C87DR_SIRGR
ID C87DR_SIRGR Reviewed; 473 AA.
AC K7NBR2; G1DGI4;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Cucurbitadienol 11-hydroxylase {ECO:0000305};
DE EC=1.14.14.71 {ECO:0000269|PubMed:26903528};
DE AltName: Full=Cytochrome P450 87D18 {ECO:0000303|PubMed:26903528};
GN Name=CYP87D18 {ECO:0000303|PubMed:26903528};
GN Synonyms=P450-5 {ECO:0000312|EMBL:AEM42986.1};
OS Siraitia grosvenorii (Monk's fruit) (Luo han guo).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Siraitieae; Siraitia.
OX NCBI_TaxID=190515;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tang Q., Ma X.J., Zhao H., Mo C.M.;
RT "Cloning of genes related to mogrosides biosynthesis in Siraitia
RT grosvenorii.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-444.
RX PubMed=21729270; DOI=10.1186/1471-2164-12-343;
RA Tang Q., Ma X.J., Mo C.M., Wilson I.W., Song C., Zhao H., Yang Y.F., Fu W.,
RA Qiu D.Y.;
RT "An efficient approach to finding Siraitia grosvenorii triterpene
RT biosynthetic genes by RNA-seq and digital gene expression analysis.";
RL BMC Genomics 12:343-343(2011).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26903528; DOI=10.1093/pcp/pcw038;
RA Zhang J., Dai L., Yang J., Liu C., Men Y., Zeng Y., Cai Y., Zhu Y., Sun Y.;
RT "Oxidation of cucurbitadienol catalyzed by CYP87D18 in the biosynthesis of
RT mogrosides from Siraitia grosvenorii.";
RL Plant Cell Physiol. 57:1000-1007(2016).
CC -!- FUNCTION: Catalyzes the oxidation of cucurbitadienol at the C-11
CC position to produce 11-oxo cucurbitadienol, a possible biosynthetic
CC intermediate from cucurbitadienol to mogrol.
CC {ECO:0000269|PubMed:26903528}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cucurbitadienol + 2 O2 + 2 reduced [NADPH--hemoprotein
CC reductase] = 11-oxocucurbitadienol + 2 H(+) + 3 H2O + 2 oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55508, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:62456, ChEBI:CHEBI:138973;
CC EC=1.14.14.71; Evidence={ECO:0000269|PubMed:26903528};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55509;
CC Evidence={ECO:0000269|PubMed:26903528};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cucurbitadienol + O2 + reduced [NADPH--hemoprotein reductase]
CC = 11-hydroxycucurbitadienol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:55512, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:62456, ChEBI:CHEBI:138972;
CC Evidence={ECO:0000269|PubMed:26903528};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55513;
CC Evidence={ECO:0000269|PubMed:26903528};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-hydroxycucurbitadienol + O2 + reduced [NADPH--hemoprotein
CC reductase] = 11-oxocucurbitadienol + H(+) + 2 H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:55516, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:138972, ChEBI:CHEBI:138973;
CC Evidence={ECO:0000269|PubMed:26903528};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55517;
CC Evidence={ECO:0000269|PubMed:26903528};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q93VK5};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HQ128571; AEM42986.1; -; mRNA.
DR EMBL; JL554667; AEG64830.1; -; mRNA.
DR AlphaFoldDB; K7NBR2; -.
DR SMR; K7NBR2; -.
DR KEGG; ag:AEM42986; -.
DR BioCyc; MetaCyc:MON-21295; -.
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:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
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 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..473
FT /note="Cucurbitadienol 11-hydroxylase"
FT /id="PRO_0000451487"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 422
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:Q93VK5"
SQ SEQUENCE 473 AA; 53883 MW; A7C122474F66F641 CRC64;
MWTVVLGLAT LFVAYYIHWI NKWRDSKFNG VLPPGTMGLP LIGETIQLSR PSDSLDVHPF
IQKKVERYGP IFKTCLAGRP VVVSADAEFN NYIMLQEGRA VEMWYLDTLS KFFGLDTEWL
KALGLIHKYI RSITLNHFGA EALRERFLPF IEASSMEALH SWSTQPSVEV KNASALMVFR
TSVNKMFGED AKKLSGNIPG KFTKLLGGFL SLPLNFPGTT YHKCLKDMKE IQKKLREVVD
DRLANVGPDV EDFLGQALKD KESEKFISEE FIIQLLFSIS FASFESISTT LTLILKLLDE
HPEVVKELEA EHEAIRKARA DPDGPITWEE YKSMTFTLQV INETLRLGSV TPALLRKTVK
DLQVKGYIIP EGWTIMLVTA SRHRDPKVYK DPHIFNPWRW KDLDSITIQK NFMPFGGGLR
HCAGAEYSKV YLCTFLHILC TKYRWTKLGG GTIARAHILS FEDGLHVKFT PKE
