C7A46_SOLLC
ID C7A46_SOLLC Reviewed; 482 AA.
AC K4CEE8;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Beta-amyrin 28-monooxygenase {ECO:0000305};
DE EC=1.14.14.126 {ECO:0000269|PubMed:28194155};
DE AltName: Full=Beta-amyrin 28-oxidase {ECO:0000305};
DE AltName: Full=Cytochrome P450 716A46 {ECO:0000305};
GN Name=CYP716A46;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28194155; DOI=10.3389/fpls.2017.00021;
RA Yasumoto S., Seki H., Shimizu Y., Fukushima E.O., Muranaka T.;
RT "Functional characterization of CYP716 family P450 enzymes in triterpenoid
RT biosynthesis in tomato.";
RL Front. Plant Sci. 8:21-21(2017).
CC -!- FUNCTION: Catalyzes the carboxylation of beta-amyrin at the C-28
CC position to form oleanolate (PubMed:28194155). Catalyzes the
CC carboxylation of alpha-amyrin at the C-28 position to form ursolate
CC (PubMed:28194155). {ECO:0000269|PubMed:28194155}.
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:28194155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43069;
CC Evidence={ECO:0000269|PubMed:28194155};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q94IP1};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_004243906.1; XM_004243858.3.
DR AlphaFoldDB; K4CEE8; -.
DR SMR; K4CEE8; -.
DR STRING; 4081.Solyc07g042880.1.1; -.
DR PaxDb; K4CEE8; -.
DR PRIDE; K4CEE8; -.
DR EnsemblPlants; Solyc07g042880.1.1; Solyc07g042880.1.1; Solyc07g042880.1.
DR GeneID; 101252702; -.
DR Gramene; Solyc07g042880.1.1; Solyc07g042880.1.1; Solyc07g042880.1.
DR KEGG; sly:101252702; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; K4CEE8; -.
DR OMA; FASEWEH; -.
DR OrthoDB; 871849at2759; -.
DR PhylomeDB; K4CEE8; -.
DR BRENDA; 1.14.14.126; 3101.
DR Proteomes; UP000004994; Chromosome 7.
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:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein 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: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..482
FT /note="Beta-amyrin 28-monooxygenase"
FT /id="PRO_0000451601"
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:Q94IP1"
SQ SEQUENCE 482 AA; 54862 MW; 0962F2CAD6339B83 CRC64;
MELFYASLVC LFVLLLSLSF LFLFNKKNKS MILSCPLPPG NSGWPVIGET LEFLSTGWKG
HPEKFIFDRI SKYKSSIFKT HLLGEKAVVF CGASSNKFLF SNENKLVQTW WPSSVDKVFP
SSTQTSSKEE AIKMRKMLPN FLKPEALQRY IRIMDHIAQK HFQSWENQQE VVVFPLAKRY
TFWLACRLFV SVEDPNHVAR LADPFDVLAS GLISIPINLP GTPFNRAIKA SNFIRKELVA
IIKQRKIDLT EGKASDSQDI LSHMLLTSDE NGKFMHELDI ADKILGLLIG GHDTASSACA
FIVKYLAELP EIYDQVYKEQ IEIAKSKGPG ELLSWEDIKK MKYSWNVACE VLRLAPPLQG
AFREALVDFT FNGFSIPKGW KIYWSANSTH INPEVFVDPL KFDPSRFEGN GPAPYTFVPF
GGGPRMCPGK EYARLEILVF MHHLVKRFSW KKIIRDEKIV VNPMPIPANG LPIRLYPHHV
KT
