C76H2_SALPM
ID C76H2_SALPM Reviewed; 453 AA.
AC A0A0S1TP26;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Ferruginol synthase {ECO:0000305};
DE EC=1.14.14.175 {ECO:0000269|PubMed:26976595};
DE AltName: Full=11-oxomiltiradiene synthase {ECO:0000305};
DE EC=1.14.14.- {ECO:0000269|PubMed:26976595};
DE AltName: Full=Cytochrome P450 76AH24 {ECO:0000303|PubMed:26572682};
DE Short=SpCYP76AH24 {ECO:0000303|PubMed:26572682};
DE AltName: Full=Ferruginol monooxygenase {ECO:0000250|UniProtKB:A0A0C5QRZ2};
DE Short=11-hydroxyferruginol synthase {ECO:0000250|UniProtKB:A0A0C5QRZ2};
DE EC=1.14.14.60 {ECO:0000250|UniProtKB:A0A0C5QRZ2};
DE Flags: Fragment;
GN Name=CYP76AH24 {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 abietatriene to produce ferruginol (PubMed:26976595). Ferruginol is
CC an intermediate in the biosynthesis of carnosate, a potent antioxidant
CC (PubMed:26976595). May also convert miltiradiene into 11-
CC oxomiltiradiene (PubMed:26976595). {ECO:0000269|PubMed:26976595}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=abieta-8,11,13-triene + O2 + reduced [NADPH--hemoprotein
CC reductase] = ferruginol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:48080, 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:86062; EC=1.14.14.175;
CC Evidence={ECO:0000269|PubMed:26976595};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48081;
CC Evidence={ECO:0000269|PubMed:26976595};
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:0000250|UniProtKB:A0A0C5QRZ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55429;
CC Evidence={ECO:0000250|UniProtKB:A0A0C5QRZ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=miltiradiene + 2 O2 + 2 reduced [NADPH--hemoprotein reductase]
CC = 11-oxomiltiradiene + 2 H(+) + 3 H2O + 2 oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:66796, 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:65037, ChEBI:CHEBI:167496;
CC Evidence={ECO:0000269|PubMed:26976595};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66797;
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:26572682}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KT157044; ALM25796.1; -; mRNA.
DR AlphaFoldDB; A0A0S1TP26; -.
DR SMR; A0A0S1TP26; -.
DR KEGG; ag:ALM25796; -.
DR BioCyc; MetaCyc:MON-21175; -.
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..453
FT /note="Ferruginol synthase"
FT /id="PRO_0000452575"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 397
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"
FT NON_TER 1
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 51265 MW; 25D6F5BE78002BCC CRC64;
MLQLGSQPHE TFAKLSKKYG PLMSIHLGSL YTVIVSSPEM AKEIMHKYGQ VFSGRTIAQA
VHACDHDKIS MGFLPVGAEW RDMRKICKEQ MFSHQSMEDS QNLRKQKLQQ LLDYTQKCSE
EGRGIDIREA AFITTLNLMS ATLFSMQATE FDSKVTMEFK EIIEGVASIV GVPNFADYFP
ILRPFDPQGV KRRADVYFGR LLGLIEGYLN ERIEFRKANP NAPKKDDFLE TLVDALDAKD
YKLKTEHLTH LMLDLFVGGS ETSTTEIEWI MWELVASPEK MAKVKAELKS VMGGEKVVDE
SMMPRLPYLQ AVVKESMRLH PPGPLLLPRK AESDQVVNGY LIPKGTQVLI NAWAMGRDSS
LWKNPDSFEP ERFLDQKIDF KGTDYELIPF GSGRRVCPGM PLANRILHTV TATLVHNFDW
KLERPEANDA HKGVLFGFAV RRAVPLKIVP IKA
