C71BE_SALPM
ID C71BE_SALPM Reviewed; 499 AA.
AC A0A0S1TQ04;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Salviol synthase {ECO:0000305};
DE EC=1.14.14.62 {ECO:0000269|PubMed:26976595};
DE AltName: Full=Cytochrome P450 71BE52 {ECO:0000303|PubMed:26572682};
DE Short=SpCYP71BE52 {ECO:0000303|PubMed:26572682};
GN Name=CYP71BE52 {ECO:0000303|PubMed:26572682};
OS Salvia pomifera (Apple 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=396869;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Trichome gland;
RX PubMed=26572682; DOI=10.1186/s12864-015-2147-3;
RA Trikka F.A., Nikolaidis A., Ignea C., Tsaballa A., Tziveleka L.A.,
RA Ioannou E., Roussis V., Stea E.A., Bozic D., Argiriou A., Kanellis A.K.,
RA Kampranis S.C., Makris A.M.;
RT "Combined metabolome and transcriptome profiling provides new insights into
RT diterpene biosynthesis in S. pomifera glandular trichomes.";
RL BMC Genomics 16:935-935(2015).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26976595; DOI=10.1073/pnas.1523787113;
RA Ignea C., Athanasakoglou A., Ioannou E., Georgantea P., Trikka F.A.,
RA Loupassaki S., Roussis V., Makris A.M., Kampranis S.C.;
RT "Carnosic acid biosynthesis elucidated by a synthetic biology platform.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:3681-3686(2016).
RN [3]
RP PATHWAY, AND REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
CC -!- FUNCTION: Monooxygenase involved in the biosynthesis of labdane-related
CC diterpenes natural products (PubMed:26976595). Catalyzes the oxidation
CC of ferruginol to produce salviol (PubMed:26976595). Salviol is an
CC intermediate in the biosynthesis of carnosate, a potent antioxidant
CC (PubMed:26976595). {ECO:0000269|PubMed:26976595}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ferruginol + O2 + reduced [NADPH--hemoprotein reductase] =
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + salviol;
CC Xref=Rhea:RHEA:55436, 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:138944; EC=1.14.14.62;
CC Evidence={ECO:0000269|PubMed:26976595};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55437;
CC Evidence={ECO:0000269|PubMed:26976595};
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|PubMed:30468448}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf glandular trichomes.
CC {ECO:0000269|PubMed:26976595}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KT157042; ALM25794.1; -; mRNA.
DR AlphaFoldDB; A0A0S1TQ04; -.
DR SMR; A0A0S1TQ04; -.
DR KEGG; ag:ALM25794; -.
DR BioCyc; MetaCyc:MON-21174; -.
DR BRENDA; 1.14.14.62; 15442.
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:0016102; P:diterpenoid 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..499
FT /note="Salviol synthase"
FT /id="PRO_0000452576"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 436
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 499 AA; 56571 MW; 987D61ECA35F1495 CRC64;
MEIHIPSLVL CISFFIFFKI VSKLKTKTSN RKHLPLPPGP WKLPLIGNLH NLVGALPHHT
LRRLSRKFGP MMSLQLGELS AVIISSADAA KEIMKTHDLN FASRPQVAAA DIIGYGSTNI
TFSPYGGHWR QLRKICTLEL LSAKRVQSFR PLRERVFVDL CRRFADHGSS AVNFSEEFMS
ATYTLISRAV LGEEAEQHEG LLPNVKEMPE LTAGFDISEV FPSVGLFKVM SRLRKRIVAV
HKDTDRILDD VIHQHRAAKS EEHKDLLDVL LQLQEDGLEL PLTDENIKSV LVDMLVAGSE
TSSTVIEWAM AEMLKNPRIL EKAQEEVRRV FDKEGTVDES HIHELKYLKS VVKETLRVHP
PAPLILPRIC GETCEINGYE IPAETKIIVN AWAVNRDPKY WEDSDCFKPE RFLDNLVDFR
GNHFQYIPFG AGRRMCPGIG FGLANVELPL AMFMYHFDWE LDGGMKPQDL DMEEKFGASA
KKLKDLFLIP AIKRTLPTK
