ID   IRL1_GINBI              Reviewed;         306 AA.
AC   M1T9X3;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Phenylcoumaran benzylic ether reductase IRL1 {ECO:0000305};
DE            EC=1.23.1.- {ECO:0000269|PubMed:23459862};
DE   AltName: Full=Isoflavone reductase-like 1 {ECO:0000303|PubMed:23459862};
DE            Short=GbIRL1 {ECO:0000303|PubMed:23459862};
DE            Short=IFR-like protein 1 {ECO:0000303|PubMed:23459862};
GN   Name=IRL1 {ECO:0000303|PubMed:23459862};
OS   Ginkgo biloba (Ginkgo) (Maidenhair tree).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Ginkgoidae; Ginkgoales; Ginkgoaceae; Ginkgo.
OX   NCBI_TaxID=3311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RX   PubMed=23459862; DOI=10.1007/s00299-013-1397-2;
RA   Hua C., Linling L., Feng X., Yan W., Honghui Y., Conghua W., Shaobing W.,
RA   Zhiqin L., Juan H., Yuping W., Shuiyuan C., Fuliang C.;
RT   "Expression patterns of an isoflavone reductase-like gene and its possible
RT   roles in secondary metabolism in Ginkgo biloba.";
RL   Plant Cell Rep. 32:637-650(2013).
CC   -!- FUNCTION: Oxidoreductase involved in lignan biosynthesis. Catalyzes the
CC       NADPH-dependent reduction of phenylcoumaran benzylic ethers. Converts
CC       dehydrodiconiferyl alcohol (DDC) to isodihydrodehydrodiconiferyl
CC       alcohol (IDDDC), and dihydrodehydrodiconiferyl alcohol (DDDC) to
CC       tetrahydrodehydrodiconiferyl alcohol (TDDC). May regulate changes in
CC       lignin content and accumulation of flavonoids.
CC       {ECO:0000269|PubMed:23459862}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(-)-dehydrodiconiferyl alcohol + H(+) + NADPH = (S)-
CC         isodihydrodehydrodiconiferyl alcohol + NADP(+); Xref=Rhea:RHEA:59440,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:70467, ChEBI:CHEBI:143259;
CC         Evidence={ECO:0000269|PubMed:23459862};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(+)-dehydrodiconiferyl alcohol + H(+) + NADPH = (R)-
CC         isodihydrodehydrodiconiferyl alcohol + NADP(+); Xref=Rhea:RHEA:59844,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:143256, ChEBI:CHEBI:143260;
CC         Evidence={ECO:0000269|PubMed:23459862};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-dihydrodehydrodiconiferyl alcohol + H(+) + NADPH =
CC         (S)-tetrahydrodehydrodiconiferyl alcohol + NADP(+);
CC         Xref=Rhea:RHEA:59848, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:143258, ChEBI:CHEBI:143262;
CC         Evidence={ECO:0000269|PubMed:23459862};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3R)-dihydrodehydrodiconiferyl alcohol + H(+) + NADPH =
CC         (R)-tetrahydrodehydrodiconiferyl alcohol + NADP(+);
CC         Xref=Rhea:RHEA:59852, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:143257, ChEBI:CHEBI:143263;
CC         Evidence={ECO:0000269|PubMed:23459862};
CC   -!- TISSUE SPECIFICITY: Highly expressed in sclerotesta. Expressed in
CC       roots, and two-to-four year stems. {ECO:0000269|PubMed:23459862}.
CC   -!- INDUCTION: Induced by UV-B, wounding, salicylate, ethephon, 5-
CC       aminolevulinic acid and abscisic acid (ABA).
CC       {ECO:0000269|PubMed:23459862}.
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC       reductase subfamily. {ECO:0000305}.
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DR   EMBL; KC244282; AGG40646.1; -; mRNA.
DR   AlphaFoldDB; M1T9X3; -.
DR   SMR; M1T9X3; -.
DR   BRENDA; 1.3.1.45; 2435.
DR   GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IDA:UniProtKB.
DR   GO; GO:0009807; P:lignan biosynthetic process; IDA: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   1: Evidence at protein level;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..306
FT                   /note="Phenylcoumaran benzylic ether reductase IRL1"
FT                   /id="PRO_0000442618"
FT   ACT_SITE        132
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         10..16
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         35
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         44
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         136
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
SQ   SEQUENCE   306 AA;  33286 MW;  6E45A81687D62A62 CRC64;
     MGKSRILIIG ATGYIGRQVA KASAALGHPT LILVRETTAS NPEKAQLLES FKSSGITIVH
     GSLEDHASLV EAIKKVDVVI STVGGAQIAD QLNIIKAIKE VGTIKRFLPT EFGNDVDKTS
     AVEPAKGLFA LKVKIRRAIE AEGIPYTYVS SNCFAGYFLP NLGQPGLTAP PRDKIVIFGD
     GNAKAVFVKE EDIGTFTIKS VDDPRTLNKT LYLRLPANTF SFNELVALWE KKIGKTLEKV
     YVPEEQVLKT IAETPFPGNI IISIAHSIFV KGDQTNFEIG DNGVEGSELY PDVKYTTVDE
     YLNQFV