OPS5_BEAB2
ID OPS5_BEAB2 Reviewed; 590 AA.
AC J5JH35;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Oxidoreductase OpS5 {ECO:0000303|PubMed:26305932};
DE EC=1.-.-.- {ECO:0000269|PubMed:26305932};
DE AltName: Full=Laccase OpS5 {ECO:0000303|PubMed:26305932};
DE AltName: Full=Oosporein biosynthesis protein 5 {ECO:0000303|PubMed:26305932};
DE Flags: Precursor;
GN Name=OpS5 {ECO:0000303|PubMed:26305932}; ORFNames=BBA_08183;
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, 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: Oxidoreductase; part of the gene cluster that mediates the
CC biosynthesis of the bibenzoquinone oosporein, a metabolite required for
CC fungal virulence that acts by evading host immunity to facilitate
CC fungal multiplication in insects (PubMed:26305932). The non-reducing
CC polyketide synthase OpS1 produces orsellinic acid by condensing acetyl-
CC CoA with 3 malonyl-CoA units (PubMed:26305932). Orsellinic acid is then
CC hydroxylated to benzenetriol by the hydroxylase OpS4 (PubMed:26305932).
CC The intermediate is oxidized either nonenzymatically to 5,5'-dideoxy-
CC oosporein or enzymatically to benzenetetrol by the oxidoreductase OpS7
CC (PubMed:26305932). The latter is further dimerized to oosporein by the
CC catalase OpS5 (PubMed:26305932). OpS6 probably functions en route for
CC protecting cells against oxidative stress by scavenging any leaked free
CC radical form of benzenetetrol by activating the thiol group of
CC glutathione (PubMed:26305932). {ECO:0000269|PubMed:26305932}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:26305932}.
CC -!- INDUCTION: 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
CC (PubMed:26305932). {ECO:0000269|PubMed:26305932}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {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; EJP62796.1; -; Genomic_DNA.
DR RefSeq; XP_008601502.1; XM_008603280.1.
DR AlphaFoldDB; J5JH35; -.
DR SMR; J5JH35; -.
DR EnsemblFungi; EJP62796; EJP62796; BBA_08183.
DR GeneID; 19891195; -.
DR HOGENOM; CLU_006504_3_2_1; -.
DR InParanoid; J5JH35; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW Copper; Glycoprotein; Metal-binding; Oxidoreductase; Reference proteome;
KW Repeat; Signal; Virulence.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..590
FT /note="Oxidoreductase OpS5"
FT /evidence="ECO:0000255"
FT /id="PRO_5003784537"
FT DOMAIN 80..194
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 205..358
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 427..554
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 590 AA; 67074 MW; 2F6D95B16603800F CRC64;
MMRPWTILIA SSWLSLAAAS ASASACAAKP SVAAEIASID HDNCEHGPNS RGCWGDYSIN
TNYYEQAPDT GVTREYWFVV ENITMAPDGY EQHVLAINRS IPGPLIEANW GDEVVIHVTN
NMERNGTAIH WHGIRQLNNN AHDGVPGVTQ CPIPPGGSYT YRWKAEQYGT SWYHSHFSLQ
YSVGLQGPMI IHGPATANYD EDLGTVMLQD WSHVSPFAMW WYARVPSGPP SLSNSLINGK
NIFRCTDPLD KNCLGTGERS EWHFEKGKRY RMRLVNTGLY SNFRFAIDGH NLTVIANDFV
PIEPYTTDNV IISMGQRYDV IVEANAPEDN YWLRAIWQTS CCPNDYANDT LGIIRYDPQS
TALPNTTHPA LHYPDNCDDE PAEKLVPHVK VDAGPPARTD VFNLYRHTYD MPRGFMWTLN
DTYLWIDWSK PTNLLVAEND TTIFPPNYLL YHTPDGPNQW VYIVFNDISE RNRSHPMHLH
GHDFFLLGTG EGNFTKDSPL QLKNPPRRDT ASWPKRGYMV FAYKTDNPGA WLIHCHIAWH
SSQGLGMQML ERPGEMTYTE DEDQALHQTC QSWNKFYESP EQYIQEDSGI
