BET2_NEOBT
ID BET2_NEOBT Reviewed; 521 AA.
AC A0A0C6DUU3;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Cytochrome P450 monooxygenase bet2 {ECO:0000303|PubMed:25530455};
DE EC=1.-.-.- {ECO:0000269|PubMed:25530455};
DE AltName: Full=Betaenone biosynthesis cluster protein 2 {ECO:0000303|PubMed:25530455};
GN Name=bet2 {ECO:0000303|PubMed:25530455};
OS Neocamarosporium betae (Beet black rot fungus) (Pleospora betae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Neocamarosporium.
OX NCBI_TaxID=1979465;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=25530455; DOI=10.1039/c4cc09512j;
RA Ugai T., Minami A., Fujii R., Tanaka M., Oguri H., Gomi K., Oikawa H.;
RT "Heterologous expression of highly reducing polyketide synthase involved in
RT betaenone biosynthesis.";
RL Chem. Commun. (Camb.) 51:1878-1881(2015).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of betaenones, phytotoxic polyketides
CC involved in leaf spot disease in sugar beets (PubMed:25530455). The
CC first step of the pathway is the synthesis of dehydroprobetaenone I by
CC the polyketide synthase bet1 and the enoyl reductase bet3 via
CC condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units
CC and 5 methylations (PubMed:25530455). The C-terminal reductase (R)
CC domain of bet1 catalyzes the reductive release of the polyketide chain
CC (PubMed:25530455). Because bet1 lacks a designated enoylreductase (ER)
CC domain, the required activity is provided the enoyl reductase bet3
CC (PubMed:25530455). The short-chain dehydrogenase/reductase bet4 then
CC catalyzes reduction of dehydroprobetaenone I to probetaenone I
CC (PubMed:25530455). The cytochrome P450 monooxygenase bet2 catalyzes
CC successive epoxidation, oxidation (resulting from epoxide opening) and
CC hydroxylation to install a tertiary alcohol in the decaline ring to
CC yield betaenone C from dehydroprobetaenone I and betaenone B from
CC probetaenone I (PubMed:25530455). The FAD-linked oxidoreductase (orf1)
CC is probably responsible for the conversion of betaenone C to betaenone
CC A via an intramolecular aldol reaction between C-1 and C-17 to form the
CC bridged tricyclic system in betaenone A (By similarity).
CC {ECO:0000250|UniProtKB:Q0UK53, ECO:0000269|PubMed:25530455}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dehydroprobetaenone I + H(+) + NADPH + O2 = epoxybetaenone +
CC H2O + NADP(+); Xref=Rhea:RHEA:61860, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:145061, ChEBI:CHEBI:145069;
CC Evidence={ECO:0000269|PubMed:25530455};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61861;
CC Evidence={ECO:0000269|PubMed:25530455};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dehydroprobetaenone I + 3 H(+) + 3 NADPH + 3 O2 = betaenone C
CC + 3 H2O + 3 NADP(+); Xref=Rhea:RHEA:61856, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:145053, ChEBI:CHEBI:145061;
CC Evidence={ECO:0000269|PubMed:25530455};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61857;
CC Evidence={ECO:0000269|PubMed:25530455};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25530455}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; LC011911; BAQ25465.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C6DUU3; -.
DR SMR; A0A0C6DUU3; -.
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.
FT CHAIN 1..521
FT /note="Cytochrome P450 monooxygenase bet2"
FT /id="PRO_0000448651"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 461
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 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 521 AA; 60184 MW; 19E40D7BF7F28ABE CRC64;
MMDLFKTDIM PDLQSSMMAS IGSNWRFALF VAATLLTSYI VIVRPLKNVL FHPLRKYPGP
KLFAGSSIPY GFWYMTGKWH TKIRQLHATY GPVVRIGPDE LSYACPEAWE DIYGRYVPAK
RKENPKPVWY CSPDAHDMVG ASLGDHGRMR RVMTPGFTYS AMCKQEPLIK VHVDLFLEKL
RGVCDDGNAT VNMLEWFTYC TFDLIGDLSF GEPFGCLENS MLHPWLQLVF ANIYVTHIIL
LCKRIPFFYL FLPIKTTLQL YRDFNRHVIL LRQVVERRLS LTTPRNDFLD IMTSKKTSTL
YLTNEEIFKN AILLTGGGAE TTSSSLTGMA FILTTRPDVK KRIVEELHAT FPNEEAINMR
SVAQLTYTGA FIEEAMRYYP PGPNTMWRTT PAGGNTILGD YIPENTIIGI PHRVLYRSEA
YWKHADEIHP ERWLPDGQRP AEFDHDRREG FQPFSYGPRA CIAMNLAYAE MRYILARFLW
NFDIQETEQS KHWMDNQKAY LVWDKPGLFV RLKPVAKEEA Q
