ID   EFUB_HORCR              Reviewed;         505 AA.
AC   A0A2Z4HPZ7;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=Cytochrome P450 monooxygenase efuB {ECO:0000303|PubMed:30051576};
DE            EC=1.-.-.- {ECO:0000305|PubMed:30051576};
DE   AltName: Full=Enfumafungin biosynthesis cluster protein B {ECO:0000303|PubMed:30051576};
GN   Name=efuB {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; MF611883; AWW17211.1; -; 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; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..505
FT                   /note="Cytochrome P450 monooxygenase efuB"
FT                   /id="PRO_0000454457"
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         450
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   505 AA;  57410 MW;  A6A2B311D1296C6C CRC64;
     MVHLASIVSD LGFWPTVAGT VATYLFYQIV ATVYDVYFGP MSNIPGPKLW AASHIPYILM
     LWNGEDASTK LALHEKYGPV VRVSPTELSY REAQAWKDIY GHQTRGKKSF PKDSRFYAPA
     VNGAPSILNA DDPTHTRHRR ILAHAFSDKA LKEQEPLLKK WSDMLVSKLK ENVEKSPSTP
     LDLVSWFNFT TFDIMADLTF AEPLYMLEGS TYSPWVRTIF GSLKLGSRLR AVRILPGMTT
     FINMIMPNSM RQKQVEHFKY SADRVDKRLA NKNLDRPDLW AQVLKRVDVD GMSMSVAEMH
     SNSAIFMLAG TETTATLLSG LTYHLLQNPA TMSKLVNEVR STFPTRDDIN VETLQRLPYL
     NACLEEGMRM YPPVATGLPR LTPKGGAAIC GTWIPEDVAV SVSQWSTYQC EENFHKAKLF
     IPERWMGEDE QFANDNHAAF QPFSTGPRNC IGRNLAYHEA RLLLCEVLWN FDLTLDEKSE
     DWLNQPVFTV WEKDPLWVRL QVASR