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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)DescriptionActionsGraphical viewLength
Binding sitei36NADPSequence analysis1
Binding sitei41NADPSequence analysis1
Binding sitei45NADPSequence analysis1
Active sitei138Proton acceptorSequence analysis1
Binding sitei142NADPSequence analysis1
Binding sitei271SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 16NADPHSequence analysis6

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)DescriptionActionsGraphical viewLength
Mutagenesisi138K → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00004229322 – 313Bifunctional pinoresinol-lariciresinol reductase 1Add BLAST312

Interactioni

Subunit structurei

Dimer.1 Publication

Structurei

Secondary structure

1313
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 11Combined sources5
Helixi17 – 26Combined sources10
Beta strandi31 – 34Combined sources4
Helixi43 – 53Combined sources11
Turni54 – 56Combined sources3
Beta strandi58 – 60Combined sources3
Helixi67 – 74Combined sources8
Beta strandi78 – 82Combined sources5
Beta strandi87 – 90Combined sources4
Turni91 – 95Combined sources5
Helixi96 – 105Combined sources10
Beta strandi110 – 113Combined sources4
Helixi133 – 147Combined sources15
Beta strandi154 – 156Combined sources3
Helixi161 – 164Combined sources4
Turni165 – 167Combined sources3
Beta strandi179 – 182Combined sources4
Beta strandi190 – 195Combined sources6
Helixi197 – 207Combined sources11
Helixi211 – 213Combined sources3
Beta strandi214 – 219Combined sources6
Helixi223 – 225Combined sources3
Beta strandi226 – 228Combined sources3
Helixi229 – 240Combined sources12
Helixi252 – 258Combined sources7
Helixi265 – 268Combined sources4
Turni269 – 271Combined sources3
Helixi272 – 275Combined sources4
Turni280 – 282Combined sources3
Beta strandi288 – 292Combined sources5
Helixi293 – 296Combined sources4
Helixi305 – 309Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QYDX-ray2.50A/B/C/D1-313[»]
ProteinModelPortaliQ9LD14.
SMRiQ9LD14.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QYDX-ray2.50A/B/C/D1-313[»]
ProteinModelPortaliQ9LD14.
SMRiQ9LD14.
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: November 2, 2016
This is version 57 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.