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