C81Q2_SESRA
ID C81Q2_SESRA Reviewed; 506 AA.
AC Q33DX9;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=(+)-piperitol/(+)-sesamin synthase CYP81Q2 {ECO:0000305};
DE EC=1.14.19.74 {ECO:0000269|PubMed:16785429};
DE AltName: Full=Cytochrome P450 81Q2 {ECO:0000303|PubMed:16785429};
DE AltName: Full=Piperitol synthase CYP81Q2 {ECO:0000305};
DE AltName: Full=Sesamin synthase CYP81Q2 {ECO:0000305};
GN Name=CYP81Q2 {ECO:0000303|PubMed:16785429};
OS Sesamum radiatum (Black benniseed).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Pedaliaceae; Sesamum.
OX NCBI_TaxID=300843;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=16785429; DOI=10.1073/pnas.0603865103;
RA Ono E., Nakai M., Fukui Y., Tomimori N., Fukuchi-Mizutani M., Saito M.,
RA Satake H., Tanaka T., Katsuta M., Umezawa T., Tanaka Y.;
RT "Formation of two methylenedioxy bridges by a Sesamum CYP81Q protein
RT yielding a furofuran lignan, (+)-sesamin.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10116-10121(2006).
CC -!- FUNCTION: Involved in the biosynthesis of (+)-sesamin, a furofuran
CC class lignan (PubMed:16785429). Functions in a dual catalytic mode
CC (PubMed:16785429). Catalyzes the synthesis of (+)-sesamin from
CC (+)- pinoresinol by formation of two successive methylenedioxy bridges
CC on (+)-pinoresinol and (+)-piperitol, respectively (PubMed:16785429).
CC {ECO:0000269|PubMed:16785429}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-piperitol + O2 + reduced [NADPH--hemoprotein reductase] =
CC (+)-sesamin + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:56780, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:66470,
CC ChEBI:CHEBI:141003; EC=1.14.19.74;
CC Evidence={ECO:0000269|PubMed:16785429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56781;
CC Evidence={ECO:0000269|PubMed:16785429};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-pinoresinol + O2 + reduced [NADPH--hemoprotein reductase]
CC = (+)-piperitol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:56776, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:40, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:141003; EC=1.14.19.74;
CC Evidence={ECO:0000269|PubMed:16785429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56777;
CC Evidence={ECO:0000269|PubMed:16785429};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds. {ECO:0000269|PubMed:16785429}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB194715; BAE48235.1; -; mRNA.
DR KEGG; ag:BAE48235; -.
DR BRENDA; 1.14.19.74; 15770.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..506
FT /note="(+)-piperitol/(+)-sesamin synthase CYP81Q2"
FT /id="PRO_0000455168"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 439
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q96242"
SQ SEQUENCE 506 AA; 57394 MW; 2F6A1614AF1AE1C9 CRC64;
MEAEMLYSAL ALTFAIFMVY RILSNSQEKS SLIKLPPSPP GWLPVIGHVH LMKNLLHRTL
YDFSQKLGPI FSLRFGTRLV VVVSSSSLVE ECFTKYDIVL ANRPQPSVDR RSLGFSTTSV
IGAPYGDHWR NLRKLCDLEV FAPTRLASFL SIRLDERDRM ISSLYKISSA GFAKVNLETK
IVELTFNNIM RMVAGKRYYG EEAEDDEEAK RFRDLTKEAL ELTSASNPGE IFPILRWLGF
NGLEKKLAVH ARKTDEFMQG LLDEHRRGER QNTMVDHLLS LQESQPEYYT DEIITGLIVA
LIIAGTDASV VTTEWAMSLI LNHPQVLEKA RKELDTLVGH ERMVDEHDLP KLRYLHCIVL
ETLRLFPSVP TLVPHEPSED CKIGGYNVPK GTMILVNAWA IHRDPKVWDD PLSFKPDRFE
TMEVETHKLL PFGMGRRACP GAGLAQKFVG LALGSLIQCF EWERMSAEKI DLNEGSGITL
PKAKTLEAMC KPRHIMERVL RQVSNV
