ID   EFUI_HORCR              Reviewed;         295 AA.
AC   A0A2Z4HPZ8;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   03-AUG-2022, entry version 6.
DE   RecName: Full=Hydroxylase/desaturase efuI {ECO:0000303|PubMed:30051576};
DE            EC=1.-.-.- {ECO:0000305|PubMed:30051576};
DE   AltName: Full=Enfumafungin biosynthesis cluster protein I {ECO:0000303|PubMed:30051576};
GN   Name=efuI {ECO:0000303|PubMed:30051576};
OS   Hormonema carpetanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Dothioraceae; Hormonema.
OX   NCBI_TaxID=284138;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX   PubMed=30051576; DOI=10.1111/1462-2920.14333;
RA   Kuhnert E., Li Y., Lan N., Yue Q., Chen L., Cox R.J., An Z., Yokoyama K.,
RA   Bills G.F.;
RT   "Enfumafungin synthase represents a novel lineage of fungal triterpene
RT   cyclases.";
RL   Environ. Microbiol. 20:3325-3342(2018).
CC   -!- FUNCTION: Hydroxylase/desaturase; part of the gene cluster that
CC       mediates the biosynthesis of enfumafungin, a glycosylated fernene-type
CC       triterpenoid with potent antifungal activity, mediated by its
CC       interaction with beta-1,3-glucan synthase and the fungal cell wall
CC       (PubMed:30051576). The pathway begins with the terpene cyclase-glycosyl
CC       transferase fusion protein that most likely uses 2,3-oxidosqualene as
CC       substrate and catalyzes glycosylation immediately after cyclization
CC       (Probable). The fernene glycoside then could be processed by the
CC       desaturase efuI which catalyzes isomerization of a double bond
CC       established by efuA to form the core structure (Probable). The latter
CC       would then undergo a series of hydroxylations in unknown order at C-2,
CC       C-19, C-23 and C-25, which would be catalyzed by two of the three
CC       cytochrome P450 monooxygenases efuB, efuG or efuH (Probable). The
CC       hydroxy-group at C-25 becomes oxidized by the dehydrogenase efuE to
CC       enable a spontaneous, non-enzymatic hemiacetal formation with C-23
CC       (Probable). After hydroxylation at C-2, acetylation by the
CC       acetyltransferase efuC takes place (Probable). The final steps in
CC       enfumafungin biosynthesis require expansion of the 5-membered ring by
CC       lactonization via a Baeyer-Villiger reaction mediated by one of the
CC       BGC's cytochrome P450 monooxygenases (efuB, efuG or efuH) followed by
CC       ring cleavage (Probable). This type of reaction would establish a
CC       double bond between C-20 and C-21 which could be reduced by the
CC       reductase efuL to form the final product (Probable).
CC       {ECO:0000269|PubMed:30051576, ECO:0000305|PubMed:30051576}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|PubMed:30051576}.
CC   -!- SIMILARITY: Belongs to the asaB hydroxylase/desaturase family.
CC       {ECO:0000305}.
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DR   EMBL; MF611891; AWW17219.1; -; Genomic_DNA.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR044053; AsaB-like.
DR   PANTHER; PTHR34598; PTHR34598; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase.
FT   CHAIN           1..295
FT                   /note="Hydroxylase/desaturase efuI"
FT                   /id="PRO_0000454464"
SQ   SEQUENCE   295 AA;  33240 MW;  5AC3F7489CFED5D3 CRC64;
     MTAAVQSPTV NTTLNYFREV ADGGLSEIRH GTVGSTRMKY NTQPVVVNDI RSNEGEFSLD
     KQGFQLVTSA TKVKAFDEKT VKEQYYEELI DLIKETTGAS FVLPMNHLVR QQLWESIHEI
     PADADDAAIV DTTAAPAMSV HIDQTPEGAE LILQMLMQAD AGRLGKTRWG IINAWRPLKL
     IRREPLAVCD VRSVPDSDLR VLGVIYPLPD GMVYNGSSDL KSDTWNVAAN PEHKWYYASN
     MTPDEVLLLK MYDTKLDGRA RKCPHSAFKR SYDEGPARES IETRCLVFWE DQERE