IFRH_NICSY
ID IFRH_NICSY Reviewed; 310 AA.
AC Q76LW3;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Isoflavone reductase homolog A622 {ECO:0000303|PubMed:12369619};
DE Short=NsA622 {ECO:0000303|PubMed:12369619};
DE EC=1.3.1.- {ECO:0000305};
GN Name=A622 {ECO:0000303|PubMed:12369619};
GN Synonyms=LOC104247368 {ECO:0000312|RefSeq:XP_009801661.1};
OS Nicotiana sylvestris (Wood tobacco) (South American 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=4096;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, INDUCTION BY JASMONIC ACID, AND SUBCELLULAR LOCATION.
RC TISSUE=Flower;
RX PubMed=12369619; DOI=10.1023/A:1019867732278;
RA Shoji T., Winz R., Iwase T., Nakajima K., Yamada Y., Hashimoto T.;
RT "Expression patterns of two tobacco isoflavone reductase-like genes and
RT their possible roles in secondary metabolism in tobacco.";
RL Plant Mol. Biol. 50:427-440(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA Peitsch M.C., Ivanov N.V.;
RT "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT tomentosiformis.";
RL Genome Biol. 14:R60.1-R60.17(2013).
CC -!- FUNCTION: NADPH-binding protein (PubMed:12369619). 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 (By similarity). Reductase involved in a late step of tobacco alkaloid
CC biosynthesis (By similarity). Triggers either the formation of a
CC nicotinic acid-derived precursor or the final condensation reaction of
CC tobacco alkaloids (By similarity). {ECO:0000250|UniProtKB:B7UEU8,
CC ECO:0000269|PubMed:12369619}.
CC -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC {ECO:0000250|UniProtKB:B7UEU8}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P52580}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12369619}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and stems.
CC {ECO:0000269|PubMed:12369619}.
CC -!- DEVELOPMENTAL STAGE: In roots, mainly localized in apical zones,
CC including root tips, in both endodermis and cortex tissues
CC (PubMed:12369619). In the differentiated region where root hairs are
CC present, localized in cortex, endodermis and xylem (PubMed:12369619).
CC {ECO:0000269|PubMed:12369619}.
CC -!- INDUCTION: Stimulated in roots by jasmonic acid (MeJa) in a dose-
CC dependent manner. {ECO:0000269|PubMed:12369619}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; AB071165; BAB83609.1; -; Genomic_DNA.
DR RefSeq; XP_009801661.1; XM_009803359.1.
DR SMR; Q76LW3; -.
DR STRING; 4096.XP_009801661.1; -.
DR GeneID; 104247368; -.
DR KEGG; nsy:104247368; -.
DR eggNOG; ENOG502QPMY; Eukaryota.
DR UniPathway; UPA00107; -.
DR Proteomes; UP000189701; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0009753; P:response to jasmonic acid; 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; Reference proteome.
FT CHAIN 1..310
FT /note="Isoflavone reductase homolog A622"
FT /id="PRO_0000455799"
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; 34654 MW; 03A7F3BB6D451885 CRC64;
MVVSEKSKIL IIGGTGYIGK YLVETSAKSG HPTFALIRES TLKNPEKSKL IDTFKSYGVT
LLFGDISNQE SLLKAIKQVD VVISTVGGQQ FTDQVNIIKA IKEAGNIKRF LPSEFGFDVD
HARAIEPAAS LFALKVRIRR MIEAEGIPYT YVICNWFADF FLPNLGQLEA KTPPRDKVVI
FGDGNPKAIY VKEEDIATYT IEAVDDPRTL NKTLHMRPPA NILSFNEIVS LWEDKIGKTL
EKLYLSEEDI LQIVQEGPLP LRTNLAICHS VFVNGDSANF EVQPPTGVEA TELYPKVKYT
TVDEFYNKFV
