPVSSESVTR TSTGSSLDQN KVNIIPGVAS GEGCSLHGGC ASCPYMKMNS LSSLLRVCQS
     LPHGKAELSA YEAGRFSLQT PNGKQIADVG CEPVLHMRHF QATKRLPEQL INQILQRSSS
     A