C7A15_VITVI
ID C7A15_VITVI Reviewed; 480 AA.
AC F6H9N6; F1T282;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Beta-amyrin 28-monooxygenase {ECO:0000305};
DE EC=1.14.14.126 {ECO:0000269|PubMed:22039103};
DE AltName: Full=Beta-amyrin 28-oxidase {ECO:0000305};
DE AltName: Full=Cytochrome P450 716A15 {ECO:0000303|PubMed:22039103};
DE Short=VvCYP716A15 {ECO:0000303|PubMed:22039103};
GN Name=CYP716A15 {ECO:0000303|PubMed:22039103};
GN OrderedLocusNames=VIT_11s0065g00130 {ECO:0000312|EMBL:CCB48905.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Pinot noir;
RX PubMed=22039103; DOI=10.1093/pcp/pcr146;
RA Fukushima E.O., Seki H., Ohyama K., Ono E., Umemoto N., Mizutani M.,
RA Saito K., Muranaka T.;
RT "CYP716A subfamily members are multifunctional oxidases in triterpenoid
RT biosynthesis.";
RL Plant Cell Physiol. 52:2050-2061(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024;
RX PubMed=17721507; DOI=10.1038/nature06148;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
CC -!- FUNCTION: Catalyzes the carboxylation of beta-amyrin at the C-28
CC position to form oleanolic acid. Catalyzes the carboxylation of alpha-
CC amyrin and lupeol at the C-28 position to form ursolic acid and
CC betulinic acid respectively. May be involved in saponin biosynthesis in
CC fruit skin. {ECO:0000269|PubMed:22039103}.
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:22039103};
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: Expressed in leaves, stems and fruit skin.
CC {ECO:0000269|PubMed:22039103}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB619802; BAJ84106.1; -; mRNA.
DR EMBL; FN595502; CCB48905.1; -; Genomic_DNA.
DR RefSeq; NP_001268115.1; NM_001281186.1.
DR AlphaFoldDB; F6H9N6; -.
DR SMR; F6H9N6; -.
DR STRING; 29760.VIT_11s0065g00130.t01; -.
DR EnsemblPlants; Vitvi11g00900_t001; Vitvi11g00900_P001; Vitvi11g00900.
DR GeneID; 100251813; -.
DR Gramene; Vitvi11g00900_t001; Vitvi11g00900_P001; Vitvi11g00900.
DR KEGG; vvi:100251813; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; F6H9N6; -.
DR OrthoDB; 871849at2759; -.
DR BRENDA; 1.14.14.126; 6671.
DR Proteomes; UP000009183; Chromosome 11.
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; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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:0102374; F:ursolic aldehyde 28-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0102373; F:uvaol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016135; P:saponin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
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 Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..480
FT /note="Beta-amyrin 28-monooxygenase"
FT /id="PRO_0000444127"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 427
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"
FT CONFLICT 340
FT /note="K -> N (in Ref. 1; BAJ84106)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="D -> N (in Ref. 1; BAJ84106)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="R -> H (in Ref. 1; BAJ84106)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 54651 MW; D25DC172A03C99F7 CRC64;
MEVFFLSLLL IFVLSVSIGL HLLFYKHRSH FTGPNLPPGK IGWPMVGESL EFLSTGWKGH
PEKFIFDRIS KYSSEVFKTS LLGEPAAVFA GAAGNKFLFS NENKLVHAWW PSSVDKVFPS
STQTSSKEEA KKMRKLLPQF FKPEALQRYI GIMDHIAQRH FADSWDNRDE VIVFPLAKRF
TFWLACRLFM SIEDPAHVAK FEKPFHVLAS GLITVPIDLP GTPFHRAIKA SNFIRKELRA
IIKQRKIDLA EGKASQNQDI LSHMLLATDE DGCHMNEMEI ADKILGLLIG GHDTASAAIT
FLIKYMAELP HIYEKVYEEQ MEIANSKAPG ELLNWDDVQK MRYSWNVACE VMRLAPPLQG
AFREAITDFV FNGFSIPKGW KLYWSANSTH KSPECFPQPE NFDPTRFEGD GPAPYTFVPF
GGGPRMCPGK EYARLEILVF MHNVVKRFKW DKLLPDEKII VDPMPMPAKG LPVRLHPRKP
