PILR2_LINUS
ID PILR2_LINUS Reviewed; 330 AA.
AC E6Y2X0;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Bifunctional pinoresinol-lariciresinol reductase 2;
DE Short=PLR-Lu2;
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_Lu2;
OS Linum usitatissimum (Flax) (Linum humile).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Linaceae; Linum.
OX NCBI_TaxID=4006;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=20514607; DOI=10.1055/s-0030-1250036;
RA Hemmati S., von Heimendahl C.B., Klaes M., Alfermann A.W., Schmidt T.J.,
RA Fuss E.;
RT "Pinoresinol-lariciresinol reductases with opposite enantiospecificity
RT determine the enantiomeric composition of lignans in the different organs
RT of Linum usitatissimum L.";
RL Planta Med. 76:928-934(2010).
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:20514607}.
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:20514607};
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:20514607};
CC -!- SUBUNIT: Dimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, leaves and seeds.
CC {ECO:0000269|PubMed:20514607}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; EU029951; ABW24501.1; -; mRNA.
DR AlphaFoldDB; E6Y2X0; -.
DR SMR; E6Y2X0; -.
DR BRENDA; 1.23.1.1; 3037.
DR BRENDA; 1.23.1.2; 3037.
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 NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..330
FT /note="Bifunctional pinoresinol-lariciresinol reductase 2"
FT /id="PRO_0000422938"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 28..34
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 53
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 62
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 160
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
SQ SEQUENCE 330 AA; 36499 MW; 835BE2599EA516AC CRC64;
MAAGFLFHMG SLPAIATVGH KSKVLVIGGT GYLGKRLVTA SLAAGHETYV LQRPEIGVDI
EKIQLLLSFK KAGASLVSGS FNDYRSLVDA VKLVDVVICA VSGVHIRSHQ ILLQLKLVDA
IKEAGNVKRF LPSEFGTDPA TMENAMEPGR VTFDDKMVVR KAIEEAGIPF TYISANCFAG
YFLGGLCQPG FILPSREQVT LLGDGNQKAV YVDEDDIARY TIKMIDDPRT LNKTVYIKPP
KNVLSQREVV GIWEKYIGKE LKKTTLSVEE FLAMMKEQDY AEQVGLTHYY HVCYEGCLTN
FEIGDEAGEA TKLYPEVGYT TVVEYMKRYV
