ID   C7A75_MAELA             Reviewed;         487 AA.
AC   A0A0B4L1W8;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Cytochrome P450 716A75 {ECO:0000303|PubMed:25578277};
DE            EC=1.14.14.- {ECO:0000269|PubMed:25578277};
GN   Name=CYP716A75 {ECO:0000303|PubMed:25578277};
OS   Maesa lanceolata (False assegai).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Primulaceae; Maesa.
OX   NCBI_TaxID=992730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=25578277; DOI=10.1016/j.molp.2014.11.004;
RA   Moses T., Pollier J., Faizal A., Apers S., Pieters L., Thevelein J.M.,
RA   Geelen D., Goossens A.;
RT   "Unraveling the triterpenoid saponin biosynthesis of the African shrub
RT   Maesa lanceolata.";
RL   Mol. Plant 8:122-135(2015).
CC   -!- FUNCTION: Catalyzes the C-28 oxidation of beta-amyrin to form
CC       erythrodiol (PubMed:25578277). Catalyzes the C-28 oxidation of
CC       erythrodiol to form oleanolic aldehyde (PubMed:25578277). Catalyzes the
CC       C-28 oxidation of oleanolic aldehyde to form oleanolate
CC       (PubMed:25578277). {ECO:0000269|PubMed:25578277}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-amyrin + O2 + reduced [NADPH--hemoprotein reductase] =
CC         erythrodiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:43072, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:10352, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:67939; Evidence={ECO:0000269|PubMed:25578277};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43073;
CC         Evidence={ECO:0000269|PubMed:25578277};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=erythrodiol + O2 + reduced [NADPH--hemoprotein reductase] =
CC         H(+) + 2 H2O + oleanolic aldehyde + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:43076, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:67939,
CC         ChEBI:CHEBI:82827; Evidence={ECO:0000269|PubMed:25578277};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43077;
CC         Evidence={ECO:0000269|PubMed:25578277};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + oleanolic aldehyde + reduced [NADPH--hemoprotein
CC         reductase] = 2 H(+) + H2O + oleanolate + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:43080, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:82827,
CC         ChEBI:CHEBI:82828; Evidence={ECO:0000269|PubMed:25578277};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43081;
CC         Evidence={ECO:0000269|PubMed:25578277};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q96242};
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; KF318733; AHF22088.1; -; mRNA.
DR   SMR; A0A0B4L1W8; -.
DR   KEGG; ag:AHF22088; -.
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:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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..487
FT                   /note="Cytochrome P450 716A75"
FT                   /id="PRO_0000455171"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         434
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:Q96242"
SQ   SEQUENCE   487 AA;  55662 MW;  3278D446B09D2778 CRC64;
     MELLFVSLLS LFLLILLPLS LLFLFPSSFS TTTTEANKNS ANLPPGLTGW PVVGESFQFL
     AAGWRGNPEK FIFDRIAKYS SYVYKTNLML ERTAVFCGAP AHKFLFSNEN KLVQSWWPSS
     VNKIFPSSNQ TSSKEEAMKM RKMLPNFFKP EALQGYIGIM DTIAQRHFAA DWDNKDYIVV
     FPLCKRYTFW LACKIFMSIE DPKDVDRFLA RFNLVAEGLL SIPIDLPGTP FHHSIKAAEF
     IREHLVAIIK QRKIDLAEGK ASPTQDIMSY MLLTPDEDGK FMKEYDIADK ILGLLVGGHD
     TASSACAFIV KYLAELPQVY QGVYKEQMEI AKSKGPGELL NWDDIQKMKY SWNVACEVLR
     LAPPLQGAFR DVLKDFMYEG FYIPKGWKVY WSAHSTHKNP EYFPEPYKFD PSRFDGSGPA
     PYTFVPFGGG PRMCPGKEYA RLEILVFMHN LVKRFRWEKL IPDEKIVVNP MPVPEKGLPI
     RLFSYDA