PILR1_LINUS
ID PILR1_LINUS Reviewed; 312 AA.
AC Q4R0H9;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Bifunctional pinoresinol-lariciresinol reductase 1;
DE Short=PLR-Lu1;
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_Lu1;
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, AND CATALYTIC ACTIVITY.
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 TISSUE 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:15949826}.
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:15949826};
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:15949826};
CC -!- SUBUNIT: Dimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds and roots, but not in stems.
CC Detected in leaves. {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; AJ849359; CAH60858.1; -; mRNA.
DR AlphaFoldDB; Q4R0H9; -.
DR SMR; Q4R0H9; -.
DR BRENDA; 1.23.1.3; 3037.
DR BRENDA; 1.23.1.4; 3037.
DR GO; GO:0010284; F:lariciresinol reductase activity; IDA:UniProtKB.
DR GO; GO:0010283; F:pinoresinol reductase activity; 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 NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..312
FT /note="Bifunctional pinoresinol-lariciresinol reductase 1"
FT /id="PRO_0000422936"
FT ACT_SITE 136
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 140
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
SQ SEQUENCE 312 AA; 35032 MW; A4DA5EDA11304A9C CRC64;
MGRCRVLVVG GTGYIGKRIV KASIEHGHDT YVLKRPETGL DIEKFQLLLS FKKQGAHLVE
ASFSDHESLV RAVKLVDVVI CTVSGAHSRS LLLQLKLVEA IKEAGNVKRF IPSEFGMDPA
RMGDALEPGR ETFDLKMVVR KAIEDANIPH TYISANCFGG YFVGNLSQLG PLTPPSDKVT
IYGDGNVKVV YMDEDDVATY TIMTIEDDRT LNKTMYLRPP ENVITHRQLV ETWEKLSGNQ
LQKTELSSQD FLALMEGKDV AEQVVIGHLY HIYYEGCLTN FDIDAAQDQV EASSLYPEVE
YIRMKDYLMI YL
