ID   PILR3_THUPL             Reviewed;         314 AA.
AC   Q9LD00;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Bifunctional pinoresinol-lariciresinol reductase 3;
DE            Short=PLR-TP3;
DE   AltName: Full=(-)-lariciresinol reductase;
DE            EC=1.23.1.4;
DE   AltName: Full=(-)-pinoresinol reductase;
DE            EC=1.23.1.3;
OS   Thuja plicata (Western red-cedar) (Giant arborvitae).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC   Thuja.
OX   NCBI_TaxID=3316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Stem;
RX   PubMed=9872995; DOI=10.1074/jbc.274.2.618;
RA   Fujita M., Gang D.R., Davin L.B., Lewis N.G.;
RT   "Recombinant pinoresinol-lariciresinol reductases from western red cedar
RT   (Thuja plicata) catalyze opposite enantiospecific conversions.";
RL   J. Biol. Chem. 274:618-627(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Stem;
RX   PubMed=10066819; DOI=10.1074/jbc.274.11.7516;
RA   Gang D.R., Kasahara H., Xia Z.Q., Vander Mijnsbrugge K., Bauw G.,
RA   Boerjan W., Van Montagu M., Davin L.B., Lewis N.G.;
RT   "Evolution of plant defense mechanisms. Relationships of phenylcoumaran
RT   benzylic ether reductases to pinoresinol-lariciresinol and isoflavone
RT   reductases.";
RL   J. Biol. Chem. 274:7516-7527(1999).
CC   -!- FUNCTION: Reductase involved in lignan biosynthesis. Catalyzes the
CC       enantioselective sequential conversion of (-)-pinoresinol into (-)-
CC       lariciresinol and of (-)-lariciresinol into (+)-secoisolariciresinol.
CC       Abstracts the 4R-hydride from the NADPH cofactor during catalysis (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(-)-lariciresinol + NADP(+) = (-)-pinoresinol + H(+) + NADPH;
CC         Xref=Rhea:RHEA:34427, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:67244, ChEBI:CHEBI:67245; EC=1.23.1.3;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(+)-secoisolariciresinol + NADP(+) = (-)-lariciresinol + H(+)
CC         + NADPH; Xref=Rhea:RHEA:34431, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:67244, ChEBI:CHEBI:67247; EC=1.23.1.4;
CC   -!- SUBUNIT: Dimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC       reductase subfamily. {ECO:0000305}.
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DR   EMBL; AF242505; AAF63509.1; -; mRNA.
DR   EMBL; AF242500; AAF64183.1; -; mRNA.
DR   AlphaFoldDB; Q9LD00; -.
DR   SMR; Q9LD00; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   NADP; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..314
FT                   /note="Bifunctional pinoresinol-lariciresinol reductase 3"
FT                   /id="PRO_0000422934"
FT   ACT_SITE        138
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         11..17
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         36
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         45
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         142
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         272
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
SQ   SEQUENCE   314 AA;  35408 MW;  64BA4ED27EF6E8CB CRC64;
     MDKKSRVLIV GGTGFIGKRI VKASLALGHP TYVLFRPEAL SYIDKVQMLI SFKQLGAKLL
     EASLDDHQGL VDVVKQVDVV ISAVSGGLVR HHILDQLKLV EAIKEAGNIK RFLPSEFGMD
     PDVVEDPLEP GNITFIDKRK VRRAIEAATI PYTYVSSNMF AGFFAGSLAQ LQDAPRMMPA
     RDKVLIYGDG NVKGVYVDED DAGIYIVKSI DDPRTLNKTV YIRPPMNILS QKEVVEIWER
     LSGLSLEKIY VSEDQLLNMK DKSYVEKMAR CHLYHFFIKG DLYNFEIGPN ATEGTKLYPE
     VKYTTMDSYM ERYL