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Protein

Bifunctional pinoresinol-lariciresinol reductase 1

Gene

PLR_Tp1

Organism
Thuja plicata (Western red-cedar) (Giant arborvitae)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reductase involved in lignan biosynthesis. Catalyzes the enantioselective sequential conversion of (-)-pinoresinol into (-)-lariciresinol and of (-)-lariciresinol into (+)-secoisolariciresinol. Can also convert with a lower efficiency (+)-pinoresinol into (+)-lariciresinol, but not (+)-lariciresinol into (-)-secoisolariciresinol. Abstracts the 4R-hydride from the NADPH cofactor during catalysis.1 Publication

Catalytic activityi

+-lariciresinol + NADP+ = (+)-pinoresinol + NADPH.1 Publication
--lariciresinol + NADP+ = (-)-pinoresinol + NADPH.1 Publication
+-secoisolariciresinol + NADP+ = (-)-lariciresinol + NADPH.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361NADPSequence analysis
Binding sitei41 – 411NADPSequence analysis
Binding sitei45 – 451NADPSequence analysis
Active sitei138 – 1381Proton acceptorSequence analysis
Binding sitei142 – 1421NADPSequence analysis
Binding sitei271 – 2711SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 166NADPHSequence analysis

GO - Molecular functioni

  • lariciresinol reductase activity Source: UniProtKB
  • pinoresinol reductase activity Source: UniProtKB

GO - Biological processi

  • (-)-lariciresinol biosynthetic process Source: UniProtKB
  • (-)-lariciresinol catabolic process Source: UniProtKB
  • (-)-pinoresinol catabolic process Source: UniProtKB
  • (+)-lariciresinol biosynthetic process Source: UniProtKB
  • (+)-pinoresinol catabolic process Source: UniProtKB
  • (+)-secoisolariciresinol biosynthetic process Source: UniProtKB
  • lignan biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.23.1.3. 6364.
1.23.1.4. 6364.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional pinoresinol-lariciresinol reductase 1
Short name:
PLR-Tp1
Alternative name(s):
(+)-pinoresinol reductase (EC:1.23.1.1)
(-)-lariciresinol reductase (EC:1.23.1.4)
(-)-pinoresinol reductase (EC:1.23.1.3)
Gene namesi
Name:PLR_Tp1
OrganismiThuja plicata (Western red-cedar) (Giant arborvitae)
Taxonomic identifieri3316 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinidaeCupressalesCupressaceaeThuja

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi138 – 1381K → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 313312Bifunctional pinoresinol-lariciresinol reductase 1PRO_0000422932Add
BLAST

Interactioni

Subunit structurei

Dimer.1 Publication

Structurei

Secondary structure

1
313
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115Combined sources
Helixi17 – 2610Combined sources
Beta strandi31 – 344Combined sources
Helixi43 – 5311Combined sources
Turni54 – 563Combined sources
Beta strandi58 – 603Combined sources
Helixi67 – 748Combined sources
Beta strandi78 – 825Combined sources
Beta strandi87 – 904Combined sources
Turni91 – 955Combined sources
Helixi96 – 10510Combined sources
Beta strandi110 – 1134Combined sources
Helixi133 – 14715Combined sources
Beta strandi154 – 1563Combined sources
Helixi161 – 1644Combined sources
Turni165 – 1673Combined sources
Beta strandi179 – 1824Combined sources
Beta strandi190 – 1956Combined sources
Helixi197 – 20711Combined sources
Helixi211 – 2133Combined sources
Beta strandi214 – 2196Combined sources
Helixi223 – 2253Combined sources
Beta strandi226 – 2283Combined sources
Helixi229 – 24012Combined sources
Helixi252 – 2587Combined sources
Helixi265 – 2684Combined sources
Turni269 – 2713Combined sources
Helixi272 – 2754Combined sources
Turni280 – 2823Combined sources
Beta strandi288 – 2925Combined sources
Helixi293 – 2964Combined sources
Helixi305 – 3095Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QYDX-ray2.50A/B/C/D1-313[»]
ProteinModelPortaliQ9LD14.
SMRiQ9LD14. Positions 2-313.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9LD14.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR016040. NAD(P)-bd_dom.
IPR008030. NmrA-like.
[Graphical view]
PfamiPF05368. NmrA. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9LD14-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKKSRVLIV GGTGYIGKRI VNASISLGHP TYVLFRPEVV SNIDKVQMLL
60 70 80 90 100
YFKQLGAKLI EASLDDHQRL VDALKQVDVV ISALAGGVLS HHILEQLKLV
110 120 130 140 150
EAIKEAGNIK RFLPSEFGMD PDIMEHALQP GSITFIDKRK VRRAIEAASI
160 170 180 190 200
PYTYVSSNMF AGYFAGSLAQ LDGHMMPPRD KVLIYGDGNV KGIWVDEDDV
210 220 230 240 250
GTYTIKSIDD PQTLNKTMYI RPPMNILSQK EVIQIWERLS EQNLDKIYIS
260 270 280 290 300
SQDFLADMKD KSYEEKIVRC HLYQIFFRGD LYNFEIGPNA IEATKLYPEV
310
KYVTMDSYLE RYV
Length:313
Mass (Da):35,580
Last modified:October 1, 2000 - v1
Checksum:i3D3178ACB73E8BE7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF242503 mRNA. Translation: AAF63507.1.

Genome annotation databases

KEGGiag:AAF63507.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF242503 mRNA. Translation: AAF63507.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QYDX-ray2.50A/B/C/D1-313[»]
ProteinModelPortaliQ9LD14.
SMRiQ9LD14. Positions 2-313.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAF63507.

Enzyme and pathway databases

BRENDAi1.23.1.3. 6364.
1.23.1.4. 6364.

Miscellaneous databases

EvolutionaryTraceiQ9LD14.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR016040. NAD(P)-bd_dom.
IPR008030. NmrA-like.
[Graphical view]
PfamiPF05368. NmrA. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPILR1_THUPL
AccessioniPrimary (citable) accession number: Q9LD14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2013
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Phe-164, Val-268 and Leu-272 are involved in enantiospecific binding of (-)-pinoresinol while in PLR_Tp2, a 'Gly-268' and a symmetric substitution between Phe and Leu favor binding of the (+)-antipode of pinoresinol.1 Publication

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.