PILR_LINUS
ID PILR_LINUS Reviewed; 312 AA.
AC P0DKC8;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Bifunctional pinoresinol-lariciresinol reductase;
DE Short=LuPLR;
DE Short=LuPLR1;
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].
RA Lewis N.G., Davin L.B., Dinkova-Kostova A.T., Fujita M., Gang D.R.,
RA Ford J.D., Sarkanen S.;
RT "Recombinant pinoresinol/lariciresinol reductase, recombinant dirigent
RT protein, and methods of use.";
RL Patent number WO0149833, 12-JUL-2001.
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=16794840; DOI=10.1007/s00425-006-0308-y;
RA Hano C., Martin I., Fliniaux O., Legrand B., Gutierrez L., Arroo R.R.,
RA Mesnard F., Lamblin F., Laine E.;
RT "Pinoresinol-lariciresinol reductase gene expression and
RT secoisolariciresinol diglucoside accumulation in developing flax (Linum
RT usitatissimum) seeds.";
RL Planta 224:1291-1301(2006).
RN [3]
RP DEVELOPMENTAL STAGE, AND INDUCTION BY ABSCISIC ACID.
RX PubMed=21837520; DOI=10.1007/s00425-011-1492-y;
RA Renouard S., Corbin C., Lopez T., Montguillon J., Gutierrez L., Lamblin F.,
RA Laine E., Hano C.;
RT "Abscisic acid regulates pinoresinol-lariciresinol reductase gene
RT expression and secoisolariciresinol accumulation in developing flax (Linum
RT usitatissimum L.) seeds.";
RL Planta 235:85-98(2012).
RN [4]
RP INDUCTION BY ABSCISIC ACID AND GIBBERELLINS.
RX PubMed=23273926; DOI=10.1016/j.jplph.2012.11.003;
RA Corbin C., Renouard S., Lopez T., Lamblin F., Laine E., Hano C.;
RT "Identification and characterization of cis-acting elements involved in the
RT regulation of ABA- and/or GA-mediated LuPLR1 gene expression and lignan
RT biosynthesis in flax (Linum usitatissimum L.) cell cultures.";
RL J. Plant Physiol. 170:516-522(2013).
CC -!- FUNCTION: Reductase involved in lignan biosynthesis. Catalyzes the
CC sequential conversion of pinoresinol into lariciresinol and of
CC lariciresinol into secoisolariciresinol. Abstracts the 4R-hydride from
CC the NADPH cofactor during catalysis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Dimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in seed coats, but not in embryos,
CC leaves, stems and roots. {ECO:0000269|PubMed:16794840}.
CC -!- DEVELOPMENTAL STAGE: Expressed during seed development, with a pic at
CC mid-maturation. {ECO:0000269|PubMed:21837520}.
CC -!- INDUCTION: Up-regulated by abscisic acid and down-regulated by
CC gibberellins. {ECO:0000269|PubMed:21837520,
CC ECO:0000269|PubMed:23273926}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; AX191955; CAC51250.1; -; Unassigned_DNA.
DR AlphaFoldDB; P0DKC8; -.
DR SMR; P0DKC8; -.
DR GO; GO:0010284; F:lariciresinol reductase activity; IEA:UniProt.
DR GO; GO:0010283; F:pinoresinol reductase activity; IEA:UniProt.
DR GO; GO:0042537; P:benzene-containing compound metabolic process; IEA:UniProt.
DR GO; GO:0034312; P:diol biosynthetic process; IEA:UniProt.
DR GO; GO:1901502; P:ether catabolic process; IEA:UniProt.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:0046700; P:heterocycle catabolic process; IEA:UniProt.
DR GO; GO:0009807; P:lignan biosynthetic process; IEA:UniProt.
DR GO; GO:0046273; P:lignan catabolic process; IEA:UniProt.
DR GO; GO:0046189; P:phenol-containing compound biosynthetic process; IEA:UniProt.
DR GO; GO:0019336; P:phenol-containing compound catabolic process; IEA:UniProt.
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 2: Evidence at transcript 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"
FT /id="PRO_0000422937"
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; 35112 MW; 533F22E27A30AA96 CRC64;
MGRCRVLVVG GTGYIGKRIV KASIEHGHDT YVLKRPETGL DIEKFQLLLS FKKQGAHLVE
ASFSDHESLV RAVKLVDVVI CTVSGAHSRS LLLQLKLVEA IKEAGNVKRF IPSEFGMDPA
RMGDALEPGR ETFDLKMVVR KAIEDANIPH TYISANCFGG YFVGNLSQLG PLTPPSDKVT
IYGDGNVKVV YMDEDDVATY TIMTIEDDRT LNKTMYFRPP ENVITHRQLV ETWEKLSGNQ
LQKTELSSQD FLALMEGKDV AEQIVIGHLY HIYYEGCLTN FDIDADQDQV EASSLYPEVE
YTRMKDYLMI YL
