PILR2_THUPL
ID PILR2_THUPL Reviewed; 312 AA.
AC Q9LD13;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Bifunctional pinoresinol-lariciresinol reductase 2;
DE Short=PLR-Tp2;
DE AltName: Full=(+)-lariciresinol reductase;
DE EC=1.23.1.2;
DE AltName: Full=(+)-pinoresinol reductase;
DE EC=1.23.1.1;
DE AltName: Full=(-)-pinoresinol reductase;
DE EC=1.23.1.3;
GN Name=PLR_Tp2;
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], FUNCTION, AND CATALYTIC ACTIVITY.
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 3D-STRUCTURE MODELING.
RX PubMed=13129921; DOI=10.1074/jbc.m308493200;
RA Min T., Kasahara H., Bedgar D.L., Youn B., Lawrence P.K., Gang D.R.,
RA Halls S.C., Park H., Hilsenbeck J.L., Davin L.B., Lewis N.G., Kang C.,
RA Lewis N.G.;
RT "Crystal structures of pinoresinol-lariciresinol and phenylcoumaran
RT benzylic ether reductases and their relationship to isoflavone
RT reductases.";
RL J. Biol. Chem. 278:50714-50723(2003).
CC -!- FUNCTION: Reductase involved in lignan biosynthesis. Catalyzes the
CC enantioselective sequential conversion of (+)-pinoresinol into (+)-
CC lariciresinol and of (+)-lariciresinol into (-)-secoisolariciresinol.
CC Can also convert with a lower efficiency (-)-pinoresinol into (-)-
CC lariciresinol, but not (-)-lariciresinol into (+)-secoisolariciresinol.
CC Abstracts the 4R-hydride from the NADPH cofactor during catalysis.
CC {ECO:0000269|PubMed:9872995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-lariciresinol + NADP(+) = (+)-pinoresinol + H(+) + NADPH;
CC Xref=Rhea:RHEA:34419, ChEBI:CHEBI:40, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67246; EC=1.23.1.1;
CC Evidence={ECO:0000269|PubMed:9872995};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(-)-secoisolariciresinol + NADP(+) = (+)-lariciresinol + H(+)
CC + NADPH; Xref=Rhea:RHEA:34423, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65004, ChEBI:CHEBI:67246; EC=1.23.1.2;
CC Evidence={ECO:0000269|PubMed:9872995};
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 Evidence={ECO:0000269|PubMed:9872995};
CC -!- SUBUNIT: Dimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: Leu-164, Gly-267 and Phe-271 are involved in
CC enantiospecific binding of (+)-pinoresinol while in PLR_Tp1, a 'Val-
CC 267' and a symmetric substitution between Phe and Leu favor binding of
CC the (-)-antipode of pinoresinol. {ECO:0000305|PubMed:13129921}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; AF242504; AAF63508.1; -; mRNA.
DR AlphaFoldDB; Q9LD13; -.
DR SMR; Q9LD13; -.
DR KEGG; ag:AAF63508; -.
DR GO; GO:0010284; F:lariciresinol reductase activity; IDA:UniProtKB.
DR GO; GO:0010283; F:pinoresinol reductase activity; IDA:UniProtKB.
DR GO; GO:1902132; P:(+)-lariciresinol biosynthetic process; IDA:UniProtKB.
DR GO; GO:1902131; P:(+)-lariciresinol catabolic process; IDA:UniProtKB.
DR GO; GO:1902125; P:(+)-pinoresinol catabolic process; IDA:UniProtKB.
DR GO; GO:1902129; P:(-)-lariciresinol biosynthetic process; IDA:UniProtKB.
DR GO; GO:1902123; P:(-)-pinoresinol catabolic process; IDA:UniProtKB.
DR GO; GO:1902138; P:(-)-secoisolariciresinol biosynthetic process; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..312
FT /note="Bifunctional pinoresinol-lariciresinol reductase 2"
FT /id="PRO_0000422933"
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 270
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
SQ SEQUENCE 312 AA; 34798 MW; F6579908F8A5717F CRC64;
MEESSRVLIV GGTGYIGRRI VKASIALGHP TFILFRKEVV SDVEKVEMLL SFKKNGAKLL
EASFDDHESL VDAVKQVDVV ISAVAGNHMR HHILQQLKLV EAIKEAGNIK RFVPSEFGMD
PGLMEHAMAP GNIVFIDKIK VREAIEAASI PHTYISANIF AGYLVGGLAQ LGRVMPPSEK
VILYGDGNVK AVWVDEDDVG IYTIKAIDDP HTLNKTMYIR PPLNILSQKE VVEKWEKLSG
KSLNKINISV EDFLAGMEGQ SYGEQIGISH FYQMFYRGDL YNFEIGPNGV EASQLYPEVK
YTTVDSYMER YL
