BOT3_BOTFU
ID BOT3_BOTFU Reviewed; 567 AA.
AC Q6WP51;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Cytochrome P450 monooxygenase BOT3 {ECO:0000303|PubMed:19035644};
DE EC=1.-.-.- {ECO:0000269|PubMed:27529428};
DE AltName: Full=Botrydial biosynthesis cluster protein 3 {ECO:0000303|PubMed:19035644};
DE AltName: Full=Calcineurin-dependent protein 11 {ECO:0000303|PubMed:14651630};
GN Name=BOT3 {ECO:0000303|PubMed:19035644};
GN Synonyms=CND11 {ECO:0000303|PubMed:14651630};
OS Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=40559 {ECO:0000312|EMBL:AAQ16574.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=T4;
RX PubMed=14651630; DOI=10.1046/j.1365-2958.2003.03798.x;
RA Viaud M., Brunet-Simon A., Brygoo Y., Pradier J.-M., Levis C.;
RT "Cyclophilin A and calcineurin functions investigated by gene inactivation,
RT cyclosporin A inhibition and cDNA arrays approaches in the phytopathogenic
RT fungus Botrytis cinerea.";
RL Mol. Microbiol. 50:1451-1465(2003).
RN [2]
RP FUNCTION.
RX PubMed=15986930; DOI=10.1094/mpmi-18-0602;
RA Siewers V., Viaud M., Jimenez-Teja D., Collado I.G., Gronover C.S.,
RA Pradier J.M., Tudzynski B., Tudzynski P.;
RT "Functional analysis of the cytochrome P450 monooxygenase gene bcbot1 of
RT Botrytis cinerea indicates that botrydial is a strain-specific virulence
RT factor.";
RL Mol. Plant Microbe Interact. 18:602-612(2005).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=19035644; DOI=10.1021/cb800225v;
RA Pinedo C., Wang C.M., Pradier J.M., Dalmais B., Choquer M., Le Pecheur P.,
RA Morgant G., Collado I.G., Cane D.E., Viaud M.;
RT "Sesquiterpene synthase from the botrydial biosynthetic gene cluster of the
RT phytopathogen Botrytis cinerea.";
RL ACS Chem. Biol. 3:791-801(2008).
RN [4]
RP FUNCTION.
RX PubMed=19476353; DOI=10.1021/ja9021649;
RA Wang C.M., Hopsn R., Lin X., Cane D.E.;
RT "Biosynthesis of the sesquiterpene botrydial in Botrytis cinerea. Mechanism
RT and stereochemistry of the enzymatic formation of presilphiperfolan-8beta-
RT ol.";
RL J. Am. Chem. Soc. 131:8360-8361(2009).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=27529428; DOI=10.1021/acschembio.6b00581;
RA Moraga J., Dalmais B., Izquierdo-Bueno I., Aleu J., Hanson J.R.,
RA Hernandez-Galan R., Viaud M., Collado I.G.;
RT "Genetic and molecular basis of botrydial biosynthesis: connecting
RT cytochrome P450-encoding genes to biosynthetic intermediates.";
RL ACS Chem. Biol. 11:2838-2846(2016).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=27721016; DOI=10.1016/j.fgb.2016.10.003;
RA Porquier A., Morgant G., Moraga J., Dalmais B., Luyten I., Simon A.,
RA Pradier J.M., Amselem J., Collado I.G., Viaud M.;
RT "The botrydial biosynthetic gene cluster of Botrytis cinerea displays a
RT bipartite genomic structure and is positively regulated by the putative
RT Zn(II)2Cys6 transcription factor BcBot6.";
RL Fungal Genet. Biol. 96:33-46(2016).
RN [7]
RP FUNCTION.
RX PubMed=28617493; DOI=10.1039/c7ob01088e;
RA Franco Dos Santos G., Moraga J., Takahashi J.A., Viaud M., Hanson J.R.,
RA Hernandez Galan R., Collado I.G.;
RT "The formation of sesquiterpenoid presilphiperfolane and cameroonane
RT metabolites in the Bcbot4 null mutant of Botrytis cinerea.";
RL Org. Biomol. Chem. 15:5357-5363(2017).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of botrydial (PubMed:14651630,
CC PubMed:19035644, PubMed:27529428). Botrydial is necessary for
CC colonization of plant tissue by the T4 strain (PubMed:19035644). It is
CC a strain-dependent virulence factor since highly aggressive strains
CC like SAS56 or B05 still retain substantial virulence when botrydial
CC synthesis is impaired, since they produce also botcinic acid
CC (PubMed:15986930). The first step of botrydial biosynthesis is
CC performed by the sesquiterpene synthase BOT2 which catalyzes the
CC cyclization of farnesyl diphosphate (FPP) to presilphiperfolan-8-beta-
CC ol (PSP) (PubMed:19035644, PubMed:19476353). The cytochrome P450
CC monooxygenase BOT4 then catalyzes the hydroxylation at C-4 to give a
CC probotryane intermediate (PubMed:27529428, PubMed:28617493).
