PILR1_ARATH
ID PILR1_ARATH Reviewed; 317 AA.
AC Q9FVQ6; Q8LBG5;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Pinoresinol reductase 1 {ECO:0000303|PubMed:18347017};
DE Short=AtPrR1 {ECO:0000303|PubMed:18347017};
DE AltName: Full=(+)-pinoresinol reductase {ECO:0000305};
DE EC=1.23.1.1 {ECO:0000269|PubMed:18347017};
DE AltName: Full=(-)-pinoresinol reductase {ECO:0000305};
DE EC=1.23.1.3 {ECO:0000269|PubMed:18347017};
DE AltName: Full=Pinoresinol-lariciresinol reductase 1 {ECO:0000303|PubMed:18347017};
DE Short=AtPLR1 {ECO:0000303|PubMed:18347017};
GN Name=PRR1 {ECO:0000303|PubMed:18347017};
GN Synonyms=PLR1 {ECO:0000303|PubMed:18347017};
GN OrderedLocusNames=At1g32100 {ECO:0000312|Araport:AT1G32100};
GN ORFNames=F3C3.10 {ECO:0000312|EMBL:AAG23447.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=18347017; DOI=10.1074/jbc.m801131200;
RA Nakatsubo T., Mizutani M., Suzuki S., Hattori T., Umezawa T.;
RT "Characterization of Arabidopsis thaliana pinoresinol reductase, a new type
RT of enzyme involved in lignan biosynthesis.";
RL J. Biol. Chem. 283:15550-15557(2008).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25107662; DOI=10.1016/j.phytochem.2014.07.008;
RA Zhao Q., Zeng Y., Yin Y., Pu Y., Jackson L.A., Engle N.L., Martin M.Z.,
RA Tschaplinski T.J., Ding S.Y., Ragauskas A.J., Dixon R.A.;
RT "Pinoresinol reductase 1 impacts lignin distribution during secondary cell
RT wall biosynthesis in Arabidopsis.";
RL Phytochemistry 112:170-178(2015).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH PINORESINOL AND
RP NADP, AND SUBUNIT.
RX PubMed=33990581; DOI=10.1038/s41467-021-23095-y;
RA Xiao Y., Shao K., Zhou J., Wang L., Ma X., Wu D., Yang Y., Chen J.,
RA Feng J., Qiu S., Lv Z., Zhang L., Zhang P., Chen W.;
RT "Structure-based engineering of substrate specificity for pinoresinol-
RT lariciresinol reductases.";
RL Nat. Commun. 12:2828-2828(2021).
CC -!- FUNCTION: Reductase involved in lignan biosynthesis (PubMed:18347017,
CC PubMed:25107662). Involved in secondary cell wall biosynthesis in fiber
CC cells (PubMed:25107662). Unlike conventional pinoresinol reductases
CC that can reduce both pinoresinol and lariciresinol, PRR1 shows a strict
CC substrate preference toward pinoresinol (PubMed:18347017). Active on
CC both (+) and (-)-pinoresinol (PubMed:18347017). Abstracts the 4R-
CC hydride from the NADPH cofactor during catalysis (PubMed:18347017).
CC {ECO:0000269|PubMed:18347017, ECO:0000269|PubMed:25107662}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(-)-lariciresinol + NADP(+) = (-)-pinoresinol + H(+) + NADPH;
CC Xref=Rhea:RHEA:34427, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:67244, ChEBI:CHEBI:67245; EC=1.23.1.3;
CC Evidence={ECO:0000269|PubMed:18347017};
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:18347017};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 uM for (+)-pinoresinol {ECO:0000269|PubMed:18347017};
CC KM=7.3 uM for (-)-pinoresinol {ECO:0000269|PubMed:18347017};
CC Vmax=35.5 nmol/min/mg enzyme toward pinoresinol
CC {ECO:0000269|PubMed:18347017};
CC Vmax=1.1 nmol/min/mg enzyme toward lariciresinol
CC {ECO:0000269|PubMed:18347017};
CC -!- SUBUNIT: Forms homodimers. {ECO:0000269|PubMed:33990581}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and stems.
CC {ECO:0000269|PubMed:18347017}.
CC -!- DISRUPTION PHENOTYPE: No significant difference in lariciresinol
CC content (PubMed:18347017). Prr1 and prr2 double mutants show a complete
CC inhibition of lariciresinol biosynthesis (PubMed:18347017). Elevated
CC levels of pinoresinol, reduced lignin content in the fiber cells, and a
CC slightly altered lignin structure with low abundance of cinnamyl
CC alcohol end groups (PubMed:25107662). {ECO:0000269|PubMed:18347017,
CC ECO:0000269|PubMed:25107662}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC084165; AAG23447.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31436.1; -; Genomic_DNA.
DR EMBL; AY065214; AAL38690.1; -; mRNA.
DR EMBL; AY096520; AAM20170.1; -; mRNA.
DR EMBL; AY087224; AAM64780.1; -; mRNA.
DR PIR; D86445; D86445.
DR RefSeq; NP_174490.1; NM_102944.3.
DR PDB; 7CS9; X-ray; 2.80 A; A/B/C/D=1-317.
DR PDB; 7CSA; X-ray; 1.96 A; A/B/C/D=1-317.
DR PDB; 7CSB; X-ray; 2.00 A; A/B/C/D=1-317.
DR PDB; 7CSC; X-ray; 2.52 A; A/B/C/D/E/F=1-317.
