PBER1_ARATH
ID PBER1_ARATH Reviewed; 308 AA.
AC Q9T030; Q8RXS0;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Phenylcoumaran benzylic ether reductase 1 {ECO:0000303|PubMed:26601823};
DE Short=AtPCBER1 {ECO:0000303|PubMed:26601823};
DE EC=1.23.1.- {ECO:0000269|PubMed:26601823};
GN Name=PCBER1 {ECO:0000303|PubMed:26601823};
GN OrderedLocusNames=At4g39230 {ECO:0000312|Araport:AT4G39230};
GN ORFNames=T22F8.130 {ECO:0000312|EMBL:CAB43638.1};
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, TISSUE
RP SPECIFICITY, AND INDUCTION BY WOUNDING.
RX PubMed=26601823; DOI=10.1007/s00299-015-1899-1;
RA Nuoendagula X., Kamimura N., Mori T., Nakabayashi R., Tsuji Y.,
RA Hishiyama S., Saito K., Masai E., Kajita S.;
RT "Expression and functional analyses of a putative phenylcoumaran benzylic
RT ether reductase in Arabidopsis thaliana.";
RL Plant Cell Rep. 35:513-526(2016).
CC -!- FUNCTION: Oxidoreductase involved in lignan biosynthesis. Catalyzes the
CC NADPH-dependent reduction of phenylcoumaran benzylic ethers. Converts
CC dehydrodiconiferyl alcohol (DDC) to isodihydrodehydrodiconiferyl
CC alcohol (IDDDC), and dihydrodehydrodiconiferyl alcohol (DDDC) to
CC tetrahydrodehydrodiconiferyl alcohol (TDDC). Plays an important role in
CC the biosynthesis of secondary metabolites. In addition to the 8-5'-
CC linked neolignan DDC, can reduce the 8-8'-linked lignans, pinoresinol,
CC and lariciresinol, but with lower activities.
CC {ECO:0000269|PubMed:26601823}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(-)-dehydrodiconiferyl alcohol + H(+) + NADPH = (S)-
CC isodihydrodehydrodiconiferyl alcohol + NADP(+); Xref=Rhea:RHEA:59440,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:70467, ChEBI:CHEBI:143259;
CC Evidence={ECO:0000269|PubMed:26601823};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-dehydrodiconiferyl alcohol + H(+) + NADPH = (R)-
CC isodihydrodehydrodiconiferyl alcohol + NADP(+); Xref=Rhea:RHEA:59844,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:143256, ChEBI:CHEBI:143260;
CC Evidence={ECO:0000269|PubMed:26601823};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-dihydrodehydrodiconiferyl alcohol + H(+) + NADPH =
CC (S)-tetrahydrodehydrodiconiferyl alcohol + NADP(+);
CC Xref=Rhea:RHEA:59848, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:143258, ChEBI:CHEBI:143262;
CC Evidence={ECO:0000269|PubMed:26601823};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3R)-dihydrodehydrodiconiferyl alcohol + H(+) + NADPH =
CC (R)-tetrahydrodehydrodiconiferyl alcohol + NADP(+);
CC Xref=Rhea:RHEA:59852, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:143257, ChEBI:CHEBI:143263;
CC Evidence={ECO:0000269|PubMed:26601823};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.33 mM for dehydrodiconiferyl alcohol
CC {ECO:0000269|PubMed:26601823};
CC KM=0.68 mM for pinoresinol {ECO:0000269|PubMed:26601823};
CC Vmax=12.1 nmol/min/mg enzyme toward dehydrodiconiferyl alcohol
CC {ECO:0000269|PubMed:26601823};
CC Vmax=0.67 nmol/min/mg enzyme toward pinoresinol
CC {ECO:0000269|PubMed:26601823};
CC -!- TISSUE SPECIFICITY: Expressed in apical meristem and cotyledon veins of
CC young seedlings. Expressed in vascular tissues of roots, leaves, stems
CC and petals. Expressed in pollen grains. Expressed at low levels in
CC cauline leaves and siliques. {ECO:0000269|PubMed:26601823}.
CC -!- INDUCTION: Induced by wounding. {ECO:0000269|PubMed:26601823}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; AL050351; CAB43638.1; -; Genomic_DNA.
DR EMBL; AL161594; CAB80586.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87040.1; -; Genomic_DNA.
DR EMBL; AY150409; AAN12954.1; -; mRNA.
DR EMBL; AY080705; AAL85023.1; -; mRNA.
DR PIR; T08571; T08571.
DR RefSeq; NP_195634.1; NM_120083.5.
DR AlphaFoldDB; Q9T030; -.
DR SMR; Q9T030; -.
DR STRING; 3702.AT4G39230.1; -.
DR iPTMnet; Q9T030; -.
DR PaxDb; Q9T030; -.
DR PRIDE; Q9T030; -.
DR ProteomicsDB; 236440; -.
DR EnsemblPlants; AT4G39230.1; AT4G39230.1; AT4G39230.
DR GeneID; 830078; -.
DR Gramene; AT4G39230.1; AT4G39230.1; AT4G39230.
DR KEGG; ath:AT4G39230; -.
DR Araport; AT4G39230; -.
DR TAIR; locus:2136383; AT4G39230.
DR eggNOG; ENOG502QPMY; Eukaryota.
DR HOGENOM; CLU_060833_0_1_1; -.
DR InParanoid; Q9T030; -.
DR OMA; GHTSFEI; -.
DR OrthoDB; 936727at2759; -.
DR PhylomeDB; Q9T030; -.
DR BioCyc; ARA:AT4G39230-MON; -.
DR PRO; PR:Q9T030; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T030; baseline and differential.
DR GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IDA:UniProtKB.
DR GO; GO:0009807; P:lignan biosynthetic process; IDA:UniProtKB.
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 NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..308
FT /note="Phenylcoumaran benzylic ether reductase 1"
FT /id="PRO_0000442615"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 11..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 137
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT CONFLICT 165
FT /note="Q -> R (in Ref. 3; AAL85023)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 34072 MW; 4324E74C99C676C3 CRC64;
MTSKSKILFI GGTGYIGKYI VEASARSGHP TLVLVRNSTL TSPSRSSTIE NFKNLGVQFL
LGDLDDHTSL VNSIKQADVV ISTVGHSLLG HQYKIISAIK EAGNVKRFFP SEFGNDVDRV
FTVEPAKSAY ATKAKIRRTI EAEGIPYTYV SCNFFAGYFL PTLAQPGATS APRDKVIVLG
DGNPKAVFNK EEDIGTYTIN AVDDPRTLNK ILYIRPPMNT YSFNDLVSLW ENKIGKTLER
IYVPEEQLLK QIIESSPPLN VMLSLCHCVF VKGGHTSFEI EPSFGVEASE LYPDVKYTTV
DEILNQYV
