ID   T4149_TANPA             Reviewed;         495 AA.
AC   X2ESR4;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   11-JUN-2014, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Cytochrome P450 Tp4149 {ECO:0000312|EMBL:AHM24034.1};
DE            Short=Tp4149 {ECO:0000303|PubMed:24704560};
OS   Tanacetum parthenium (Feverfew) (Matricaria parthenium).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC   Anthemidinae; Tanacetum.
OX   NCBI_TaxID=127999;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=24704560; DOI=10.1016/j.ymben.2014.03.005;
RA   Liu Q., Manzano D., Tanic N., Pesic M., Bankovic J., Pateraki I.,
RA   Ricard L., Ferrer A., de Vos R., van de Krol S., Bouwmeester H.;
RT   "Elucidation and in planta reconstitution of the parthenolide biosynthetic
RT   pathway.";
RL   Metab. Eng. 23C:145-153(2014).
RN   [2]
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: Probably involved in the biosynthesis of germacrene-derived
CC       sesquiterpene lactones. {ECO:0000303|PubMed:24704560}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000303|PubMed:30468448}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DEVELOPMENTAL STAGE: During ovary development, accumulates until the
CC       stage 3 and fades out progressively to disappear at stage 6.
CC       {ECO:0000269|PubMed:24704560}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KC954156; AHM24034.1; -; mRNA.
DR   AlphaFoldDB; X2ESR4; -.
DR   SMR; X2ESR4; -.
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:0051762; P:sesquiterpene biosynthetic process; IEA:UniProt.
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   2: Evidence at transcript level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..495
FT                   /note="Cytochrome P450 Tp4149"
FT                   /id="PRO_0000448401"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
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:P04798"
FT   CARBOHYD        419
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   495 AA;  55480 MW;  FFABACC6D63AF595 CRC64;
     MANILSLETL LISWLSSFIL MFFILKWVSF YSKTKKNLPP SPQKLPIIGN FHQLGPNPHR
     SLQALSEKHG PIMLLHLGSV PMLVASNSEV AQEIMKTHDV SFASRPNSPI LNILLYGCKD
     IAFAPSGEYW RQLKSIIVSN LLSSTQVKSF KNVREKEIGH MIGVIGESYG SSVDMSALLV
     SLAENVICTV ALGRKFDGLK LTSLLRRYLS MFNLFSVGSY IPWLSWVDQL SGLTGRATKV
     VKEFDEFLEV IIEDHANAKI NGGKDFIDML LNAQQDQTTG FAFQRDTIKA VIFDIFGGGI
     DSVSTSIDWV MSELVKHPNV MKKLQKEVTE ISQGRSMVAE EDLEKMQYLK AVIKESWRLH
     PPVPLLIPRK STNDVKLMGY DIQAGTQVMV NVWQIGRDPT LWDEPNEFRP ERFSKGSVNY
     SGLNFEWLPF GVGRRACPGT QFGAAVIELA IANIVYKFDL ALPNGVKHED LDMSEKYGIT
     VHRKNPLLVT ASPRF