IFRH_TOBAC
ID IFRH_TOBAC Reviewed; 310 AA.
AC P52579; A0A076JBH7; A0A7F0KMK4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Isoflavone reductase homolog A622 {ECO:0000305};
DE Short=NtA622 {ECO:0000303|PubMed:19002761};
DE EC=1.3.1.- {ECO:0000305};
GN Name=A622 {ECO:0000303|PubMed:12369619};
GN Synonyms=IRL1 {ECO:0000312|EMBL:AII71784.1};
GN ORFNames=LOC107784748 {ECO:0000312|RefSeq:XP_016461410.1};
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], TISSUE SPECIFICITY, REPRESSION BY AUXIN, AND
RP INDUCTION BY YOUNG AERIAL TISSUES REMOVAL.
RC STRAIN=cv. Burley 21; TISSUE=Root;
RX PubMed=8038607; DOI=10.2307/3869875;
RA Hibi N., Higashiguchi S., Hashimoto T., Yamada Y.;
RT "Gene expression in tobacco low-nicotine mutants.";
RL Plant Cell 6:723-735(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Chen W., Lin Y.-C., Gao W.-C., Li C.-J., Wang S.-G., Lu J., Chai Y.-R.;
RT "Molecular cloning of isoflavone reductase-like gene family from tobacco.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY METHYL JASMONATE.
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY METHYL JASMONATE, AND PATHWAY.
RC STRAIN=cv. Petit Havana SR1;
RX PubMed=19002761; DOI=10.1007/s11103-008-9424-3;
RA Kajikawa M., Hirai N., Hashimoto T.;
RT "A PIP-family protein is required for biosynthesis of tobacco alkaloids.";
RL Plant Mol. Biol. 69:287-298(2009).
RN [6]
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 [7]
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 [8]
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) (PubMed:19002761, PubMed:31276744). Probable
CC NADPH-dependent oxidoreductase that binds NADPH in vitro. Does not seem
CC to be involved in the NADPH-dependent reduction of phenylcoumaran
CC benzylic ethers (PubMed:12369619). Reductase that may be involved in a
CC late step of tobacco alkaloid biosynthesis. Maybe involved in either
CC the formation of a nicotinic acid-derived precursor or the final
CC condensation reaction of tobacco alkaloids (PubMed:19002761).
CC {ECO:0000269|PubMed:12369619, ECO:0000269|PubMed:19002761,
CC ECO:0000269|PubMed:31276744}.
CC -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC {ECO:0000269|PubMed:19002761}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P52580}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52580}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:12369619,
CC ECO:0000269|PubMed:19002761, ECO:0000269|PubMed:8038607}.
CC -!- INDUCTION: Induced by methyl jasmonate in roots (PubMed:12369619,
CC PubMed:19002761). Down-regulated by auxin (PubMed:8038607). Accumulates
CC upon the removal of flower heads and young leaves (PubMed:8038607).
CC {ECO:0000269|PubMed:12369619, ECO:0000269|PubMed:19002761,
CC ECO:0000269|PubMed:8038607}.
CC -!- MISCELLANEOUS: Root cells silencing A622 exhibit inhibition of cell
CC growth, severely decreased formation of several alkaloids, and
CC accumulation of nicotinic acid beta-N-glucoside and N-methylpyrrolinium
CC cation. {ECO:0000269|PubMed:19002761}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D28505; BAA05866.1; -; mRNA.
DR EMBL; KJ776595; AII71783.1; -; Genomic_DNA.
DR EMBL; KJ776596; AII71784.1; -; mRNA.
DR PIR; T02202; T02202.
DR RefSeq; NP_001312315.1; NM_001325386.1.
DR RefSeq; XP_016461410.1; XM_016605924.1.
DR AlphaFoldDB; P52579; -.
DR SMR; P52579; -.
DR STRING; 4097.P52579; -.
DR GeneID; 107784748; -.
DR KEGG; nta:107784748; -.
DR OMA; IHPPKNI; -.
DR OrthoDB; 936727at2759; -.
DR PhylomeDB; P52579; -.
DR UniPathway; UPA00107; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009733; P:response to auxin; IDA:UniProtKB.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP: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_0000204551"
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
