C76K1_SALMI
ID C76K1_SALMI Reviewed; 503 AA.
AC A0A125QZE2;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=11-hydroxysugiol 20-monooxygenase {ECO:0000305};
DE EC=1.14.14.67 {ECO:0000269|PubMed:26682704};
DE AltName: Full=Cytochrome P450 76AK1 {ECO:0000303|PubMed:26682704};
GN Name=CYP76AK1 {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 11-hydroxysugiol to produce
CC 11,20-dihydroxysugiol (PubMed:26682704). Can oxidize 11-
CC hydroxyferruginol to produce 11,20-dihydroxyferruginol
CC (PubMed:26682704). These products are intermediates in tanshinone
CC biosynthesis (PubMed:26682704). {ECO:0000269|PubMed:26682704}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-hydroxysugiol + O2 + reduced [NADPH--hemoprotein reductase]
CC = 11,20-dihydroxysugiol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:55464, 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:138962,
CC ChEBI:CHEBI:138963; EC=1.14.14.67;
CC Evidence={ECO:0000269|PubMed:26682704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55465;
CC Evidence={ECO:0000269|PubMed:26682704};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-hydroxyferruginol + O2 + reduced [NADPH--hemoprotein
CC reductase] = 11,20-dihydroxyferruginol + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55468, 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:138942, ChEBI:CHEBI:138965;
CC EC=1.14.14.67; Evidence={ECO:0000269|PubMed:26682704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55469;
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: Highly expressed in roots.
CC {ECO:0000269|PubMed:26682704}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KR140169; AMB36497.1; -; mRNA.
DR AlphaFoldDB; A0A125QZE2; -.
DR SMR; A0A125QZE2; -.
DR KEGG; ag:AMB36497; -.
DR BRENDA; 1.14.14.67; 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..503
FT /note="11-hydroxysugiol 20-monooxygenase"
FT /id="PRO_0000452247"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 446
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 503 AA; 56234 MW; 6BABC0BD95567881 CRC64;
MQVLIVASLA FLAAWLVYSR WSDSRRRRGG GGSLPPGPPR LPIIGNMHQL GPNPHKSLAH
LAKTYGPLMS LKLGNQLAVV ASSPEMAREV LIKQGVALCR PFTPNAVCIH GHGEVSVLML
PATSNIWKRI RRIAREKLFS NPALQGTQDI RRERLRKLTD YAAGCSREGR AMNVGEATFT
TMSNLMFATL FSIELTEYGA SDAGANRKFR EHVNAITTNM GVPNVADFFP IFAPLDPQGL
RRKLTHHLGS LLELVQNLID QRLQARDSSD YRKKKDFLDT LLDLSQGNEY DLSIKEIKHF
FVDIIIAGSD TSAATAEWGM VELLLHPDKL EKLKAEMKSV VGEKSIVEES DIARLPYLRA
TVNEVFRLHP AAPLLAPHVA EEEARVNEYI IPKDTKVFVN VWAITRDPSI WKNPDSFEPE
RFLESDINFE GQHFELIPFG SGRRSCPGIP LASRMLHCMV GTLCHNFDWE LEKGAESKQL
QRQDVFGLAL QKKVPLKAIP VKV
