PILR4_THUPL
ID PILR4_THUPL Reviewed; 312 AA.
AC Q9LD12;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Bifunctional pinoresinol-lariciresinol reductase;
DE Short=PLR-TP4;
DE AltName: Full=(+)-lariciresinol reductase;
DE EC=1.23.1.2;
DE AltName: Full=(+)-pinoresinol reductase;
DE EC=1.23.1.1;
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).
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:34419, ChEBI:CHEBI:40, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:67246; EC=1.23.1.1;
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 -!- 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; AF242506; AAF63510.1; -; mRNA.
DR AlphaFoldDB; Q9LD12; -.
DR SMR; Q9LD12; -.
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..312
FT /note="Bifunctional pinoresinol-lariciresinol reductase"
FT /id="PRO_0000422935"
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; 34856 MW; 927E1947CCFD7552 CRC64;
MEESSRILVV GGTGYIGRRI VKASIALGHP TFILFRKEVV SDVEKVEMLL SFKKNGAKLL
EASFDDHESL VDAVKQVDVV ISAVAGNHMR HHILQQLKLV EAIKEAGNIK RFVPSEFGMD
PGLMDHAMAP GNIVFIDKIK VREAIEAAAI PHTYISANIF AGYLVGGLAQ LGRVMPPSDK
VFLYGDGNVK AVWIDEEDVG IYTIKAIDDP RTLNKTVYIR PPLNVLSQKE VVEKWEKLSR
KSLDKIYMSV EDFLAGMEGQ SYGEKIGISH FYQMFYKGDL YNFEIGPNGV EASQLYPGVK
YTTVDSYMER YL
