PCBER_PINTA
ID PCBER_PINTA Reviewed; 308 AA.
AC Q9LL41; O81651;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Phenylcoumaran benzylic ether reductase PT1 {ECO:0000303|PubMed:10066819};
DE Short=PCBER-Pt1 {ECO:0000303|PubMed:10066819};
DE EC=1.23.1.- {ECO:0000269|PubMed:10066819, ECO:0000269|PubMed:12369619};
DE AltName: Full=PtPCBER {ECO:0000303|PubMed:12369619};
GN Name=PCBER {ECO:0000305};
OS Pinus taeda (Loblolly pine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3352;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12369619; DOI=10.1023/A:1019867732278;
RA Shoji T., Winz R., Iwase T., Nakajima K., Yamada Y., Hashimoto T.;
RT "Expression patterns of two tobacco isoflavone reductase-like genes and
RT their possible roles in secondary metabolism in tobacco.";
RL Plant Mol. Biol. 50:427-440(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
RX PubMed=13129921; DOI=10.1074/jbc.m308493200;
RA Min T., Kasahara H., Bedgar D.L., Youn B., Lawrence P.K., Gang D.R.,
RA Halls S.C., Park H., Hilsenbeck J.L., Davin L.B., Lewis N.G., Kang C.,
RA Lewis N.G.;
RT "Crystal structures of pinoresinol-lariciresinol and phenylcoumaran
RT benzylic ether reductases and their relationship to isoflavone
RT reductases.";
RL J. Biol. Chem. 278:50714-50723(2003).
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, ECO:0000269|PubMed:12369619}.
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, ECO:0000269|PubMed:12369619};
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, ECO:0000269|PubMed:12369619};
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, ECO:0000269|PubMed:12369619};
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, ECO:0000269|PubMed:12369619};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.61 mM for dehydrodiconiferyl alcohol
CC {ECO:0000269|PubMed:10066819};
CC KM=1.95 mM for dihydrodehydrodiconiferyl alcohol
CC {ECO:0000269|PubMed:10066819};
CC Vmax=104.2 nmol/h/mg enzyme toward dehydrodiconiferyl alcohol
CC {ECO:0000269|PubMed:10066819};
CC Vmax=55.8 nmol/h/mg enzyme toward dihydrodehydrodiconiferyl alcohol
CC {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; AF081678; AAC32591.1; -; mRNA.
DR EMBL; AF242490; AAF64173.2; -; mRNA.
DR PDB; 1QYC; X-ray; 2.20 A; A/B=1-308.
DR PDBsum; 1QYC; -.
DR AlphaFoldDB; Q9LL41; -.
DR SMR; Q9LL41; -.
DR EvolutionaryTrace; Q9LL41; -.
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 3D-structure; NADP; Oxidoreductase.
FT CHAIN 1..308
FT /note="Phenylcoumaran benzylic ether reductase PT1"
FT /id="PRO_0000442613"
FT ACT_SITE 134
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:0000305|PubMed:10066819"
FT BINDING 36
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 138
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT CONFLICT 103
FT /note="V -> I (in Ref. 1; AAC32591)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="S -> N (in Ref. 1; AAC32591)"
FT /evidence="ECO:0000305"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1QYC"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:1QYC"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:1QYC"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:1QYC"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:1QYC"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:1QYC"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1QYC"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:1QYC"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1QYC"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1QYC"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1QYC"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:1QYC"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1QYC"
FT HELIX 127..144
FT /evidence="ECO:0007829|PDB:1QYC"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1QYC"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:1QYC"
FT TURN 161..165
FT /evidence="ECO:0007829|PDB:1QYC"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:1QYC"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:1QYC"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:1QYC"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1QYC"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:1QYC"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:1QYC"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1QYC"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:1QYC"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:1QYC"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:1QYC"
FT HELIX 260..271
FT /evidence="ECO:0007829|PDB:1QYC"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:1QYC"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:1QYC"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:1QYC"
FT HELIX 300..305
FT /evidence="ECO:0007829|PDB:1QYC"
SQ SEQUENCE 308 AA; 33524 MW; E93FA4456C7854BF CRC64;
MGSRSRILLI GATGYIGRHV AKASLDLGHP TFLLVRESTA SSNSEKAQLL ESFKASGANI
VHGSIDDHAS LVEAVKNVDV VISTVGSLQI ESQVNIIKAI KEVGTVKRFF PSEFGNDVDN
VHAVEPAKSV FEVKAKVRRA IEAEGIPYTY VSSNCFAGYF LRSLAQAGLT APPRDKVVIL
GDGNARVVFV KEEDIGTFTI KAVDDPRTLN KTLYLRLPAN TLSLNELVAL WEKKIDKTLE
KAYVPEEEVL KLIADTPFPA NISIAISHSI FVKGDQTNFE IGPAGVEASQ LYPDVKYTTV
DEYLSNFV
