PILR1_LINCY
ID PILR1_LINCY Reviewed; 315 AA.
AC B5KRH5;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Bifunctional pinoresinol-lariciresinol reductase;
DE Short=PLR-Lc1;
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_Lc1;
OS Linum corymbulosum (Linum) (Linum strictum subsp. corymbulosum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Linaceae; Linum.
OX NCBI_TaxID=480358;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18489708; DOI=10.1111/j.1365-313x.2008.03558.x;
RA Bayindir U., Alfermann A.W., Fuss E.;
RT "Hinokinin biosynthesis in Linum corymbulosum Reichenb.";
RL Plant J. 55:810-820(2008).
CC -!- FUNCTION: Reductase involved in lignan (-)-hinokinin biosynthesis.
CC Catalyzes the enantioselective conversion of (+)-pinoresinol into (+)-
CC lariciresinol and of (+)-lariciresinol into (-)-secoisolariciresinol.
CC Abstracts the 4R-hydride from the NADPH cofactor during catalysis. Has
CC also a low phenylcoumaran benzylic ether reductase activity.
CC {ECO:0000269|PubMed:18489708}.
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:18489708};
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:18489708};
CC -!- SUBUNIT: Dimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: Knock-down mutants of PLR_Lc1 show unequivocally that
CC (-)-hinokinin is synthesized via the (-)-secoisolariciresinol/(-)-
CC matairesinol pathway and not via the piperitol/sesamin pathway.
CC {ECO:0000305|PubMed:18489708}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; EU107358; ABW86959.1; -; mRNA.
DR AlphaFoldDB; B5KRH5; -.
DR SMR; B5KRH5; -.
DR KEGG; ag:ABW86959; -.
DR BRENDA; 1.23.1.1; 13209.
DR BRENDA; 1.23.1.2; 13209.
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..315
FT /note="Bifunctional pinoresinol-lariciresinol reductase"
FT /id="PRO_0000422940"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 14..20
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 146
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
SQ SEQUENCE 315 AA; 35137 MW; 59ADCF2D51572508 CRC64;
MGSLNESSKV LVIGGTGYLG KRLVKASLDA GHDTYVMHRP EIGVDIEKVQ LLLSFKMQGA
HLVSASFDDH RSLVDAVSLV DVVICAISGV HIRSHQILLQ LKLVQAIKEA GNVKRFLPSE
FGTDPARMGD AMEPGRVTFD DKMVVRRAIE EAAIPFTYVS ANCFAGYFLG GLCQPGSILP
SRDHVTLLGD GNQKGVYVDE NDIAAYTLKA IDDPRTLNKT LYIKPPKNIL SQRQVVGIWE
KHIGKQLHKT LLSEQDFLAA MKEQDYAEQV GLTHYYHVCY EGCLTNFEVE QDQEASKLYP
DVRYTTVEEY LKRYV
