ID   OBLE_EMEVA              Reviewed;         529 AA.
AC   A0A1V1FNZ5;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Cytochrome P450 monooxygenase oblE {ECO:0000303|PubMed:27116000};
DE            EC=1.-.-.- {ECO:0000305|PubMed:27116000};
DE   AltName: Full=Ophiobolin biosynthesis cluster protein E {ECO:0000303|PubMed:27116000};
GN   Name=oblE {ECO:0000303|PubMed:27116000};
OS   Emericella variicolor (Aspergillus stellatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1549217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=GF10;
RX   PubMed=27116000; DOI=10.1021/acs.orglett.6b00552;
RA   Narita K., Chiba R., Minami A., Kodama M., Fujii I., Gomi K., Oikawa H.;
RT   "Multiple oxidative modifications in the ophiobolin biosynthesis: P450
RT   oxidations found in genome mining.";
RL   Org. Lett. 18:1980-1983(2016).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of the sesterterpenes ophiobolins, fungal
CC       phytotoxins with potential anti-cancer activities (PubMed:27116000).
CC       The first step of the pathway is performed by the sesterterpene
CC       synthase oblA that possesses both prenyl transferase and terpene
CC       cyclase activity, converting isopentenyl diphosphate and dimethylallyl
CC       diphosphate into geranylfarnesyl diphosphate (GFPP) and further
CC       converting GFPP into ophiobolin F, respectively (By similarity). Other
CC       sesterterpenoids (C(25) terpenoids) are found as minor products of oblA
CC       (By similarity). The cytochrome P450 monooxygenase oblB then catalyzes
CC       a four-step oxidative transformation of ophiobolin F to yield
CC       ophiobolin C (PubMed:27116000). The function of the cytochrome P450
CC       monooxygenase oblE has still to be determined (Probable).
CC       {ECO:0000250|UniProtKB:A1C8C3, ECO:0000269|PubMed:27116000,
CC       ECO:0000305|PubMed:27116000}.
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:27116000}.
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; LC127211; BAX09280.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V1FNZ5; -.
DR   SMR; A0A1V1FNZ5; -.
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; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
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..529
FT                   /note="Cytochrome P450 monooxygenase oblE"
FT                   /id="PRO_0000451172"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         477
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   529 AA;  59856 MW;  A3D963B1E0EAF89D CRC64;
     MDSQFLSVSR PQLDVSAWTP QKWFVQGALR SFEEWSAWQY IVTLLIAIIT YDQVMYIWRK
     ASIAGPAFKI PLMGPFLQAL HPRFESYLEQ WASGPLSCVS IFHKFVVLAS DRDLAHKVFK
     SPTYAEPCIV PIAKDILGHK AWVFLQGKAH AEYRRGLTPL FTNKAMETYL PAQERVCADY
     FDKFVAASAA NNGQPREFMT LFREINCALS LRTFFGDYIS QDAVKKIADD FYLATAALEL
     VNVPLSMYIP GTKPWRGKRT ADAVHAEFAR CAAACKANMA TGSEPTCIVD HWVLHMMESS
     RYHARVAAGE EGVEKPTNVI REFSNQEISE TLFTFLFASQ DASSSATTWL FQILAQRPDV
     LSRLREENLA ARNGDRFKPF DLPMLESLPY TTAVIKELLR HRPPVIFVPY LATKPFPITP
     SYTVPKNSMI IPSCYPALHD PEAYPNPEVF DPDRWITGDA EKQTKNWLVF GAGPHDCLAR
     RYVPLSMAGM IGKAALELDW VHHPTERSEE IRVFATLFPM DGCQLVFSK