ID   C7A81_BARVU             Reviewed;         475 AA.
AC   A0A0U2U8U5;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   16-MAR-2016, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=Beta-amyrin 28-monooxygenase {ECO:0000305};
DE            EC=1.14.14.126 {ECO:0000269|PubMed:26333142, ECO:0000269|PubMed:29603041};
DE   AltName: Full=Cytochrome P450 716A81 {ECO:0000303|PubMed:26333142};
DE            Short=BvCYP716A81 {ECO:0000303|PubMed:29603041};
GN   Name=CYP716A81 {ECO:0000303|PubMed:26333142};
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=26333142; DOI=10.1111/tpj.13012;
RA   Khakimov B., Kuzina V., Erthmann P.O., Fukushima E.O., Augustin J.M.,
RA   Olsen C.E., Scholtalbers J., Volpin H., Andersen S.B., Hauser T.P.,
RA   Muranaka T., Bak S.;
RT   "Identification and genome organization of saponin pathway genes from a
RT   wild crucifer, and their use for transient production of saponins in
RT   Nicotiana benthamiana.";
RL   Plant J. 84:478-490(2015).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=29603041; DOI=10.1007/s11103-018-0723-z;
RA   Erthmann P.O., Agerbirk N., Bak S.;
RT   "A tandem array of UDP-glycosyltransferases from the UGT73C subfamily
RT   glycosylate sapogenins, forming a spectrum of mono- and bisdesmosidic
RT   saponins.";
RL   Plant Mol. Biol. 97:37-55(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:26333142, ECO:0000269|PubMed:29603041}.
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:26333142, ECO:0000269|PubMed:29603041};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43069;
CC         Evidence={ECO:0000269|PubMed:26333142, ECO:0000269|PubMed:29603041};
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; KP795925; ALR73781.1; -; mRNA.
DR   AlphaFoldDB; A0A0U2U8U5; -.
DR   SMR; A0A0U2U8U5; -.
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..475
FT                   /note="Beta-amyrin 28-monooxygenase"
FT                   /id="PRO_0000452133"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         422
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   475 AA;  54966 MW;  98AEAC695344E747 CRC64;
     MYLTILFLFV SSILLSLMFL LRKHLSHFSY QNLPPGKTGF PLIGESLSFL SEGRQGRPEK
     FVTDRVRRFI SSSTGVFKTH LFGYPTAVMT GASGNKFLFT NENKLVVSWW PDSVKKIFPY
     TQSTYTDESK KLRILLMQFM KPEALRKYIG VMDEVAQRHF ETLWTNQKQL IVYPLSKKLT
     FSVACRLFLS MDDPERVSKL EDRFNSVVTG IYSVPIDLPG TRFNRSIKAS RLLRKEVCAI
     IGQRREELKA GRASAEQDVL SHMLMSVGET KDEDLANYLI GILIGGHDTA AIATTFIINY
     LAEYPHVYQR VLQEQKEILK EKKEEERLKW EDIEKMKYSW NVACEVMRLV PPLTGNFREA
     IDHFTFKGFY IPKGWKLYWS ATATHMNPDY FPEPERFEPN RFEGSGPKPY SYIPFGGGPR
     MCPGREFARL EILVIIHNLV NRFKWEKVFP NENKIVVDPL PKPGNGLPIR IFPHF