ID   EFUG_HORCR              Reviewed;         563 AA.
AC   A0A2Z4HPY0;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Cytochrome P450 monooxygenase efuG {ECO:0000303|PubMed:30051576};
DE            EC=1.-.-.- {ECO:0000305|PubMed:30051576};
DE   AltName: Full=Enfumafungin biosynthesis cluster protein G {ECO:0000303|PubMed:30051576};
GN   Name=efuG {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: Cytochrome P450 monooxygenase; 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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|PubMed:30051576}.
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; MF611889; AWW17217.1; -; Genomic_DNA.
DR   UniPathway; UPA00213; -.
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   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..563
FT                   /note="Cytochrome P450 monooxygenase efuG"
FT                   /id="PRO_0000454458"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          462..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         505
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"
SQ   SEQUENCE   563 AA;  63784 MW;  09B94EEEE4A3F03F CRC64;
     MEFLEYLTPI TSHQWGIGSV FLLISIPLIV TRLLTTFWSW RELSAANQKA PGQKRGPTRP
     TTIPLIGHIV SFLLDGPGFL YNTARYYGRG IPVRVHLATF PSYVISGPEL VSAFLKDSTR
     SLTPMKRSLN YMEHAFGCPH DLVKSFATSD DKDMEQQIHS ALQNMLSGPR LGILSERYQQ
     SVKSQVLSVD AGIGDEWVEL PDLCTFVETH VFQAATRTIF GPSIVDLNPT LAKDFWNFNK
     RVKTMFLGIP AWANRTAIRA RDDMTEDIKR WQRHAEKNCN IDEIPEDVEW EEYYGSKSTR
     IRQQLLTKRG ITNESARAAE NLSMMWATNA NSIPAACWFL LQTLHDPLLQ ARVRKELDAV
     RIHDTEETNK AAAFKFDITG LTESPLCQSV YAEVLRLGVA AMIVREPTHD NLALGDWKFK
     KDEFISVPTN NELMDPDFWN SGTPKDPHPL DKFWADRFLV HPDDPQSGPR KDAKKQKAKS
     DGKPYFSMDG CTWNWIPYGG GAHLCPGRNF AKREIMLTSA IMLTAFDIEL LTDTLPKHDK
     SLFGFGTLPP IGKAPCRIRR RQL