ID   C72A5_BARVU             Reviewed;         513 AA.
AC   A0A481NR20;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-JUN-2019, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Cytochrome P450 72A552 {ECO:0000303|PubMed:30661245};
DE            EC=1.14.14.- {ECO:0000269|PubMed:30661245};
GN   Name=CYP72A552 {ECO:0000303|PubMed:30661245};
OS   Barbarea vulgaris (Yellow rocket) (Erysimum barbarea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Cardamineae; Barbarea.
OX   NCBI_TaxID=50459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=30661245; DOI=10.1111/nph.15689;
RA   Liu Q., Khakimov B., Cardenas P.D., Cozzi F., Olsen C.E., Jensen K.R.,
RA   Hauser T.P., Bak S.;
RT   "The cytochrome P450 CYP72A552 is key to production of hederagenin-based
RT   saponins that mediate plant defense against herbivores.";
RL   New Phytol. 222:1599-1609(2019).
CC   -!- FUNCTION: Catalyzes the oxidation of oleanolate at the C-23 position to
CC       form hederagenin. {ECO:0000269|PubMed:30661245}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + oleanolate + reduced [NADPH--hemoprotein reductase] =
CC         H(+) + H2O + hederagenin + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:56488, 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:82828,
CC         ChEBI:CHEBI:140466; Evidence={ECO:0000269|PubMed:30661245};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56489;
CC         Evidence={ECO:0000269|PubMed:30661245};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q94IP1};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
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; MH252571; QAV52438.1; -; mRNA.
DR   AlphaFoldDB; A0A481NR20; -.
DR   SMR; A0A481NR20; -.
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:0016134; P:saponin metabolic process; IDA:UniProtKB.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
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.
PE   1: Evidence at protein level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..513
FT                   /note="Cytochrome P450 72A552"
FT                   /id="PRO_0000452134"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         460
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   513 AA;  58607 MW;  C3B09261712A8F43 CRC64;
     MEISVASVTV SVVIAVVTWW VWRTLKWVWF QPKMLESYLR RQGLSGTPYT PLVGDLKRNS
     KMLTEAISKP IRLNDDITQR VVPYPLQMLK TYGRTHFTWL GPIPAITIMD PELIKEVFNR
     VYDFQKARLF PLARLIATGL VRYDGDKWAK HRKIINPAFH LEKLKNMVPA FHQCCSEVVG
     AWDKLVSDKR SSCEVDVWPG LVSMTADMIS RTAFGSSYKE GQRIFELQEE IKELLIQSLG
     KAFIPGYHYL PTKGNRRMKA ADREIKVILR GIVNKRLRAR EAGEAPSEDL LGILLESNLG
     QAKGNGMSIE DVMEECKLFY LAGQETTSVL LVWTMVMLSQ HQDWQARARE EVKQVFGDKE
     PNTEGLNQLK VMTMILYEVL RLYPPVTQLP RAIHKEMKLG DMTLPAGVHI NLPIMLVQRD
     TELWGNDAAE FKPERFKDGL SKAAKNQVSF FSFAWGPRIC IGQNFALMEA KMAMALILQR
     FSLELSPSYV HAPYSVITLH PQFGAHLILH KLY