PILR2_ARATH
ID PILR2_ARATH Reviewed; 317 AA.
AC Q9SVP6;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Pinoresinol reductase 2 {ECO:0000303|PubMed:18347017};
DE Short=AtPrR2 {ECO:0000303|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 2 {ECO:0000303|PubMed:18347017};
DE Short=AtPLR2 {ECO:0000303|PubMed:18347017};
GN Name=PRR2 {ECO:0000303|PubMed:18347017};
GN Synonyms=PLR2 {ECO:0000303|PubMed:18347017};
GN OrderedLocusNames=At4g13660 {ECO:0000312|Araport:AT4G13660};
GN ORFNames=F18A5.50 {ECO:0000312|EMBL:CAB36830.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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 [5]
RP X-RAY CRYSTALLOGRAPHY (1.59 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 Unlike conventional pinoresinol reductases that can reduce both
CC pinoresinol and lariciresinol, PRR2 shows a strict substrate
CC selectivity for (-)-pinoresinol (PubMed:18347017). No activity with
CC (+)-pinoresinol or lariciresinol (PubMed:18347017). Abstracts the 4R-
CC hydride from the NADPH cofactor during catalysis (PubMed:18347017).
CC {ECO:0000269|PubMed:18347017}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.6 uM for (-)-pinoresinol {ECO:0000269|PubMed:18347017};
CC Vmax=5.9 nmol/min/mg enzyme toward pinoresinol
CC {ECO:0000269|PubMed:18347017};
CC -!- SUBUNIT: Forms homodimers. {ECO:0000269|PubMed:33990581}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. Detected in 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).
CC {ECO:0000269|PubMed:18347017}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; AL035528; CAB36830.1; -; Genomic_DNA.
DR EMBL; AL161537; CAB78408.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83310.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67572.1; -; Genomic_DNA.
DR EMBL; BT002882; AAO22699.1; -; mRNA.
DR EMBL; BT004406; AAO42400.1; -; mRNA.
DR PIR; T05235; T05235.
DR RefSeq; NP_001319922.1; NM_001340871.1.
DR RefSeq; NP_193102.1; NM_117440.3.
DR PDB; 7CSG; X-ray; 2.00 A; A/B=1-317.
DR PDB; 7CSH; X-ray; 1.59 A; A=1-317.
DR PDBsum; 7CSG; -.
DR PDBsum; 7CSH; -.
DR AlphaFoldDB; Q9SVP6; -.
DR SMR; Q9SVP6; -.
DR BioGRID; 12297; 1.
DR STRING; 3702.AT4G13660.1; -.
DR PaxDb; Q9SVP6; -.
DR PRIDE; Q9SVP6; -.
DR ProteomicsDB; 236629; -.
DR EnsemblPlants; AT4G13660.1; AT4G13660.1; AT4G13660.
DR EnsemblPlants; AT4G13660.2; AT4G13660.2; AT4G13660.
DR GeneID; 827000; -.
DR Gramene; AT4G13660.1; AT4G13660.1; AT4G13660.
DR Gramene; AT4G13660.2; AT4G13660.2; AT4G13660.
DR KEGG; ath:AT4G13660; -.
DR Araport; AT4G13660; -.
DR TAIR; locus:2119455; AT4G13660.
DR eggNOG; ENOG502QQTV; Eukaryota.
DR HOGENOM; CLU_060833_0_1_1; -.
DR InParanoid; Q9SVP6; -.
DR OMA; ERWGINY; -.
DR OrthoDB; 1427286at2759; -.
DR PhylomeDB; Q9SVP6; -.
DR BioCyc; ARA:AT4G13660-MON; -.
DR BRENDA; 1.23.1.1; 399.
DR BRENDA; 1.23.1.2; 399.
DR BRENDA; 1.23.1.3; 399.
DR PRO; PR:Q9SVP6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SVP6; baseline and differential.
DR Genevisible; Q9SVP6; AT.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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 2"
FT /id="PRO_0000422930"
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:7CSH"
FT BINDING 20
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSH"
FT BINDING 21
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSH"
FT BINDING 41
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSH"
FT BINDING 50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSH"
FT BINDING 90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSH"
FT BINDING 91
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSH"
FT BINDING 95
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSH"
FT BINDING 98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSH"
FT BINDING 121
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSH"
FT BINDING 125
FT /ligand="(-)-pinoresinol"
FT /ligand_id="ChEBI:CHEBI:67245"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSH"
FT BINDING 144
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSH"
FT BINDING 166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSH"
FT BINDING 178
FT /ligand="(-)-pinoresinol"
FT /ligand_id="ChEBI:CHEBI:67245"
FT /evidence="ECO:0000269|PubMed:33990581,
FT ECO:0007744|PDB:7CSH"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:7CSH"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:7CSH"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:7CSH"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:7CSH"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:7CSH"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:7CSH"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 138..154
FT /evidence="ECO:0007829|PDB:7CSH"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:7CSH"
FT TURN 171..175
FT /evidence="ECO:0007829|PDB:7CSH"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:7CSH"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:7CSH"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:7CSH"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:7CSH"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:7CSH"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:7CSH"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:7CSH"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:7CSH"
SQ SEQUENCE 317 AA; 35415 MW; BDCFC6BDEC403619 CRC64;
MKETNFGEKT RVLVVGGTGS LGRRIVSACL AEGHETYVLQ RPEIGVDIEK VQLLLSFKRL
GAHLVEGSFS DHQSLVSAVK QVDVVVSAMS GVHFRTHNIP VQLKLVAAIK EAGNVKRFLP
SEFGMDPSRM GHAMPPGSET FDQKMEIRNA IKAAGISHTY LVGACFAAYF GGNLSQMGTL
FPPKNKVDIY GDGNVKVVFV DEDDMAKYTA KTLNDPRTLN KTVYVRPTDN ILTQMELVQI
WEKLTEKELE KTYVSGNDFL ADIEDKEISH QAGLGHFYHI YYEGCLTDHE VGDDEEATKL
YPDVKYKRMD EYLKIFV
