PILR1_LINPE
ID PILR1_LINPE Reviewed; 314 AA.
AC A3R052;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Bifunctional pinoresinol-lariciresinol reductase;
DE Short=PLR-Lp1;
DE AltName: Full=(+)-pinoresinol reductase;
DE EC=1.23.1.1;
DE AltName: Full=(-)-lariciresinol reductase;
DE EC=1.23.1.4;
GN Name=PLR_Lp1;
OS Linum perenne (Perennial flax).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Linaceae; Linum.
OX NCBI_TaxID=35941;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17257599; DOI=10.1016/j.febslet.2007.01.018;
RA Hemmati S., Schmidt T.J., Fuss E.;
RT "(+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt
RT involved in the biosynthesis of justicidin B.";
RL FEBS Lett. 581:603-610(2007).
CC -!- FUNCTION: Reductase involved in the lignan justicidin B biosynthesis.
CC Catalyzes the enantioselective conversion of (+)-pinoresinol into (+)-
CC lariciresinol and of (-)-lariciresinol into (+)-secoisolariciresinol.
CC Low activity with the other enantiomers. Abstracts the 4R-hydride from
CC the NADPH cofactor during catalysis. {ECO:0000269|PubMed:17257599}.
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:17257599};
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:17257599};
CC -!- SUBUNIT: Dimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: Unlike most other PLRs, this enzyme has an opposite
CC enantiospecificity within the two reaction steps.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; EF050530; ABM68630.1; -; mRNA.
DR AlphaFoldDB; A3R052; -.
DR SMR; A3R052; -.
DR PRIDE; A3R052; -.
DR KEGG; ag:ABM68630; -.
DR BioCyc; MetaCyc:MON-16668; -.
DR BRENDA; 1.23.1.1; 13210.
DR BRENDA; 1.23.1.4; 13210.
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:1902125; P:(+)-pinoresinol catabolic process; IDA:UniProtKB.
DR GO; GO:1902135; P:(+)-secoisolariciresinol biosynthetic process; IDA:UniProtKB.
DR GO; GO:1902128; P:(-)-lariciresinol 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..314
FT /note="Bifunctional pinoresinol-lariciresinol reductase"
FT /id="PRO_0000422928"
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"
SQ SEQUENCE 314 AA; 35226 MW; 5D8951261983AD4F CRC64;
MKPCSVLVVG GTGYIGKRIV SASLYLGHDT YVLKRPGTGL DIEKLQLLLS FKKRGAHLVE
ASFSDHDSLV RAVRLVDVVI CTMSGVHFRS HNILLQLKLV EAIKEAGNVK RFIPSEFGMD
PARMGQAMEP GRETFDQKMV VRKAIEEANI PHTYISANCF AGYFVGNLSQ LGTLTPPSDK
VIIYGDGNVK VVYVDEDDVA KYTIKAIEDD RTVNKTVYLR PPENMMSQRE LVAVWEKLSG
NQLEKIELPP QDFLALMEGT TVAEQAGIGH FYHIFYEGCL TNFEINAENG EEEASRLYPE
VEYTRVHDYL KIYL
