C7AV8_CICIN
ID C7AV8_CICIN Reviewed; 496 AA.
AC E1B2Z9;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Cytochrome P450 71AV8;
DE AltName: Full=(+)-Valencene oxidase;
DE EC=1.14.13.-;
GN Name=CYP71AV8;
OS Cichorium intybus (Chicory).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Cichoriinae; Cichorium.
OX NCBI_TaxID=13427;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=21115006; DOI=10.1016/j.febslet.2010.11.040;
RA Cankar K., Houwelingen A., Bosch D., Sonke T., Bouwmeester H.,
RA Beekwilder J.;
RT "A chicory cytochrome P450 mono-oxygenase CYP71AV8 for the oxidation of
RT (+)-valencene.";
RL FEBS Lett. 585:178-182(2011).
CC -!- FUNCTION: Valencene oxidase, which preferentially hydroylates the C2
CC position of (+)-valencene in the trans-orientation, producing trans-
CC nootkatol that can be further oxidized to (+)-nootkatone. Can also
CC catalyze the three-step conversion of germacrene A to germacra-
CC 1(10),4,11(13)-trien-12-oic acid and the partial conversion of the non-
CC natural substrate amorpha-4,11-diene into artemisinic alcohol and
CC artemisinic aldehyde.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
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; HQ166835; ADM86719.1; -; mRNA.
DR AlphaFoldDB; E1B2Z9; -.
DR SMR; E1B2Z9; -.
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:1901576; P:organic substance biosynthetic process; IEA:UniProt.
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 Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..496
FT /note="Cytochrome P450 71AV8"
FT /id="PRO_0000421933"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 432
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"
SQ SEQUENCE 496 AA; 56135 MW; 5153D5A9FEB5E8DE CRC64;
MEISIPTTLG LAVIIFIIFK LLTRTTSKKN LLPEPWRLPI IGHMHHLIGT MPHRGVMELA
RKHGSLMHLQ LGEVSTIVVS SPRWAKEVLT TYDITFANRP ETLTGEIVAY HNTDIVLAPY
GEYWRQLRKL CTLELLSNKK VKSFQSLREE ECWNLVKDIR STGQGSPINL SENIFKMIAT
ILSRAAFGKG IKDQMKFTEL VKEILRLTGG FDVADIFPSK KLLHHLSGKR AKLTNIHNKL
DNLINNIIAE HPGNRTSSSQ ETLLDVLLRL KESAEFPLTA DNVKAVILDM FGAGTDTSSA
TIEWAISELI RCPRAMEKVQ TELRQALNGK ERIQEEDLQE LNYLKLVIKE TLRLHPPLPL
VMPRECREPC VLGGYDIPSK TKLIVNVFAI NRDPEYWKDA ETFMPERFEN SPITVMGSEY
EYLPFGAGRR MCPGAALGLA NVELPLAHIL YYFNWKLPNG KTFEDLDMTE SFGATVQRKT
ELLLVPTDFQ TLTAST
