BET5_NEOBT
ID BET5_NEOBT Reviewed; 586 AA.
AC A0A0C6E5D0;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=FAD-linked oxidoreductase orf1 {ECO:0000303|PubMed:25530455};
DE EC=1.-.-.- {ECO:0000250|UniProtKB:Q0UK53};
DE AltName: Full=Betaenone biosynthesis cluster protein B {ECO:0000303|PubMed:25530455};
DE AltName: Full=FAD-dependent BBE enzyme-like protein {ECO:0000250|UniProtKB:Q0UK53};
DE Flags: Precursor;
GN Name=orf1 {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].
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: FAD-linked oxidoreductase; 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=betaenone C = betaenone A; Xref=Rhea:RHEA:61896,
CC ChEBI:CHEBI:145053, ChEBI:CHEBI:145055;
CC Evidence={ECO:0000250|UniProtKB:Q0UK53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61897;
CC Evidence={ECO:0000250|UniProtKB:Q0UK53};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25530455}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; LC011911; BAQ25462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C6E5D0; -.
DR SMR; A0A0C6E5D0; -.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..586
FT /note="FAD-linked oxidoreductase orf1"
FT /id="PRO_5002199092"
FT DOMAIN 124..303
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 586 AA; 62959 MW; CDFFC0694470EC82 CRC64;
MKSFATTVLL VTPGIYAAAL SGRQGQAINS SCKVIPGDTA WPSRQIWSQL NDTLDGRLIQ
STPQAAVCRP GGYGSISENG TECTTLKEDW DYAKAFLDSA VEIMNPWYQN TSCSPFYRVD
QPCTLGNYVS YAIPVSGPED VVTAINFTQT HNVRLVIKNT GHDYLGKSTG TGGLSLWTHN
LQSKQIVNYT SPAYSGPAIK VGAGVTGGEA LLHASQFGYR LVSGDCSTVG YAGGYSSGGG
HSLLNSVHGM AADNVLEWEV VTADGRHLVA SATQNSDLYW ALSGGGAGNL AVVLSMTAKV
HPDGLVGAAT LSFNATSSPS NTSYISAINA WWTFLPTLID AGASPSFNIY TNNFLIYNTT
APGKSAQDMS TLYAPYLSTL SSLSIPYTFQ TYTAPSFLQH YNATDGPLPY GPYVASQLFN
SRMIPRSLSS SPSNLTTAIL SSVATDAPGI WQLGCLGINV NSTRISHPDN AVAPHWRTAM
AVCLEFSLYD WAIPEEEMVA RRQHLADVIH PAIVKVTPGS GAYLNEADPL VYPVGEDGWK
DAFYGANYER LRGLKREWDP ERVFYAYTAP GSEEWVSDAE GRLCRV
