C7A17_VITVI
ID C7A17_VITVI Reviewed; 480 AA.
AC A5BFI4; F1T283;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2018, sequence version 2.
DT 03-AUG-2022, entry version 66.
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 716A17 {ECO:0000303|PubMed:22039103};
DE Short=VvCYP716A17 {ECO:0000303|PubMed:22039103};
GN Name=CYP716A17 {ECO:0000303|PubMed:22039103};
GN ORFNames=VITISV_041935 {ECO:0000312|EMBL:CAN72302.1};
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;
RX PubMed=18094749; DOI=10.1371/journal.pone.0001326;
RA Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT "A high quality draft consensus sequence of the genome of a heterozygous
RT grapevine variety.";
RL PLoS ONE 2:E1326-E1326(2007).
CC -!- FUNCTION: Catalyzes the carboxylation of beta-amyrin at the C-28
CC position to form oleanolic acid. May be involved in saponin
CC biosynthesis in 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; AB619803; BAJ84107.1; -; mRNA.
DR EMBL; AM457725; CAN72302.1; -; Genomic_DNA.
DR RefSeq; NP_001268076.1; NM_001281147.1.
DR AlphaFoldDB; A5BFI4; -.
DR SMR; A5BFI4; -.
DR STRING; 29760.VIT_11s0065g00040.t01; -.
DR GeneID; 100246675; -.
DR KEGG; vvi:100246675; -.
DR OrthoDB; 871849at2759; -.
DR BRENDA; 1.14.14.126; 6671.
DR ExpressionAtlas; A5BFI4; baseline.
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: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 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..480
FT /note="Beta-amyrin 28-monooxygenase"
FT /id="PRO_0000444128"
FT TRANSMEM 3..23
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 12
FT /note="C -> S (in Ref. 1; BAJ84107)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 54637 MW; 9596468F3568C74B CRC64;
MEVFFLSLLL ICVLSVSIRL YLLLYKHRSH FTGPNLPPGK IGWPMVGESL EFLSTGWKGH
PEKFIFDRIS KYSSEVFKTS LLGEPAAVFA GAAGNKFLFS NENKLVHAWW PSSVDKVFPS
STQTSSKEEA KKMRKLLPQF LKPEALQRYT GIMDHIAQRH FADSWDNRDE VIVFPLAKRF
TFWLACRLFM SIEDPAHVAK FEKPFHVLAS GLITIPIDLP GTPFHRAIKA SNFIRKELRA
IIKQRKIDLA ESKASKTQDI LSHMLLATDE DGCHMNEMSI ADKILGLLIG GHDTASSAIT
FLVKYMAELP HIYEKVYKEQ MEIANSKAPG ELLNWDDVQK MRYSWNVACE VMRLAPPLQG
AFREAITDFV FNGFSIPKGW KLYWSANSTH KSLECFPQPE KFDPTRFEGA GPAPYTFVPF
GGGPRMCPGK EYARLEILIF MHNLVKRFKW DKLLPDEKII VDPMPMPAKG LPVRLHPHKP
