ID   C7A94_KALSE             Reviewed;         481 AA.
AC   A0A0S2II38;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Beta-amyrin 28-monooxygenase;
DE            EC=1.14.14.126 {ECO:0000269|PubMed:29186583};
DE   AltName: Full=Cytochrome P450 716A94 {ECO:0000303|PubMed:29186583};
GN   Name=CYP716A94 {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 the methyl group to a carboxyl
CC       group at the C-28 position of beta-amyrin to form oleanolate.
CC       {ECO:0000269|PubMed:29186583}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-amyrin + 3 O2 + 3 reduced [NADPH--hemoprotein reductase]
CC         = 4 H(+) + 4 H2O + oleanolate + 3 oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:43068, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:10352, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:82828; EC=1.14.14.126;
CC         Evidence={ECO:0000269|PubMed:29186583};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43069;
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; KT150521; ALO23117.1; -; mRNA.
DR   AlphaFoldDB; A0A0S2II38; -.
DR   SMR; A0A0S2II38; -.
DR   BRENDA; 1.14.14.126; 15444.
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:0102374; F:ursolic aldehyde 28-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102373; F:uvaol dehydrogenase activity; IEA:UniProtKB-EC.
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..481
FT                   /note="Beta-amyrin 28-monooxygenase"
FT                   /id="PRO_0000452135"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         428
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   481 AA;  54011 MW;  61F89D44893772C4 CRC64;
     MQLFYVPLLS LFVLFVSLSF YFLFYKSKSG STSGLPLPPG KTGWPVIGES FEFLSTGWKG
     YPEKFIFDRL AKYSSNVFKT SLFGQPAAAF CGAACNKFLF SNENKLVQAW WPDSVNKVFP
     SSTQTSSKEE AIKMRKLLPN FLKPEALQRY VGVMDQIATK HFKSGWENKK EVLVFPLAKN
     YTFWIACKVF VSVEEPTQVA KLLEPFNAIA SGIISVPIDL PGTPFNSAIK SSKIVRDKLM
     GIIKQRKTDL GEGKASPTQD ILSHMLLTSD ENGKFMTEGD IADKILGLLI GGHDTASSAC
     TFVVKFLAEL PEIYEGVYKE QMEIAKSKKA GELLNWEDIQ KMKYSWNVAC EVLRLAPPLQ
     GAFREALTDF SYNGFSIPKG WKLYWSANST HRNSEVFPEP LKFDPSRFEG AGPPPYSFVP
     FGGGPRMCPG KEYARLEILV FMHHVVKRFK WEKVIPDEKI VVNPMPIPAK GLPVRLFPHK
     A