ID   C71E6_SOLLC             Reviewed;         475 AA.
AC   A0A3Q7HS74;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Beta-amyrin 6-beta-monooxygenase {ECO:0000305};
DE            EC=1.14.14.64 {ECO:0000269|PubMed:28194155};
DE   AltName: Full=Cytochrome P450 716E26 {ECO:0000305};
GN   Name=CYP716E26 {ECO:0000303|PubMed:28194155};
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].
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, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
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 C-6 beta-hydroxylation of beta-amyrin to form
CC       daturadiol (PubMed:28194155). Catalyzes the C-6 beta-hydroxylation of
CC       alpha-amyrin to form 6-beta-hydroxy-alpha-amyrin (PubMed:28194155).
CC       {ECO:0000269|PubMed:28194155}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-amyrin + O2 + reduced [NADPH--hemoprotein reductase] =
CC         daturadiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:55452, 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:138955; EC=1.14.14.64;
CC         Evidence={ECO:0000269|PubMed:28194155};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55453;
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   -!- TISSUE SPECIFICITY: Specifically expressed in roots.
CC       {ECO:0000269|PubMed:28194155}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   RefSeq; XP_004241821.1; XM_004241773.3.
DR   AlphaFoldDB; A0A3Q7HS74; -.
DR   SMR; A0A3Q7HS74; -.
DR   STRING; 4081.Solyc06g065430.2.1; -.
DR   EnsemblPlants; Solyc06g065430.3.1; Solyc06g065430.3.1; Solyc06g065430.3.
DR   GeneID; 101250025; -.
DR   Gramene; Solyc06g065430.3.1; Solyc06g065430.3.1; Solyc06g065430.3.
DR   KEGG; sly:101250025; -.
DR   OMA; FMDSMAR; -.
DR   BRENDA; 1.14.14.64; 3101.
DR   Proteomes; UP000004994; Chromosome 6.
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:0019742; P:pentacyclic triterpenoid metabolic 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..475
FT                   /note="Beta-amyrin 6-beta-monooxygenase"
FT                   /id="PRO_0000451599"
FT   TRANSMEM        6..22
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:Q94IP1"
SQ   SEQUENCE   475 AA;  54462 MW;  05D869BC0333311C CRC64;
     MDPFILYSLA FALVYISLYF IFKGNYSNNK HTNLPLGSNG WPILGENIDM AYSSSPEKFI
     HERMEKHSSQ VFKTSLLGQK IAIFCGTSGN KFLFSNENKL LTTWWPPSLT KPLMCPTQSQ
     SQNSVKEIAL LNRGFLREIL KPENLKQYIP FMDSMARDHL KQEWIPFKEV KIYPLVKKYT
     FSLACKLFLS IDDFRHVKKL SDPFVLVTSG MFTVPINLPG TPYNRAIKGG KMVHEELMKI
     IKERKINEKN NHSNDLLSQL ISFSDENGQF MNDAEIYNNI IGLLVASYDT TSAAITFVLK
     YLAELPNIFN EVYKEQMEIA KSKGEGELLN WDDIQKMKYS WNVACEAIRL MPPAQGAFRE
     AITDFTFGGF TVPKGWKTFW SVYSTHKNPK YFPEPEKFDP CRFEGSGPEP YTFVPFGGGP
     RMCPGKEYAR LEILVFMYNI VTNFKLEKLV PHEKIIYKSS PVPLNGLPVR IQPIA