ID   C7263_MEDTR             Reviewed;         524 AA.
AC   H1A981;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=11-oxo-beta-amyrin 30-oxidase;
DE            EC=1.14.14.115 {ECO:0000269|PubMed:22128119};
DE   AltName: Full=Cytochrome P450 72A63;
GN   Name=CYP72A63;
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND INDUCTION BY SALT.
RX   PubMed=22128119; DOI=10.1105/tpc.110.082685;
RA   Seki H., Sawai S., Ohyama K., Mizutani M., Ohnishi T., Sudo H.,
RA   Fukushima E.O., Akashi T., Aoki T., Saito K., Muranaka T.;
RT   "Triterpene functional genomics in licorice for identification of CYP72A154
RT   involved in the biosynthesis of glycyrrhizin.";
RL   Plant Cell 23:4112-4123(2011).
CC   -!- FUNCTION: Involved in the biosynthesis of triterpenoid saponins.
CC       Catalyzes three sequential oxidation steps at C-30 of 11-oxo-beta-
CC       amyrin. Also able to catalyze sequential C-30 hydroxylation of beta-
CC       amyrin to produce 30-hydroxy-beta-amyrin and 11-deoxoglycyrrhetinic
CC       acid. {ECO:0000269|PubMed:22128119}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=11-oxo-beta-amyrin + 3 O2 + 3 reduced [NADPH--hemoprotein
CC         reductase] = glycyrrhetinate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:35499, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17573, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:63184; EC=1.14.14.115;
CC         Evidence={ECO:0000269|PubMed:22128119};
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   -!- TISSUE SPECIFICITY: Expressed in flowers. Detected in roots upon salt
CC       treatment. {ECO:0000269|PubMed:22128119}.
CC   -!- INDUCTION: Up-regulated in roots by salt treatment.
CC       {ECO:0000269|PubMed:22128119}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB558146; BAL45200.1; -; mRNA.
DR   AlphaFoldDB; H1A981; -.
DR   SMR; H1A981; -.
DR   STRING; 3880.AET02541; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   BioCyc; MetaCyc:MON-20540; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0102375; F:11-oxo-beta-amyrin 30-oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR   GO; GO:1902382; P:11-oxo-beta-amyrin catabolic process; IDA:UniProtKB.
DR   GO; GO:1902386; P:glycyrrhetinate biosynthetic 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..524
FT                   /note="11-oxo-beta-amyrin 30-oxidase"
FT                   /id="PRO_0000424184"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         472
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   524 AA;  59454 MW;  E5908AFF15553C5C CRC64;
     MEVFMFPTGT TVIISVLSVL LAVIPWYLLN KLWLKPKRFE KLLKAQGFQG EPYNLSVLKD
     KSKQNYMLKL QQEDKSKSIG LSKEAAPSIF TPVHQTVRKY GNNSFLWEGT TPRVIITDPD
     QIKDVFNKID DFPKPKLRSI AKYLSVGILD HEGKKWAKHR KIANPAFHLE KLKVMLPAFS
     HSCNEMISKW KELLSSDGTC EIDVWPSLQN FTCDVISRTA FGSSYAEGTK LFQLLKKQGF
     LLMTGRHTNN PLWGLLATTT KTKMKEIDRE IHDSLEGIIE KREKALKNGE TTNDDLLGIL
     LQSNHAEKQG QGNSKNIGMT TQDVIDECKL FYLAGQETTS SLLVWTMVLL GRYPEWQARA
     REEVLQVFGN QNPNNEGLSQ LKIVTMILYE VLRLFPPLIY FNRALRKDLK LGNLLLPEGT
     QISLPILLIH QDHDLWGDDA KEFKPERFAE GIAKATKGQV SYFPFGWGPR ICLGQNFALL
     EAKIAVSLLL QNFSFELSPN YVHVPTTVLT LQPKNGASII LHKL