CC Acetylation of the hydroxyl at C-4 is carried out by the
CC acetyltransferase BOT5, followed by the combined action of the P450
CC monooxygenases BOT3 and BOT1, to yield finally the glycol, via the
CC regio- and stereospecific hydroxylations at C-10 and C-15 of the
CC probotryane intermediates, respectively (PubMed:15986930,
CC PubMed:27529428). The cleavage of the C10-C15 bond of probotryane
CC skeleton is an intriguing and chemically important reaction, which
CC could be mediated by some of the monooxygenases or by a combination of
CC them (PubMed:27529428). It is possible that either BOT3 or BOT1 would
CC oxidize either the 10- or the 15-hydroxy group to the hydroperoxide
CC derivative, which would then undergo heterolytic fragmentation to give
CC the dialdehyde botrydial (PubMed:27529428). Finally, the dehydrogenase
CC BOT7 might be involved in the conversion of botrydial to
CC dihydrobotrydial (PubMed:27721016). {ECO:0000269|PubMed:14651630,
CC ECO:0000269|PubMed:15986930, ECO:0000269|PubMed:19035644,
CC ECO:0000269|PubMed:19476353, ECO:0000269|PubMed:27529428,
CC ECO:0000269|PubMed:27721016, ECO:0000269|PubMed:28617493}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:27529428}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: The botrydial biosynthesis cluster genes are co-regulated by
CC the Ca(2+)/calcineurin signal transduction pathway, which is under the
CC control of the alpha subunit BCG1 of a heterotrimeric G protein
CC (PubMed:14651630, PubMed:19035644). Expression of the cluster is also
CC positively regulated by the cluster-specific transcription factor BOT6
CC (PubMed:27721016). {ECO:0000269|PubMed:14651630,
CC ECO:0000269|PubMed:19035644, ECO:0000269|PubMed:27721016}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of botrydial and
CC accumulates high levels of the biosynthetic intermediate beta-acetoxy-
CC 15-alpha--hydroxyprobotryane and small amounts of botcinin A
CC (PubMed:27529428). {ECO:0000269|PubMed:27529428}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AY277723; AAQ16574.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6WP51; -.
DR SMR; Q6WP51; -.
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 Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
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.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..567
FT /note="Cytochrome P450 monooxygenase BOT3"
FT /id="PRO_0000444643"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 509
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:P04798"
SQ SEQUENCE 567 AA; 64374 MW; A6E9EFC2982681CA CRC64;
MEKSNPTLDL ATKTALLTWQ KSNALLQHGI ERATPFVLAV KSKAWQDAQS IGSKVAEAKF
RDIDRTEITT ITSVALGLYF AYVFCLVFYR LYLHPLAKFP GYRICAACEW YEFYCYIVKG
GQWGNEIRKM HEKYGPIVRT SPWELSVRDP AFYDQLYVTA STRKTDMWPR GREGNGFDNS
HHLSVSHELH RTRRKHLEPF FSRQGITRIE SRIAERVMKM DDRLVGLKGS GSIIEVDHML
CALTGDIIGQ VSSGMEAGLL DDPEFTPAWK DLMIKSTAIA PLFRCFPWIN KFLQSLPTSI
MNSVYPKGIS NMMLGKTGQQ NIEKIKTQIA TSKRDLSDVS VFHHLLSSNV PESEKSIDRL
RAESMILLLA GTLAGAHTLT FVVFYVLQNP QIEKRLRAEL QPVFKGYPNK MPTWAELEKL
PYLRGCVKEA LRLNGLVGNL ARCSPDEDIQ FHQWVIPKKT PVGMSIYAMH FDQNVFSEPE
AFKPERWIGE YNKQMDRNFV PFTKGSRSCL GVNLAWAELY LASAMLFRPG GPKLVLHDGG
ESDIKIARDY IMGFPKAGAK DVRVKIE
