PILR1_THUPL
ID PILR1_THUPL Reviewed; 313 AA.
AC Q9LD14;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Bifunctional pinoresinol-lariciresinol reductase 1;
DE Short=PLR-Tp1;
DE AltName: Full=(+)-pinoresinol reductase;
DE EC=1.23.1.1;
DE AltName: Full=(-)-lariciresinol reductase;
DE EC=1.23.1.4;
DE AltName: Full=(-)-pinoresinol reductase;
DE EC=1.23.1.3;
GN Name=PLR_Tp1;
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 X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), SUBUNIT, ACTIVE SITE, BINDING
RP SITES, AND MUTAGENESIS OF LYS-138.
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=(-)-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 -!- 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 Evidence={ECO:0000269|PubMed:9872995};
CC -!- SUBUNIT: Dimer. {ECO:0000269|PubMed:13129921}.
CC -!- MISCELLANEOUS: Phe-164, Val-268 and Leu-272 are involved in
CC enantiospecific binding of (-)-pinoresinol while in PLR_Tp2, a 'Gly-
CC 268' 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; AF242503; AAF63507.1; -; mRNA.
DR PDB; 1QYD; X-ray; 2.50 A; A/B/C/D=1-313.
DR PDBsum; 1QYD; -.
DR AlphaFoldDB; Q9LD14; -.
DR SMR; Q9LD14; -.
DR KEGG; ag:AAF63507; -.
DR BRENDA; 1.23.1.3; 6364.
DR BRENDA; 1.23.1.4; 6364.
DR EvolutionaryTrace; Q9LD14; -.
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:1902125; P:(+)-pinoresinol catabolic process; IDA:UniProtKB.
DR GO; GO:1902135; P:(+)-secoisolariciresinol biosynthetic process; IDA:UniProtKB.
DR GO; GO:1902129; P:(-)-lariciresinol biosynthetic process; IDA:UniProtKB.
DR GO; GO:1902128; P:(-)-lariciresinol catabolic process; IDA:UniProtKB.
DR GO; GO:1902123; P:(-)-pinoresinol catabolic 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 3D-structure; NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..313
FT /note="Bifunctional pinoresinol-lariciresinol reductase 1"
FT /id="PRO_0000422932"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:13129921"
FT BINDING 11..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000305|PubMed:13129921"
FT BINDING 36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000305|PubMed:13129921"
FT BINDING 45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000305|PubMed:13129921"
FT BINDING 142
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000305|PubMed:13129921"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:13129921"
FT MUTAGEN 138
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:13129921"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1QYD"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:1QYD"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:1QYD"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:1QYD"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1QYD"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1QYD"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:1QYD"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1QYD"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1QYD"
FT TURN 91..95
FT /evidence="ECO:0007829|PDB:1QYD"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:1QYD"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1QYD"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:1QYD"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1QYD"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:1QYD"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1QYD"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:1QYD"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1QYD"
FT HELIX 197..207
FT /evidence="ECO:0007829|PDB:1QYD"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1QYD"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:1QYD"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:1QYD"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1QYD"
FT HELIX 229..240
FT /evidence="ECO:0007829|PDB:1QYD"
FT HELIX 252..258
FT /evidence="ECO:0007829|PDB:1QYD"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:1QYD"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:1QYD"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:1QYD"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:1QYD"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:1QYD"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:1QYD"
FT HELIX 305..309
FT /evidence="ECO:0007829|PDB:1QYD"
SQ SEQUENCE 313 AA; 35580 MW; 3D3178ACB73E8BE7 CRC64;
MDKKSRVLIV GGTGYIGKRI VNASISLGHP TYVLFRPEVV SNIDKVQMLL YFKQLGAKLI
EASLDDHQRL VDALKQVDVV ISALAGGVLS HHILEQLKLV EAIKEAGNIK RFLPSEFGMD
PDIMEHALQP GSITFIDKRK VRRAIEAASI PYTYVSSNMF AGYFAGSLAQ LDGHMMPPRD
KVLIYGDGNV KGIWVDEDDV GTYTIKSIDD PQTLNKTMYI RPPMNILSQK EVIQIWERLS
EQNLDKIYIS SQDFLADMKD KSYEEKIVRC HLYQIFFRGD LYNFEIGPNA IEATKLYPEV
KYVTMDSYLE RYV
