ID PILR3_ARATH Reviewed; 306 AA.
AC O65679;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 24-JAN-2024, entry version 130.
DE RecName: Full=Probable pinoresinol-lariciresinol reductase 3;
DE Short=AtPLR3;
DE EC=1.23.1.-;
DE AltName: Full=lariciresinol reductase;
GN Name=PLR3; OrderedLocusNames=At4g34540; ORFNames=T4L20.120;
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).
CC -!- FUNCTION: Probable reductase that might be involved in the reduction of
CC lariciresinol into secoisolariciresinol. In most plant species, a
CC single enzyme is able to reduce both pinoresinol and lariciresinol
CC efficiently while in Arabidopsis, PRR1 and PRR2 show a strict substrate
CC selectivity for pinoresinol.
CC -!- SUBUNIT: Dimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; AL023094; CAA18833.1; -; Genomic_DNA.
DR EMBL; AL161585; CAB80171.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86390.1; -; Genomic_DNA.
DR PIR; T05274; T05274.
DR RefSeq; NP_195180.1; NM_119619.2.
DR AlphaFoldDB; O65679; -.
DR SMR; O65679; -.
DR STRING; 3702.O65679; -.
DR PaxDb; 3702-AT4G34540-1; -.
DR ProteomicsDB; 236159; -.
DR EnsemblPlants; AT4G34540.1; AT4G34540.1; AT4G34540.
DR GeneID; 829605; -.
DR Gramene; AT4G34540.1; AT4G34540.1; AT4G34540.
DR KEGG; ath:AT4G34540; -.
DR Araport; AT4G34540; -.
DR TAIR; AT4G34540; GVS1.
DR eggNOG; ENOG502QTF0; Eukaryota.
DR HOGENOM; CLU_060833_0_0_1; -.
DR InParanoid; O65679; -.
DR OMA; TPYPENM; -.
DR PhylomeDB; O65679; -.
DR BioCyc; ARA:AT4G34540-MONOMER; -.
DR PRO; PR:O65679; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65679; baseline and differential.
DR Genevisible; O65679; AT.
DR GO; GO:0010283; F:pinoresinol reductase activity; ISS:TAIR.
DR GO; GO:1900057; P:positive regulation of leaf senescence; IMP:TAIR.
DR GO; GO:0033194; P:response to hydroperoxide; IMP:TAIR.
DR CDD; cd05259; PCBER_SDR_a; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR008030; NmrA-like.
DR InterPro; IPR045312; PCBER-like.
DR PANTHER; PTHR43349; PINORESINOL REDUCTASE-RELATED; 1.
DR PANTHER; PTHR43349:SF34; PINORESINOL-LARICIRESINOL REDUCTASE 3-RELATED; 1.
DR Pfam; PF05368; NmrA; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..306
FT /note="Probable pinoresinol-lariciresinol reductase 3"
FT /id="PRO_0000422931"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 14..20
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 46
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 135
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
SQ SEQUENCE 306 AA; 34071 MW; 46E09D5AC4C60174 CRC64;
MEEEKKKSRV LIIGATGRLG NYLTRFSIES GHPTFALIRN TTLSDKLKSL SDAGVTLLKG
SLEDEGSLAE AVSKVDVVIS AIPSKHVLDQ KLLVRVIKQA GSIKRFIPAE YGANPDKTQV
SDLDHDFYSK KSEIRHMIES EGIPYTYICC GLFMRVLLPS LVQPGLQSPP TDKVTVFGDG
NVKAVFVNDV DVAAFTIKTI DDPRTLNKTL YLSPPGNICS MNDLVELWEG KIEKKLEKTF
ATENQLLKKI KETPYPDNME MVFIYSVFIK GDHTYFDIES CGGVNGTELY PDVKYMTVSE
FLDTLL
//
