PLR_SINHE
ID PLR_SINHE Reviewed; 311 AA.
AC B0LL23; B5AKD4;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Bifunctional pinoresinol-lariciresinol reductase {ECO:0000303|PubMed:23653238, ECO:0000303|Ref.2};
DE Short=PhPLR {ECO:0000303|PubMed:23653238};
DE AltName: Full=(+)-lariciresinol reductase {ECO:0000305};
DE EC=1.23.1.2 {ECO:0000269|PubMed:26359402};
DE AltName: Full=(+)-pinoresinol reductase {ECO:0000305};
DE EC=1.23.1.1 {ECO:0000269|PubMed:26359402};
GN Name=PLR {ECO:0000303|PubMed:23653238};
OS Sinopodophyllum hexandrum (Himalayan may apple) (Podophyllum hexandrum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Berberidaceae; Podophylloideae;
OC Sinopodophyllum.
OX NCBI_TaxID=93608;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY WOUNDING;
RP UV-LIGHT AND JASMONIC ACID.
RX PubMed=23653238; DOI=10.1007/s00709-013-0505-z;
RA Wankhede D.P., Biswas D.K., Rajkumar S., Sinha A.K.;
RT "Expressed sequence tags and molecular cloning and characterization of gene
RT encoding pinoresinol/lariciresinol reductase from Podophyllum hexandrum.";
RL Protoplasma 250:1239-1249(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sharma M., Pal R.S., Kumar S., Ahuja P.;
RT "Molecular cloning of genes involved in podophyllotoxin biosynthetic
RT pathway.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOTECHNOLOGY, TISSUE SPECIFICITY, INDUCTION
RP BY WOUNDING, AND PATHWAY.
RX PubMed=26359402; DOI=10.1126/science.aac7202;
RA Lau W., Sattely E.S.;
RT "Six enzymes from mayapple that complete the biosynthetic pathway to the
RT etoposide aglycone.";
RL Science 349:1224-1228(2015).
CC -!- FUNCTION: Reductase involved in lignan biosynthesis (PubMed:26359402).
CC Also involved in the biosynthesis of etoposide, a chemotherapeutic
CC compound of the topoisomerase inhibitor family (PubMed:26359402).
CC Catalyzes the enantioselective sequential conversion of (+)-pinoresinol
CC into (+)-lariciresinol and of (+)-lariciresinol into (-)-
CC secoisolariciresinol (PubMed:26359402). Abstracts the 4R-hydride from
CC the NADPH cofactor during catalysis (PubMed:26359402).
CC {ECO:0000269|PubMed:26359402}.
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:26359402};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34424;
CC Evidence={ECO:0000269|PubMed:26359402};
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:26359402};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34420;
CC Evidence={ECO:0000269|PubMed:26359402};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000269|PubMed:26359402}.
CC -!- SUBUNIT: Dimer. {ECO:0000250|UniProtKB:Q9LD14}.
CC -!- TISSUE SPECIFICITY: Expressed in rhizomes, stems, and leaves.
CC {ECO:0000269|PubMed:23653238, ECO:0000269|PubMed:26359402}.
CC -!- INDUCTION: Transiently induced after wounding and by jasmonic acid
CC (MeJA) (PubMed:26359402, PubMed:23653238). After an exposition to UV-
CC light, first transiently induced before fading out (PubMed:23653238).
CC {ECO:0000269|PubMed:23653238, ECO:0000269|PubMed:26359402}.
CC -!- BIOTECHNOLOGY: Combinatorially expression of Sinopodophyllum hexandrum
CC (mayapple) genes of the podophyllotoxin pathway (e.g. DIR, PLR, SDH,
CC CYP719A23, OMT3, CYP71CU1, OMT1, 2-ODD, CYP71BE54 and CYP82D61) in
CC Nicotiana benthamiana (tobacco) results in the production of the
CC chemotherapeutic compound etoposide. {ECO:0000305|PubMed:26359402}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; EU855792; ACF71492.1; -; mRNA.
DR EMBL; EU240218; ABY75535.2; -; mRNA.
DR AlphaFoldDB; B0LL23; -.
DR SMR; B0LL23; -.
DR KEGG; ag:ABY75535; -.
DR UniPathway; UPA00711; -.
DR GO; GO:0010284; F:lariciresinol reductase activity; IDA:UniProtKB.
DR GO; GO:0010283; F:pinoresinol reductase activity; 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:0019438; P:aromatic compound biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009411; P:response to UV; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP: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 CHAIN 1..311
FT /note="Bifunctional pinoresinol-lariciresinol reductase"
FT /id="PRO_0000451899"
FT ACT_SITE 138
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 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"
FT CONFLICT 24
FT /note="L -> F (in Ref. 1; ACF71492)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="V -> I (in Ref. 1; ACF71492)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="E -> K (in Ref. 1; ACF71492)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 34775 MW; C06FBFE0CE2753C6 CRC64;
MAKSRVLIVG GTGYLGRRMV KACLDQGHTT YVLHRQEVGV DIDKIQMLLS FKEQGAHLVE
GSFNDHRSLV EAVKLVDVVI CTISGVHIRS HQILLQLKLV EAIEEAGNVK RFLPSEFGMD
PARMAHAMEP GRATFDEKMV VRKAIEDAKI PHTYASANCF AGYFLGGLCQ FGKIIPSKES
VILSGDGNVK GIYVDEYDIA TYTIKTMDDP RTLNKTIYIR PPANILSQRE VVEIWEKLIG
KVLDKSSLSE EDFLALMKGL SHGHQAGLTH YYHVSYEGCL TNFEVEDGVD ASKLYPQVNY
TTVSEYLKRY L
