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TP7_TOBAC
ID   TP7_TOBAC               Reviewed;         308 AA.
AC   B6VRE8;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Phenylcoumaran benzylic ether reductase TP7 {ECO:0000305};
DE            Short=NtPCBER {ECO:0000305};
DE            EC=1.23.1.- {ECO:0000269|PubMed:12369619};
DE   AltName: Full=Protein TOBACCO PETAL 7 {ECO:0000305};
GN   Name=TP7 {ECO:0000303|PubMed:12369619};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Petit Havana SR1;
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).
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: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: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: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: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:12369619};
CC   -!- TISSUE SPECIFICITY: Expressed in flowers. Expressed at low levels in
CC       stems. {ECO:0000269|PubMed:12369619}.
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC       reductase subfamily. {ECO:0000305}.
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DR   EMBL; AB445398; BAG84267.1; -; mRNA.
DR   RefSeq; NP_001313018.1; NM_001326089.1.
DR   AlphaFoldDB; B6VRE8; -.
DR   SMR; B6VRE8; -.
DR   GeneID; 107822129; -.
DR   KEGG; nta:107822129; -.
DR   OMA; PIPINIM; -.
DR   OrthoDB; 936727at2759; -.
DR   PhylomeDB; B6VRE8; -.
DR   Proteomes; UP000084051; Unplaced.
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 TP7"
FT                   /id="PRO_0000442617"
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"
SQ   SEQUENCE   308 AA;  34005 MW;  F84DFC3C05FEBA89 CRC64;
     MAEKSKVLII GGTGYIGKFV VEASAKSGHP TFALVRESTL SDPVKSKIVE NFKNLGVTIL
     HGDLYDHESL VKAIKQVDVV ISTMGMMQLG DQVKLIAAIK EAGNIKRFFP SEFGMDVDKT
     NAVEPAKSAF AVKVQIRRAI EAEGIPYTYV SCNCFAGYFL PTMVQPGATV PPRDKVIIPG
     DGNVKAVFNE EHDIGTYTIK AVDDPRTLNK TLYIKPPKNT LSFNELVAMW EKMIGKTLEK
     IYIPEEQILK DIETSPMPLP VILAINHATF VKGDQTNFKI EPSFGVEASE LYPDVKYTTV
     EDYLGHFV
 
 
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