A622L_TOBAC
ID A622L_TOBAC Reviewed; 310 AA.
AC B6VRE6;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Isoflavone reductase homolog A622-like {ECO:0000305};
DE Short=NtA622L {ECO:0000303|PubMed:19002761};
DE EC=1.3.1.- {ECO:0000305};
GN Name=A622L {ECO:0000303|PubMed:19002761};
GN Synonyms=IRL2 {ECO:0000312|EMBL:AII71785.1};
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 [GENOMIC DNA / MRNA], FUNCTION, INDUCTION BY METHYL
RP 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 [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 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).
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). Reductase that may be
CC involved in a late step of tobacco alkaloid biosynthesis
CC (PubMed:19002761). Maybe involved in either the formation of a
CC nicotinic acid-derived precursor or the final condensation reaction of
CC tobacco alkaloids (PubMed:19002761). {ECO:0000269|PubMed:19002761}.
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:19002761}.
CC -!- INDUCTION: Induced by methyl jasmonate in roots.
CC {ECO:0000269|PubMed:19002761}.
CC -!- MISCELLANEOUS: Root cells silencing A622L 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}.
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DR EMBL; AB445396; BAG84265.1; -; mRNA.
DR EMBL; AB445397; BAG84266.1; -; Genomic_DNA.
DR EMBL; KJ776597; AII71785.1; -; Genomic_DNA.
DR EMBL; KJ776598; AII71786.1; -; mRNA.
DR RefSeq; NP_001312742.1; NM_001325813.1.
DR AlphaFoldDB; B6VRE6; -.
DR SMR; B6VRE6; -.
DR STRING; 4097.B6VRE6; -.
DR ProMEX; B6VRE6; -.
DR GeneID; 107807959; -.
DR KEGG; nta:107807959; -.
DR OMA; WATGGAM; -.
DR OrthoDB; 936727at2759; -.
DR PhylomeDB; B6VRE6; -.
DR UniPathway; UPA00107; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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-like"
FT /id="PRO_0000442616"
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; 34652 MW; D2B8CC22168D9218 CRC64;
MVVSEKSKIL IIGGTGYIGK YLVETSAKSG HPTFVLIRES TLVNPEKSKL IDTFKSYGVT
LLFGDISNQE SLLKAIKQVD VVISTVGGQQ FADQVNIIKA IKEAGNIKRF LPSEFGFDVD
HAHAIEPAAS LFALKVKIRR MIEAEGIPYT YVICNWFADF FLPNLGQLEA KTPPRDKVVI
FGDGNPKAIY VKEEDIATYT MKAVDDPRTL NKTLHMRPPA NILSFNEIVS LWEEKIGKTL
EKLYLSEEDI LHIVQEGPMP LRVNLAICHS VFVNGDSANF EIQPSTGVEA TELYPKVKYT
TVDEYYNKFV
