C7A14_PLAGD
ID C7A14_PLAGD Reviewed; 481 AA.
AC A0A1I9Q5Z0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Beta-amyrin 16-beta-monooxygenase {ECO:0000303|PubMed:28371833};
DE EC=1.14.14.63 {ECO:0000269|PubMed:28371833};
DE AltName: Full=Beta-amyrin 16-oxidase {ECO:0000303|PubMed:28371833};
DE AltName: Full=Cytochrome P450 716A141 {ECO:0000303|PubMed:28371833};
GN Name=CYP716A141 {ECO:0000303|PubMed:28371833};
OS Platycodon grandiflorus (Balloon flower) (Campanula grandiflora).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Campanulaceae; Platycodon.
OX NCBI_TaxID=94286;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Miettinen K., Pollier J., Arendt P., Moses T., Mertens J., Goossens A.;
RT "CYP716 enzymes form the cradle of triterpenoid diversity in eudicots.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=28371833; DOI=10.1093/pcp/pcx043;
RA Tamura K., Teranishi Y., Ueda S., Suzuki H., Kawano N., Yoshimatsu K.,
RA Saito K., Kawahara N., Muranaka T., Seki H.;
RT "Cytochrome P450 monooxygenase CYP716A141 is a unique beta-amyrin C-16beta
RT oxidase involved in triterpenoid saponin biosynthesis in Platycodon
RT grandiflorus.";
RL Plant Cell Physiol. 58:874-884(2017).
CC -!- FUNCTION: Involved in triterpenoid saponin biosynthesis in roots
CC (PubMed:28371833). Catalyzes the hydroxylation of beta-amyrin at the C-
CC 16 beta position to form maniladiol (PubMed:28371833). Is also able to
CC oxidize oleanolat to cochalate (PubMed:28371833). Has weak activity
CC catalyzing the three-step oxidation at C-28 of beta-amyrin to form
CC oleanolate (PubMed:28371833). {ECO:0000269|PubMed:28371833}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-amyrin + O2 + reduced [NADPH--hemoprotein reductase] =
CC H(+) + H2O + maniladiol + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:55440, 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:138945; EC=1.14.14.63;
CC Evidence={ECO:0000269|PubMed:28371833};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55441;
CC Evidence={ECO:0000269|PubMed:28371833};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + oleanolate + reduced [NADPH--hemoprotein reductase] =
CC cochalate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:55444, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:82828,
CC ChEBI:CHEBI:138946; EC=1.14.14.63;
CC Evidence={ECO:0000269|PubMed:28371833};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55445;
CC Evidence={ECO:0000269|PubMed:28371833};
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 -!- TISSUE SPECIFICITY: Highly expressed in roots (PubMed:28371833).
CC Expressed at very low levels in leaves and petals (PubMed:28371833).
CC {ECO:0000269|PubMed:28371833}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KU878855; AOG74838.1; -; mRNA.
DR EMBL; LC209200; BAX04008.1; -; mRNA.
DR KEGG; ag:BAX04008; -.
DR BRENDA; 1.14.14.115; 15439.
DR BRENDA; 1.14.14.126; 15439.
DR BRENDA; 1.14.14.63; 15439.
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 GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
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 16-beta-monooxygenase"
FT /id="PRO_0000454861"
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:Q96242"
SQ SEQUENCE 481 AA; 54169 MW; 3501DC7927280C54 CRC64;
MDSLFIIISL VIVILTTIFI LSNLLSKKTI LLPGKTGLPL IGESIDYFNK LRTGINEKFV
MERKLKYASD VFKTSILGEN MAFLTGPEGN KFLFSNENKL VQVWWPSSVD SIIKKSHNKS
AQAESAKVRV LLPPFLRAHA IKHYVSTMDS ELRQHVADFW VGRDEVEVCP LVRKYTFALA
VRLFLSVRDP GELEALARPF EEAAGGIIAI PINFPGTRFN RGIKASQRIR KVIGGIIEQR
RKDLSEGKAT PSQDLLSHMI VEVDRRNAEN PDIAPATDSD ISSDILGLLI GGYDTINTTI
VFVMMTLVEY PDVYDQVLKE QREIAASKAP GELLNWDDLG KMKYSWNVAC EVLRLRPPTV
GAFRVAKTDF NYGGYTIPKG WKLHYIPHFT QKNPDYFPNP EKFDPSRFAG DGPAPYTFVP
FGGGPRMCPG NEYARAEILV FMHNIILRYN WEKLIPNEKV VIDPLPRPSQ GLPIRLIPHK
A
