PILR1_FORIN
ID PILR1_FORIN Reviewed; 312 AA.
AC P93143;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Bifunctional pinoresinol-lariciresinol reductase;
DE Short=PLR-Fi1;
DE Short=PLR3;
DE AltName: Full=(+)-lariciresinol reductase;
DE EC=1.23.1.2;
DE AltName: Full=(+)-pinoresinol reductase;
DE EC=1.23.1.1;
GN Name=PLR_Fi1;
OS Forsythia intermedia (Border forsythia) (Forsythia suspensa x Forsythia
OS viridissima).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Oleaceae; Forsythieae; Forsythia.
OX NCBI_TaxID=55183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-31; 47-53; 113-140;
RP 231-238 AND 301-310, CLEAVAGE OF INITIATOR METHIONINE, FUNCTION, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Stem;
RX PubMed=8910615; DOI=10.1074/jbc.271.46.29473;
RA Dinkova-Kostova A.T., Gang D.R., Davin L.B., Bedgar D.L., Chu A.,
RA Lewis N.G.;
RT "(+)-Pinoresinol/(+)-lariciresinol reductase from Forsythia intermedia.
RT Protein purification, cDNA cloning, heterologous expression and comparison
RT to isoflavone reductase.";
RL J. Biol. Chem. 271:29473-29482(1996).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=11423140; DOI=10.1016/s0031-9422(01)00108-x;
RA Kwon M., Davin L.B., Lewis N.G.;
RT "In situ hybridization and immunolocalization of lignan reductases in woody
RT tissues: implications for heartwood formation and other forms of vascular
RT tissue preservation.";
RL Phytochemistry 57:899-914(2001).
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.
CC {ECO:0000269|PubMed:8910615}.
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:8910615};
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:8910615};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=27 uM for (+)-pinoresinol {ECO:0000269|PubMed:8910615};
CC KM=121 uM for (+)-lariciresinol {ECO:0000269|PubMed:8910615};
CC Vmax=16.2 umol/h/mg enzyme toward (+)-pinoresinol
CC {ECO:0000269|PubMed:8910615};
CC Vmax=25.2 umol/h/mg enzyme toward (+)-lariciresinol
CC {ECO:0000269|PubMed:8910615};
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:8910615};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:8910615};
CC -!- SUBUNIT: Dimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in young stems, young roots and petioles.
CC In stems, expressed in radial parenchyma cells and in the cambial cells
CC of developing secondary xylem. {ECO:0000269|PubMed:11423140}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; U81158; AAC49608.1; -; mRNA.
DR AlphaFoldDB; P93143; -.
DR SMR; P93143; -.
DR KEGG; ag:AAC49608; -.
DR BRENDA; 1.23.1.1; 13002.
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: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 Direct protein sequencing; NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8910615"
FT CHAIN 2..312
FT /note="Bifunctional pinoresinol-lariciresinol reductase"
FT /id="PRO_0000422927"
FT ACT_SITE 139
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 143
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
SQ SEQUENCE 312 AA; 34929 MW; B375128A931F7877 CRC64;
MGKSKVLIIG GTGYLGRRLV KASLAQGHET YILHRPEIGV DIDKVEMLIS FKMQGAHLVS
GSFKDFNSLV EAVKLVDVVI SAISGVHIRS HQILLQLKLV EAIKEAGNVK RFLPSEFGMD
PAKFMDTAME PGKVTLDEKM VVRKAIEKAG IPFTYVSANC FAGYFLGGLC QFGKILPSRD
FVIIHGDGNK KAIYNNEDDI ATYAIKTIND PRTLNKTIYI SPPKNILSQR EVVQTWEKLI
GKELQKITLS KEDFLASVKE LEYAQQVGLS HYHDVNYQGC LTSFEIGDEE EASKLYPEVK
YTSVEEYLKR YV
