OPS4_BEAB2
ID OPS4_BEAB2 Reviewed; 427 AA.
AC J4VWM7;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=FAD-dependent monooxygenase OpS4 {ECO:0000303|PubMed:26305932};
DE EC=1.-.-.- {ECO:0000269|PubMed:26305932};
DE AltName: Full=Oosporein biosynthesis protein 4 {ECO:0000303|PubMed:26305932};
DE Flags: Precursor;
GN Name=OpS4 {ECO:0000303|PubMed:26305932}; ORFNames=BBA_08182;
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860;
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.-H., Zheng P., Wang Z.-L., Zhang S., Xie X.-Q., Shang Y.,
RA St Leger R.J., Zhao G.-P., Wang C., Feng M.-G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=26305932; DOI=10.1073/pnas.1503200112;
RA Feng P., Shang Y., Cen K., Wang C.;
RT "Fungal biosynthesis of the bibenzoquinone oosporein to evade insect
RT immunity.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11365-11370(2015).
CC -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the bibenzoquinone oosporein, a metabolite
CC required for fungal virulence that acts by evading host immunity to
CC facilitate fungal multiplication in insects (PubMed:26305932). The non-
CC reducing polyketide synthase OpS1 produces orsellinic acid by
CC condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:26305932).
CC Orsellinic acid is then hydroxylated to benzenetriol by the hydroxylase
CC OpS4 (PubMed:26305932). The intermediate is oxidized either
CC nonenzymatically to 5,5'-dideoxy-oosporein or enzymatically to
CC benzenetetrol by the oxidoreductase OpS7 (PubMed:26305932). The latter
CC is further dimerized to oosporein by the catalase OpS5
CC (PubMed:26305932). OpS6 probably functions en route for protecting
CC cells against oxidative stress by scavenging any leaked free radical
CC form of benzenetetrol by activating the thiol group of glutathione
CC (PubMed:26305932). {ECO:0000269|PubMed:26305932}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:26305932}.
CC -!- INDUCTION: Expression is positively regulated by the oosporein cluster
CC specific regulator OpS3 that binds the promoter at a 5'-CGGA-3' motif
CC (PubMed:26305932). Expression is negatively regulated by the global
CC transcription factor Msn2 that binds the stress-response element 5'-
CC AGGGG-3' (PubMed:26305932). {ECO:0000269|PubMed:26305932}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of oosporein and leads to
CC the accumulation of orsellinic acid (PubMed:26305932).
CC {ECO:0000269|PubMed:26305932}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH725181; EJP62795.1; -; Genomic_DNA.
DR RefSeq; XP_008601501.1; XM_008603279.1.
DR AlphaFoldDB; J4VWM7; -.
DR SMR; J4VWM7; -.
DR STRING; 655819.J4VWM7; -.
DR EnsemblFungi; EJP62795; EJP62795; BBA_08182.
DR GeneID; 19891194; -.
DR HOGENOM; CLU_009665_19_3_1; -.
DR InParanoid; J4VWM7; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Glycoprotein; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal; Virulence.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..427
FT /note="FAD-dependent monooxygenase OpS4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000438575"
FT BINDING 37..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 306
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 316..320
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 427 AA; 47309 MW; AF9959EB3DE52BF0 CRC64;
MGSIREPLHL VVIGGGLAGL SAAIATRLEG HRCTLLEKAP EFNEVGAGLQ LTPNSTRLLR
RWGVLDKLRS KAGIPTQLTV RRYDGSKVLS RADGWDETMQ SQYDAPFWDM HRADLQAAMV
ARARHLGVDV RTGAEVESID TDGVAVILAG TRERLQGDVV LAADGLWSRT RAALFPDLGT
APQPTGDLAY RIILRLENLQ HDPELAAWVA KPTVNFWVGA DAHAVAYSVR GGSELNLVLL
CPDDLPEGCA RAQADLEEMR ARFQGWDPLL CRFLDNVKTV EKWRLMHMPS LPKWNHESGY
FTMAGDSCHP MLPYLAQGAN SAMEDGAVLG RLLGSIHEAS RIPDVLAVYQ EIRKVRVEKI
AKQALKQRYN FHMPDGPLQE ARDEAMTTHQ QREEEYASQW TCPIMQPWLY GYDAIAVADS
AVANTKL