DR PDB; 7CSD; X-ray; 1.80 A; A/B/C/D=1-317.
DR PDB; 7CSE; X-ray; 2.44 A; A/B/C/D/E/F=1-317.
DR PDB; 7CSF; X-ray; 1.98 A; A/B/C/D=1-317.
DR PDBsum; 7CS9; -.
DR PDBsum; 7CSA; -.
DR PDBsum; 7CSB; -.
DR PDBsum; 7CSC; -.
DR PDBsum; 7CSD; -.
DR PDBsum; 7CSE; -.
DR PDBsum; 7CSF; -.
DR AlphaFoldDB; Q9FVQ6; -.
DR SMR; Q9FVQ6; -.
DR BioGRID; 25336; 6.
DR IntAct; Q9FVQ6; 2.
DR STRING; 3702.AT1G32100.1; -.
DR PaxDb; Q9FVQ6; -.
DR PRIDE; Q9FVQ6; -.
DR ProteomicsDB; 236734; -.
DR EnsemblPlants; AT1G32100.1; AT1G32100.1; AT1G32100.
DR GeneID; 840102; -.
DR Gramene; AT1G32100.1; AT1G32100.1; AT1G32100.
DR KEGG; ath:AT1G32100; -.
DR Araport; AT1G32100; -.
DR TAIR; locus:2031730; AT1G32100.
DR eggNOG; ENOG502QQTV; Eukaryota.
DR HOGENOM; CLU_060833_0_1_1; -.
DR InParanoid; Q9FVQ6; -.
DR OMA; MKEMDYA; -.
DR OrthoDB; 1427286at2759; -.
DR PhylomeDB; Q9FVQ6; -.
DR BioCyc; ARA:AT1G32100-MON; -.
DR BRENDA; 1.23.1.1; 399.
DR BRENDA; 1.23.1.3; 399.
DR BRENDA; 1.23.1.4; 399.
DR PRO; PR:Q9FVQ6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FVQ6; baseline and differential.
DR Genevisible; Q9FVQ6; AT.
DR GO; GO:0010283; F:pinoresinol reductase activity; IDA:TAIR.
DR GO; GO:0009807; P:lignan biosynthetic process; IDA:TAIR.
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 3D-structure; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..317
FT /note="Pinoresinol reductase 1"
FT /id="PRO_0000422929"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 18
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSA, ECO:0007744|PDB:7CSB"
FT BINDING 20
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSA, ECO:0007744|PDB:7CSB"
FT BINDING 21
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSA, ECO:0007744|PDB:7CSB"
FT BINDING 41
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSA, ECO:0007744|PDB:7CSB"
FT BINDING 50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSA, ECO:0007744|PDB:7CSB"
FT BINDING 90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSA, ECO:0007744|PDB:7CSB"
FT BINDING 91
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSB, ECO:0007744|PDB:7CSC"
FT BINDING 95
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSB, ECO:0007744|PDB:7CSC"
FT BINDING 98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSB, ECO:0007744|PDB:7CSC"
FT BINDING 121
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSA, ECO:0007744|PDB:7CSB"
FT BINDING 122
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSA, ECO:0007744|PDB:7CSD"
FT BINDING 125
FT /ligand="(-)-pinoresinol"
FT /ligand_id="ChEBI:CHEBI:67245"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSB, ECO:0007744|PDB:7CSC"
FT BINDING 144
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSA, ECO:0007744|PDB:7CSB"
FT BINDING 166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSA, ECO:0007744|PDB:7CSB"
FT BINDING 177
FT /ligand="(-)-pinoresinol"
FT /ligand_id="ChEBI:CHEBI:67245"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSC"
FT BINDING 178
FT /ligand="(-)-pinoresinol"
FT /ligand_id="ChEBI:CHEBI:67245"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSB"
FT CONFLICT 262
FT /note="N -> H (in Ref. 4; AAM64780)"
FT /evidence="ECO:0000305"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:7CSD"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:7CSD"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:7CSD"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:7CS9"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:7CSD"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:7CSD"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:7CSD"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:7CSD"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 138..153
FT /evidence="ECO:0007829|PDB:7CSD"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:7CSD"
FT TURN 171..175
FT /evidence="ECO:0007829|PDB:7CSD"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:7CSD"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:7CSD"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:7CSD"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:7CSD"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:7CSD"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:7CSF"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:7CSD"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:7CSD"
FT HELIX 309..314
FT /evidence="ECO:0007829|PDB:7CSD"
SQ SEQUENCE 317 AA; 35549 MW; 4D1819B9CF5C8B85 CRC64;
MGESKRTEKT RVLVVGATGY IGKRIVRACL AEGHETYVLQ RPEIGLEIEK VQLFLSFKKL
GARIVEGSFS DHQSLVSAVK LVDVVVSAMS GVHFRSHNIL VQLKLVEAIK EAGNVKRFLP
SEFGMDPPRM GHALPPGRET FDQKMEVRQA IEAAGIPYTY VVGACFAAYF AGNLSQMVTL
LPPKEKVNIY GDGNVKVVFA DEDDIAKYTA KTLNDPRTLN KTVNIRPPDN VLTQLELVQI
WEKLTGKELE KTNIAAQDFL ANIEQMEIPH QAGIGHFYHI FYEGCLTDHE VGEDEEASSL
YPDVKYKRMD DYLRMFL
