ID   IFRH_NICGL              Reviewed;         310 AA.
AC   B7UEU8;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Isoflavone reductase homolog A622 {ECO:0000303|PubMed:19011764};
DE            Short=NgA622 {ECO:0000303|PubMed:19011764};
DE            EC=1.3.1.- {ECO:0000305};
GN   Name=A622 {ECO:0000303|PubMed:19011764};
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, DISRUPTION PHENOTYPE, PATHWAY,
RP   AND INDUCTION BY JASMONIC ACID AND WOUNDING.
RC   TISSUE=Leaf;
RX   PubMed=19011764; DOI=10.1007/s11103-008-9425-2;
RA   Deboer K.D., Lye J.C., Aitken C.D., Su A.K., Hamill J.D.;
RT   "The A622 gene in Nicotiana glauca (tree tobacco): evidence for a
RT   functional role in pyridine alkaloid synthesis.";
RL   Plant Mol. Biol. 69:299-312(2009).
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: NADPH-binding protein (PubMed:19011764). Involved in the
CC       biosynthesis of pyridine alkaloid natural products, leading mainly to
CC       the production of anabasine, anatabine, nicotine and nornicotine,
CC       effective deterrents against herbivores with antiparasitic and
CC       pesticide properties (neurotoxins); nornicotine serves as the precursor
CC       in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN)
CC       (PubMed:19011764, PubMed:31276744). Reductase involved in a late step
CC       of tobacco alkaloid biosynthesis (PubMed:19011764). Triggers either the
CC       formation of a nicotinic acid-derived precursor or the final
CC       condensation reaction of tobacco alkaloids (PubMed:19011764).
CC       {ECO:0000269|PubMed:19011764, ECO:0000269|PubMed:31276744}.
CC   -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC       {ECO:0000269|PubMed:19011764}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P52580}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52580}.
CC   -!- INDUCTION: Stimulated by jasmonic acid (MeJa) (PubMed:19011764).
CC       Induced by wounding (PubMed:32688942). {ECO:0000269|PubMed:19011764,
CC       ECO:0000269|PubMed:32688942}.
CC   -!- DISRUPTION PHENOTYPE: Reduces capacity to produce anabasine and
CC       nicotine associated with barely detectable levels of pyridine alkaloids
CC       in leaf tissues. {ECO:0000269|PubMed:19011764}.
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC       reductase subfamily. {ECO:0000305}.
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DR   EMBL; FM173206; CAQ64599.1; -; Genomic_DNA.
DR   SMR; B7UEU8; -.
DR   UniPathway; UPA00107; -.
DR   GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IMP:UniProtKB.
DR   GO; GO:0009821; P:alkaloid biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0042179; P:nicotine biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR   GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR   CDD; cd05259; PCBER_SDR_a; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR008030; NmrA-like.
DR   InterPro; IPR045312; PCBER-like.
DR   Pfam; PF05368; NmrA; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Alkaloid metabolism; Cytoplasm; NADP; Oxidoreductase.
FT   CHAIN           1..310
FT                   /note="Isoflavone reductase homolog A622"
FT                   /id="PRO_0000455800"
FT   ACT_SITE        135
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         13..19
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         38
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         47
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         139
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
SQ   SEQUENCE   310 AA;  34558 MW;  13965256666C0DE8 CRC64;
     MVASEKSKIL IIGGTGYIGK YLVETSAKSG HPTFVLIRES TLKNPQKSKL IDTFKSYGVT
     LLFGDISNQE SLLKAIKQVD VVISTVGGQQ FADQVNIINA IKEAGNIKRF LPSEFGFDVD
     HAHAIEPAAS LFALKVKIRR MIEAEGIPYT YVICNWFADF FLPNLGHLDA KTPPRDKVVI
     FGDGNPKAIY VKEEDIATYT IEAVDDPRTL NKTLHMRPPA NILSFNEVVS LWEEKIGKTL
     EKIYLSEEDI LEIVKEGPLP LRTNLAICHS VFVNGDSANF EVQPPTGVEA TELYPKVKYT
     TVDEFYNKFV