PCBER_POPTR
ID PCBER_POPTR Reviewed; 306 AA.
AC B9HRL7; A9PF66;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Phenylcoumaran benzylic ether reductase POP1 {ECO:0000303|PubMed:10066819};
DE Short=PCBER-Pop1 {ECO:0000303|PubMed:10066819};
DE EC=1.23.1.- {ECO:0000269|PubMed:10066819};
GN Name=PCBER {ECO:0000305};
GN ORFNames=POPTR_0009s12070g {ECO:0000312|EMBL:EEE87743.1};
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually;
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.-L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA dePamphilis C.W., Detter J., Dirks B., Dubchak I., Duplessis S.,
RA Ehlting J., Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J.,
RA Groover A., Gunter L., Hamberger B., Heinze B., Helariutta Y.,
RA Henrissat B., Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.-J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.S.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Leaf;
RX PubMed=18230180; DOI=10.1186/1471-2164-9-57;
RA Ralph S.G., Chun H.J., Cooper D., Kirkpatrick R., Kolosova N., Gunter L.,
RA Tuskan G.A., Douglas C.J., Holt R.A., Jones S.J., Marra M.A., Bohlmann J.;
RT "Analysis of 4,664 high-quality sequence-finished poplar full-length cDNA
RT clones and their utility for the discovery of genes responding to insect
RT feeding.";
RL BMC Genomics 9:57-57(2008).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10066819; DOI=10.1074/jbc.274.11.7516;
RA Gang D.R., Kasahara H., Xia Z.Q., Vander Mijnsbrugge K., Bauw G.,
RA Boerjan W., Van Montagu M., Davin L.B., Lewis N.G.;
RT "Evolution of plant defense mechanisms. Relationships of phenylcoumaran
RT benzylic ether reductases to pinoresinol-lariciresinol and isoflavone
RT reductases.";
RL J. Biol. Chem. 274:7516-7527(1999).
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).
CC {ECO:0000269|PubMed:10066819}.
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:10066819};
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:10066819};
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:10066819};
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:10066819};
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; CM009298; EEE87743.1; -; Genomic_DNA.
DR EMBL; EF146981; ABK95019.1; -; mRNA.
DR RefSeq; XP_002313788.1; XM_002313752.2.
DR AlphaFoldDB; B9HRL7; -.
DR SMR; B9HRL7; -.
DR STRING; 3694.POPTR_0009s12070.1; -.
DR EnsemblPlants; PNT20896; PNT20896; POPTR_009G118100v3.
DR GeneID; 7464022; -.
DR Gramene; PNT20896; PNT20896; POPTR_009G118100v3.
DR KEGG; pop:7464022; -.
DR eggNOG; ENOG502QPMY; Eukaryota.
DR HOGENOM; CLU_060833_0_1_1; -.
DR InParanoid; B9HRL7; -.
DR OMA; GHTSFEI; -.
DR Proteomes; UP000006729; Chromosome 9.
DR ExpressionAtlas; B9HRL7; 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..306
FT /note="Phenylcoumaran benzylic ether reductase POP1"
FT /id="PRO_0000442614"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 9..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000305|PubMed:10066819"
FT BINDING 34
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 43
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"
FT CONFLICT 48
FT /note="Y -> D (in Ref. 2; ABK95019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 33752 MW; 21E2D888E4C543BD CRC64;
MASKILFIGG TGYIGKFIVE ASAKAGHPTF VLVRESTLSN PAKSVVIYNF KNLGVNFLIG
DLFDHESLVK AIKQVDVVIS TVGHAQLVEQ DRIIAAIKEA GNVKRFFPSE FGNDVDRVNA
VEPAKSAFAT KANVRRAIEA EGIPYTYVSS NFFSGYFLLS FNQPGATAPP RDKVVILGDG
NPKAVFNKED DIATYTIKAV DDPRTLNKIL YIKPPANTIS FNDLVSLWEK KIGKTLERIY
VPEEQLLKNI QEASVPVNVV LSIGHSVFVK GDHTNFEIEP SFGVEASELY PDVKYTTVDE
YLKQFV
