C76H3_SALMI
ID C76H3_SALMI Reviewed; 494 AA.
AC A0A0Y0GRS3;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Sugiol synthase {ECO:0000305};
DE EC=1.14.14.65 {ECO:0000269|PubMed:26682704};
DE AltName: Full=Cytochrome P450 76AH3 {ECO:0000303|PubMed:26682704};
DE AltName: Full=Ferruginol monooxygenase {ECO:0000305};
DE EC=1.14.14.60 {ECO:0000269|PubMed:26682704};
GN Name=CYP76AH3 {ECO:0000303|PubMed:26682704};
OS Salvia miltiorrhiza (Chinese sage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Salviinae;
OC Salvia; Salvia incertae sedis.
OX NCBI_TaxID=226208;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=26682704; DOI=10.1111/nph.13790;
RA Guo J., Ma X., Cai Y., Ma Y., Zhan Z., Zhou Y.J., Liu W., Guan M., Yang J.,
RA Cui G., Kang L., Yang L., Shen Y., Tang J., Lin H., Ma X., Jin B., Liu Z.,
RA Peters R.J., Zhao Z.K., Huang L.;
RT "Cytochrome P450 promiscuity leads to a bifurcating biosynthetic pathway
RT for tanshinones.";
RL New Phytol. 210:525-534(2016).
CC -!- FUNCTION: Monooxygenase that oxidizes ferruginol to produce sugiol
CC (PubMed:26682704). Oxidizes ferruginol at C-12 to produce 11-
CC hydroxyferruginol (PubMed:26682704). Can oxidize 11-hydroxyferruginol
CC to 11-hydroxysugiol (PubMed:26682704). These products are intermediates
CC in tanshinone biosynthesis (PubMed:26682704).
CC {ECO:0000269|PubMed:26682704}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ferruginol + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] =
CC 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase] + sugiol;
CC Xref=Rhea:RHEA:55456, 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:78274,
CC ChEBI:CHEBI:138961; EC=1.14.14.65;
CC Evidence={ECO:0000269|PubMed:26682704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55457;
CC Evidence={ECO:0000269|PubMed:26682704};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ferruginol + O2 + reduced [NADPH--hemoprotein reductase] = 11-
CC hydroxyferruginol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:55428, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78274,
CC ChEBI:CHEBI:138942; EC=1.14.14.60;
CC Evidence={ECO:0000269|PubMed:26682704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55429;
CC Evidence={ECO:0000269|PubMed:26682704};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-hydroxyferruginol + 2 O2 + 2 reduced [NADPH--hemoprotein
CC reductase] = 11-hydroxysugiol + 2 H(+) + 3 H2O + 2 oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:55460, 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:138942, ChEBI:CHEBI:138962; EC=1.14.14.65;
CC Evidence={ECO:0000269|PubMed:26682704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55461;
CC Evidence={ECO:0000269|PubMed:26682704};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q94IP1};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:26682704}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KR140168; AMB36496.1; -; mRNA.
DR AlphaFoldDB; A0A0Y0GRS3; -.
DR SMR; A0A0Y0GRS3; -.
DR KEGG; ag:AMB36496; -.
DR BRENDA; 1.14.14.60; 9850.
DR BRENDA; 1.14.14.65; 9850.
DR UniPathway; UPA00213; -.
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 GO; GO:0016114; P:terpenoid biosynthetic process; 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 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..494
FT /note="Sugiol synthase"
FT /id="PRO_0000452246"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 437
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:Q94IP1"
SQ SEQUENCE 494 AA; 55757 MW; 33C817438E372DEB CRC64;
MDSFSLLAAL FFISAATWFI SSRRRRNLPP GPFPYPIVGN MLQLGAQPHE TFAKLSKKYG
PLMSVHLGSL YTVIVSSPEM AKEIMLKYGT VFSGRTVAQA VHACDHDKIS MGFLPIGAEW
RDMRKICKEQ MFSHQSMEDS QGLRKQKLQQ LLDHAHRCSE QGRAIDIREA AFITTLNLMS
ATLFSMQATE FDSKVTMEFK EIIEGVASIV GVPNFADYFP ILRPFDPQGV KRRADVYFGR
LLALIEGYLN DRIQSRKANP DAPKKDDFLE TLVDILNSND NKLKTDHLLH LMLDLFVGGS
ETSTTEIEWI MEELVAHPDK MAKVKAELKS VMGDEKVVDE SLMPRLPYLQ AVVKESMRLH
PPGPLLLPRK AESDQVVNGY LIPKGTQVLI NAWAMGRDST IWNNPDAFQP ERFLDNKIDF
KGQDYELIPF GSGRRVCPGM PLANRMLHTV TATLVHNFDW KLERPDAPLA EHQGVLFGFA
VRRAVPLRIV PYKA
