CP182_THYVU
ID CP182_THYVU Reviewed; 496 AA.
AC A0A159AKG3;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Cytochrome P450 71D182 {ECO:0000303|Ref.1};
DE AltName: Full=Gamma-terpinene hydroxylase {ECO:0000305|Ref.1};
DE AltName: Full=Thymol synthase {ECO:0000305|Ref.1};
DE EC=1.14.14.- {ECO:0000303|Ref.1};
GN Name=CYP71D182 {ECO:0000303|Ref.1};
OS Thymus vulgaris (Thyme).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Thymus.
OX NCBI_TaxID=49992;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Tc; TISSUE=Leaf;
RA Crocoll C.;
RT "Biosynthesis of the phenolic monoterpenes, thymol and carvacrol, by
RT terpene synthases and cytochrome P450s in oregano and thyme.";
RL Thesis (2011), Friedrich Schiller University of Jena, Germany.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Rudolph K., Loos S., Ebertsch L., Mueller-Uri F., Kreis W.;
RT "Biosynthetic enzymes in thyme.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP REVIEW ON THYMOL.
RX PubMed=29785774; DOI=10.1002/ptr.6109;
RA Salehi B., Mishra A.P., Shukla I., Sharifi-Rad M., Contreras M.D.M.,
RA Segura-Carretero A., Fathi H., Nasrabadi N.N., Kobarfard F.,
RA Sharifi-Rad J.;
RT "Thymol, thyme, and other plant sources: Health and potential uses.";
RL Phytother. Res. 32:1688-1706(2018).
RN [4]
RP REVIEW ON CARVACROL AND THYMOL.
RX PubMed=29874939; DOI=10.1080/14786419.2018.1480618;
RA Wang K., Jiang S., Yang Y., Fan L., Su F., Ye M.;
RT "Synthesis and antifungal activity of carvacrol and thymol esters with
RT heteroaromatic carboxylic acids.";
RL Nat. Prod. Res. 33:1924-1930(2019).
RN [5]
RP REVIEW ON PLANT ESSENTIAL OILS EFFECTS ON COVID-19, AND BIOTECHNOLOGY.
RX PubMed=32834111; DOI=10.1016/j.molstruc.2020.128823;
RA Kulkarni S.A., Nagarajan S.K., Ramesh V., Palaniyandi V., Selvam S.P.,
RA Madhavan T.;
RT "Computational evaluation of major components from plant essential oils as
RT potent inhibitors of SARS-CoV-2 spike protein.";
RL J. Mol. Struct. 1221:128823-128823(2020).
RN [6]
RP REVIEW ON PLANT ESSENTIAL OILS EFFECTS ON COVID-19, AND BIOTECHNOLOGY.
RX PubMed=33855010; DOI=10.3389/fchem.2021.642026;
RA Yadalam P.K., Varatharajan K., Rajapandian K., Chopra P., Arumuganainar D.,
RA Nagarathnam T., Sohn H., Madhavan T.;
RT "Antiviral essential oil components against SARS-CoV-2 in pre-procedural
RT mouth rinses for dental settings during COVID-19: A computational study.";
RL Front. Chem. 9:642026-642026(2021).
CC -!- FUNCTION: Involved in the biosynthesis of phenolic monoterpene natural
CC product thymol which has a broad range of biological activities acting
CC as antimicrobial compound, insecticide, antioxidant and pharmaceutical
CC agent (Ref.1). Catalyzes probably the C3-hydroxylation of gamma-
CC terpinene to produce thymol (Ref.1). {ECO:0000303|Ref.1}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000303|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- BIOTECHNOLOGY: The monoterpenic phenol thymol is widely used as a
CC fragrance and a flavoring ingredient in food and cosmetic industries
CC (PubMed:29785774). Its derivatives have also several biological and
CC pharmacological properties such as antimicrobial, antioxidant,
CC anticarcinogenesis, anti-inflammatory and antispasmodic activities
CC (PubMed:29785774, PubMed:29874939). Medical applications include the
CC treatment of disorders affecting the respiratory, nervous, and
CC cardiovascular systems (PubMed:29785774). It may also act as a growth
CC enhancer and immunomodulator (PubMed:29785774). Thymol may also have
CC antiviral activity toward COVID-19 by binding to the S1 receptor
CC binding domain of the SARS-CoV-2 spike (S) glycoprotein
CC (PubMed:32834111, PubMed:33855010). {ECO:0000303|PubMed:29785774,
CC ECO:0000303|PubMed:29874939, ECO:0000303|PubMed:32834111,
CC ECO:0000303|PubMed:33855010}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KM272331; AKF17614.1; -; mRNA.
DR SMR; A0A159AKG3; -.
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:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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 Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..496
FT /note="Cytochrome P450 71D182"
FT /id="PRO_0000453330"
FT TRANSMEM 1..21
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT BINDING 435
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:Q96242"
FT CONFLICT 1..4
FT /note="MDIS -> MELMDVK (in Ref. 2; AKF17614)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="W -> L (in Ref. 2; AKF17614)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="T -> S (in Ref. 2; AKF17614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 496 AA; 56293 MW; 7918740B04562736 CRC64;
MDISISWVVI IVSVLSYLIL MDKWRAAKLP KNIPPGPPKL PLIGHLHLLR GGLPQHLLRG
ITQKYGPVAH VQLGELFSVV LSSTEAARQA MKVLDPNFAD RFVNIGSRIM WYDSEDIIFS
RYNDHWRQIR KICVSELLSP KNVRSFGYIR QDEMARLIRL FESSEGKPVN VSEEISKTVC
TIVSRVAFGS AVKDQSLLMN LVKESLRMAS GFELADVFPS SWLLNLLCFN KYRLWRMRAR
LDKFLDGFLA EHRVKKSGEF GGEDIIDVLY RMQEDSETKV PITNNGIKGF IYDVFSAGTD
TSGATILWAL SELMRYPEKM AKAQAEVRET LKGKTNVDMA EVHELKYLRS VVKEALRLHP
PFPMIPRLCV QESEVTGYTI PANTRILINV WSIGRDPLYW EDPDTFNPDR YDEVPRDIIG
NDFELIPFGS GRRICPGLHF GLANIEVPLA QLLYHFDWKL PPGMTAADID MTEKTGLSGP
RKNPLILVPI IHNPTS
