ID   C87D1_MAELA             Reviewed;         475 AA.
AC   A0A0B4KZX8;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Beta-amyrin 16-alpha-hydroxylase CYP87D16 {ECO:0000305};
DE            EC=1.14.14.171 {ECO:0000269|PubMed:25578277};
DE   AltName: Full=Cytochrome P450 87D16 {ECO:0000303|PubMed:25578277};
GN   Name=CYP87D16 {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: Involved in the biosynthetic pathway of maesasaponins, which
CC       are oleanane-type saponins with diverse biological activities
CC       (PubMed:25578277). Catalyzes the C-16alpha oxidation of beta-amyrin to
CC       form 16alpha-hydroxy-beta-amyrin (PubMed:25578277).
CC       {ECO:0000269|PubMed:25578277}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-amyrin + O2 + reduced [NADPH--hemoprotein reductase] =
CC         16alpha-hydroxy-beta-amyrin + H(+) + H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:56708, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:10352, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:140655; EC=1.14.14.171;
CC         Evidence={ECO:0000269|PubMed:25578277};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56709;
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; KF318735; AHF22090.1; -; mRNA.
DR   SMR; A0A0B4KZX8; -.
DR   KEGG; ag:AHF22090; -.
DR   BRENDA; 1.14.14.171; 16279.
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   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 16-alpha-hydroxylase CYP87D16"
FT                   /id="PRO_0000455170"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         423
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   475 AA;  53412 MW;  143F1DF1604E7715 CRC64;
     MWVVGLIGVA VVTILITQYV YKWRNPKTVG VLPPGSMGLP LIGETLQLLS RNPSLDLHPF
     IKSRIQRYGQ IFATNIVGRP IIVTADPQLN NYLFQQEGRA VELWYLDSFQ KLFNLEGANR
     PNAVGHIHKY VRSVYLSLFG VESLKTKLLA DIEKTVRKNL IGGTTKGTFD AKHASANMVA
     VFAAKYLFGH DYEKSKEDVG SIIDNFVQGL LAFPLNVPGT KFHKCMKDKK RLESMITNKL
     KERIADPNSG QGDFLDQAVK DLNSEFFITE TFIVSVTMGA LFATVESVST AIGLAFKFFA
     EHPWVLDDLK AEHEAVLSKR EDRNSPLTWD EYRSMTHTMH FINEVVRLGN VFPGILRKAL
     KDIPYNGYTI PSGWTIMIVT STLAMNPEIF KDPLAFNPKR WRDIDPETQT KNFMPFGGGT
     RQCAGAELAK AFFATFLHVL ISEYSWKKVK GGSVARTPML SFEDGIFIEV TKKNK