BOT1_BOTFU
ID BOT1_BOTFU Reviewed; 510 AA.
AC Q6WP49;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Cytochrome P450 monooxygenase BOT1 {ECO:0000303|PubMed:19035644};
DE EC=1.-.-.- {ECO:0000269|PubMed:15986930};
DE AltName: Full=Botrydial biosynthesis cluster protein 1 {ECO:0000303|PubMed:19035644};
DE AltName: Full=Calcineurin-dependent protein 5 {ECO:0000303|PubMed:14651630};
GN Name=BOT1 {ECO:0000303|PubMed:19035644};
GN Synonyms=CND5 {ECO:0000303|PubMed:14651630},
GN P450-12 {ECO:0000303|PubMed:15986930};
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:AAQ16576.1};
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, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
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.
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:15986930). Botrydial is necessary for colonization of plant
CC tissue by the T4 strain (PubMed:19035644). It is a strain-dependent
CC virulence factor since highly aggressive strains like SAS56 or B05
CC still retain substantial virulence when botrydial synthesis is
CC impaired, since they produce also botcinic acid (PubMed:15986930). The
CC first step of botrydial biosynthesis is performed by the sesquiterpene
CC synthase BOT2 which catalyzes the cyclization of farnesyl diphosphate
CC (FPP) to presilphiperfolan-8-beta-ol (PSP) (PubMed:19035644,
CC PubMed:19476353). The cytochrome P450 monooxygenase BOT4 then catalyzes
CC the hydroxylation at C-4 to give a probotryane intermediate
CC (PubMed:27529428, PubMed:28617493). Acetylation of the hydroxyl at C-4
CC is carried out by the acetyltransferase BOT5, followed by the combined
CC action of the P450 monooxygenases BOT3 and BOT1, to yield finally the
CC glycol, via the regio- and stereospecific hydroxylations at C-10 and C-
CC 15 of the 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:15986930}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-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 10-beta,15-alpha-
CC dihydroxyprobotryane, botrydial, and of some of its relatives
CC (PubMed:15986930). {ECO:0000269|PubMed:15986930}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AY277723; AAQ16576.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6WP49; -.
DR SMR; Q6WP49; -.
DR PHI-base; PHI:438; -.
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; 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 Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..510
FT /note="Cytochrome P450 monooxygenase BOT1"
FT /id="PRO_0000444642"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 454
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"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 510 AA; 58162 MW; A591F786FC5D565C CRC64;
MGLLSDVINN FLPETPLAWA ALILASFTLY SVQLVVRRLY FHPLSKIPGP FLARSRYWYE
FYQDIILGGI YVKNYAALHE KYGPVLRASP DRVHVSDPDF FHEVYSSGSK YMKDPAFFQA
AGGIPEALPA IVDVEYHRRR RKLINDLFSA KSMEALSHLV LKVVQNALSK AHEHHEANKV
LDIQRLYTGI TIDTIMQVLC DRTLNFIDAK EEEEPPFLAT LRTFSENFFL LKHFPILIWM
ALNIPKSIAQ KLIPGEFEFR ASINQWIRDR ASEHELGVEK AEDGRKTVID LLLRPEDGGR
PLTHQAVEDE TYSFAFAGTH TTSHTMSMGT YYLLSHPAKL QKLRDELKPI PKNDQGLYEY
KTVRSLPYLN ACIKESLRMS SPVPGILPRL VPAEGMTWRG HYLPPGTSVS SSIYSVHTDP
NIFPNPEQFI PERWLANENL DHYLVVFGKG SRACIGLNVA WMETYLTFSN FFTSLNMTLF
ETNEQSTDWT DCGNAMIKKH VRVKVDSLAS
