ID   C7A39_KALSE             Reviewed;         520 AA.
AC   A0A0S2IHL2;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=Cytochrome P450 72A397;
DE            EC=1.14.14.- {ECO:0000269|PubMed:29186583};
GN   Name=CYP72A397 {ECO:0000303|PubMed:29186583};
OS   Kalopanax septemlobus (Castor aralia) (Acanthopanax septemlobus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Araliaceae; Kalopanax.
OX   NCBI_TaxID=228393;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=29186583; DOI=10.1093/pcp/pcx188;
RA   Han J.Y., Chun J.H., Oh S.A., Park S.B., Hwang H.S., Lee H., Choi Y.E.;
RT   "Transcriptomic analysis of Kalopanax septemlobus and characterization of
RT   KsBAS, CYP716A94 and CYP72A397 genes involved in hederagenin saponin
RT   biosynthesis.";
RL   Plant Cell Physiol. 59:319-330(2018).
CC   -!- FUNCTION: Catalyzes the oxidation of oleanolate at the C-23 position to
CC       form hederagenin. {ECO:0000269|PubMed:29186583}.
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:29186583};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56489;
CC         Evidence={ECO:0000269|PubMed:29186583};
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}.
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DR   EMBL; KT150517; ALO23113.1; -; mRNA.
DR   AlphaFoldDB; A0A0S2IHL2; -.
DR   SMR; A0A0S2IHL2; -.
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; 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..520
FT                   /note="Cytochrome P450 72A397"
FT                   /id="PRO_0000452136"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         468
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   520 AA;  59385 MW;  4A730850AA12485B CRC64;
     MDGVVVTYTK IAAAVAVAVV VVGWAWKVLN WVWVSPRKLE ESLRKQGFRG NSYRLFYGDL
     KESSEMTRKA KLKPINLSDD PVLRVRPFIH QTVKKYGKSS FIWIGPTPRV QIMDPEIIKE
     IMVKSYKFNK PKRNPLVKLF ADGLANHEGE LWAKHRKLLN PAFHLERLKC MLPAMYFSCI
     EMVSKWDKMI SKDGSRELDV WPFLQRLTSD VISHTAFGSS YEEGNIVFEL QTEQAELVMK
     TLQSVYIPGW SYLPTKRNRK MKEIDRKTQS CLMNIINKKT KAMQAGEGST DDILGILLES
     NLKEQLGQGK KNVGMSIQEV MGECKQFYFA GQETTSGLLV WTMVLLSIHP NWQARAREEV
     LQQFGNAKPD FDNLNHLKIV TMILYEVLRL YPPVDTLFRR VDQETTLGDI TLPAGVQISL
     PIMILHHDQN IWGDDAKEFN PERFSEGVSK ATKNQVVFFP FGWGPRICIG QNFALLEAKL
     ALAIILQRFS FELSPSYTHA PTTVLTVQPQ HGANLILHKL