OBLB_EMEVA
ID OBLB_EMEVA Reviewed; 547 AA.
AC A0A1V1FNM9;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Cytochrome P450 monooxygenase oblB {ECO:0000303|PubMed:27116000};
DE EC=1.-.-.- {ECO:0000269|PubMed:27116000};
DE AltName: Full=Ophiobolin biosynthesis cluster protein B {ECO:0000303|PubMed:27116000};
GN Name=oblB {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], CATALYTIC ACTIVITY, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=4 O2 + ophiobolin F + 4 reduced [NADPH--hemoprotein reductase]
CC = 4 H(+) + 6 H2O + ophiobolin C + 4 oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:66896, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78293,
CC ChEBI:CHEBI:167548; Evidence={ECO:0000269|PubMed:27116000};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66897;
CC Evidence={ECO:0000269|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}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; LC127211; BAX09283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1FNM9; -.
DR SMR; A0A1V1FNM9; -.
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; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..547
FT /note="Cytochrome P450 monooxygenase oblB"
FT /id="PRO_0000451171"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 489
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"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 547 AA; 62433 MW; 467D6E4CE1FEE945 CRC64;
MEAYFPQTTR DALAGLLPSQ MSGRFPEMPA YLTQDVLLRA AGAVGAIYAI YISGLVIYRL
FLSPLAKFPG PKIAAMTSYY ELYYDVIHKG KYIFQIEKMH DKYGPIVRIN PFELSIRDSE
YYDELYVMGN IRKTDRYEAF VEGVVDFEGS HLATISHDLH RKRRKPLDPY FSRQGITRLE
PMVAELTEKL VVNRLESYKG TGKVVRLDHA FTAFSGDVIN RICVNRPSEV YVEDEDFAPW
WFDMFHLGAV SLPLFMGMPW LIRLIRFMPA SLASYLNTSM GSFSKFKLMC DEQLNEAKRE
KALKSKSQNS NQPTPGRLTL FRHLVDSDLP PAELSDTRLS REAQVLIGSG TMTTAGTMGF
LCYYIMINPK IRARLSEELG SVMAEYPAKK PSLAELERLP YLQAVIKEGL RLSYGTMHRR
ARVSPSQPLL FKEWVIPPGT PVGMSAYFQH RDEKTFPRPM EFLPERWLGE ITPAMYRNYI
PFSKGSRHCL GMNLAYCELN FILAAMFRPG AAPFELYGTD ESDVRPVHDL IVPMPRLDSL
GVRVVYN
