PILR1_LINAL
ID PILR1_LINAL Reviewed; 326 AA.
AC Q4R0I0; D2KYC2;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Bifunctional pinoresinol-lariciresinol reductase;
DE Short=PLR-La1;
DE AltName: Full=(+)-lariciresinol reductase;
DE EC=1.23.1.2;
DE AltName: Full=(+)-pinoresinol reductase;
DE EC=1.23.1.1;
GN Name=PLR1;
OS Linum album (Flax).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Linaceae; Linum.
OX NCBI_TaxID=191219;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS
RP OF MET-143; GLY-282; TYR-286 AND VAL-318.
RX PubMed=15949826; DOI=10.1016/j.phytochem.2005.04.026;
RA von Heimendahl C.B., Schafer K.M., Eklund P., Sjoholm R., Schmidt T.J.,
RA Fuss E.;
RT "Pinoresinol-lariciresinol reductases with different stereospecificity from
RT Linum album and Linum usitatissimum.";
RL Phytochemistry 66:1254-1263(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ahmadian Chashmi N., Tahsili J., Yousefzadi M., Sharifi M., Behmanesh M.;
RT "Coloning of PLR gene in Linum album.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INDUCTION BY SALICYLIC ACID.
RX PubMed=20607358; DOI=10.1007/s10529-010-0343-4;
RA Yousefzadi M., Sharifi M., Behmanesh M., Ghasempour A., Moyano E.,
RA Palazon J.;
RT "Salicylic acid improves podophyllotoxin production in cell cultures of
RT Linum album by increasing the expression of genes related with its
RT biosynthesis.";
RL Biotechnol. Lett. 32:1739-1743(2010).
RN [4]
RP INDUCTION BY ELICITOR.
RX PubMed=22218086; DOI=10.1016/j.jplph.2011.12.006;
RA Esmaeilzadeh Bahabadi S., Sharifi M., Behmanesh M., Safaie N., Murata J.,
RA Araki R., Yamagaki T., Satake H.;
RT "Time-course changes in fungal elicitor-induced lignan synthesis and
RT expression of the relevant genes in cell cultures of Linum album.";
RL J. Plant Physiol. 169:487-491(2012).
RN [5]
RP INDUCTION BY BLUE LIGHT.
RX PubMed=22579943; DOI=10.1016/j.plaphy.2012.04.010;
RA Yousefzadi M., Sharifi M., Behmanesh M., Ghasempour A., Moyano E.,
RA Palazon J.;
RT "The effect of light on gene expression and podophyllotoxin biosynthesis in
RT Linum album cell culture.";
RL Plant Physiol. Biochem. 56:41-46(2012).
CC -!- FUNCTION: Reductase involved in lignan biosynthesis. Catalyzes the
CC enantioselective conversion of (+)-pinoresinol into (+)-lariciresinol
CC and of (+)-lariciresinol into (-)-secoisolariciresinol. Abstracts the
CC 4R-hydride from the NADPH cofactor during catalysis.
CC {ECO:0000269|PubMed:15949826}.
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:15949826};
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:15949826};
CC -!- SUBUNIT: Dimer. {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by continuous blue light and fungal elicitor
CC treatment. Not regulated by salicylic acid.
CC {ECO:0000269|PubMed:20607358, ECO:0000269|PubMed:22218086,
CC ECO:0000269|PubMed:22579943}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; AJ849358; CAH60857.1; -; mRNA.
DR EMBL; AB525816; BAI66418.1; -; mRNA.
DR AlphaFoldDB; Q4R0I0; -.
DR SMR; Q4R0I0; -.
DR BRENDA; 1.23.1.1; 13208.
DR BRENDA; 1.23.1.2; 13208.
DR GO; GO:0010284; F:lariciresinol reductase activity; IDA:UniProtKB.
DR GO; GO:0010283; F:pinoresinol reductase activity; 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: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..326
FT /note="Bifunctional pinoresinol-lariciresinol reductase"
FT /id="PRO_0000422939"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 25..31
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 59
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 157
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT MUTAGEN 143
FT /note="M->L: No effect on enantiospecificity; when
FT associated with V-282; L-286 and M-318."
FT /evidence="ECO:0000269|PubMed:15949826"
FT MUTAGEN 282
FT /note="G->V: No effect on enantiospecificity; when
FT associated with L-286. No effect on enantiospecificity;
FT when associated with L-143; L-286 and M-318."
FT /evidence="ECO:0000269|PubMed:15949826"
FT MUTAGEN 286
FT /note="Y->L: No effect on enantiospecificity; when
FT associated with V-282. No effect on enantiospecificity;
FT when associated with L-143; V-282 and M-318."
FT /evidence="ECO:0000269|PubMed:15949826"
FT MUTAGEN 318
FT /note="V->M: No effect on enantiospecificity; when
FT associated with L-143; V-282 and L-286."
FT /evidence="ECO:0000269|PubMed:15949826"
FT CONFLICT 233
FT /note="Y -> H (in Ref. 2; BAI66418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 36379 MW; D13BCB60BC70B26F CRC64;
MGSLGKVNNE IPTKSSGGSK VLVIGGTGYL GKRLVKASLD SGHDTYVMHR PEIGVDIEKV
QLLLSFKMQG AHLVSASFDD QRSLVDAVKL VDVVICAISG VHIRSHQILL QLKLVEAIKE
AGNVKRFVPS EFGTDPARME NAMEPGRITF DDKMVVRRAI EEAGIPFTYV SANCFAGYFL
GGLCQPGYIL PSRDHVTLLG DGDKKGVYVD EDDTAAYTLR AIDDPRTLNK TIYVKPPKNV
LSQREVVGIW EKYIGKELQK TILSEQDFLA TMREQNYAEQ VGLTHYYHVC YEGCLSNFEV
DDEQEASKLY PDVHYTTVEE YLKRYV
