OBLB_ASPCL
ID OBLB_ASPCL Reviewed; 520 AA.
AC A1C8C2;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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}; ORFNames=ACLA_076840;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
RN [2]
RP FUNCTION.
RX PubMed=23324037; DOI=10.1021/ol303408a;
RA Chiba R., Minami A., Gomi K., Oikawa H.;
RT "Identification of ophiobolin F synthase by a genome mining approach: a
RT sesterterpene synthase from Aspergillus clavatus.";
RL Org. Lett. 15:594-597(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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:23324037,
CC PubMed:27116000). The first step of the pathway is performed by the
CC sesterterpene synthase oblA that possesses both prenyl transferase and
CC terpene cyclase activity, converting isopentenyl diphosphate and
CC dimethylallyl diphosphate into geranylfarnesyl diphosphate (GFPP) and
CC further converting GFPP into ophiobolin F, respectively
CC (PubMed:23324037). Other sesterterpenoids (C(25) terpenoids) are found
CC as minor products of oblA (PubMed:23324037). It is expected that
CC ophiobolin F is then oxidized to ophiobolin A via ophiobolin C and
CC ophiobolin B intermediates by the combined action of the cytochrome
CC P450 monooxygenase oblB and the FAD-dependent oxidoreductase oblC
CC (Probable). Although oblB catalyzes multistep oxygenations at C5 and
CC C21/C7 in a relatively efficient manner, it is unable to convert
CC ophiobolin F to ophiobolin C and produces instead several unexpected
CC derivatives (PubMed:27116000). {ECO:0000269|PubMed:23324037,
CC ECO:0000269|PubMed:27116000, 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:0000269|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; DS027045; EAW14643.1; -; Genomic_DNA.
DR RefSeq; XP_001276069.1; XM_001276068.1.
DR AlphaFoldDB; A1C8C2; -.
DR SMR; A1C8C2; -.
DR EnsemblFungi; EAW14643; EAW14643; ACLA_076840.
DR GeneID; 4708280; -.
DR KEGG; act:ACLA_076840; -.
DR VEuPathDB; FungiDB:ACLA_076840; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_14_4_1; -.
DR OMA; RLSYGVM; -.
DR OrthoDB; 1247045at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
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 Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..520
FT /note="Cytochrome P450 monooxygenase oblB"
FT /id="PRO_0000451169"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 462
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 520 AA; 59400 MW; E934C34D7008860E CRC64;
MEASLHFPID ASLRAAVAVI SAGAFYLLNL VIYRLFLSPL AKFPGPKLAA VTSWYELYYD
LVHKGKYLFE IEKMHDKYGP IVRINPFELS IRDSEYYDEL YVAGSVRPTD RYEAFVEGIV
DFKGSHIATI EHDLHRKRRK PLDPYFSRLG VSRLEPMLGE LTEKLIVNRF ESFKRTGKVV
RLDHAFTAYS GDVINRLCMD DPPDVLVDDP EFSPWWYNMF HNGIATLPLF MGLPWLIHVV
RLIPVSILAK LDPGTQTFNK FKMMCDDHLR VAKREKAAQG SKDTSMMDAR PTIFRHLLNS
DLPPSELTDD LLSKEAQVLI GTGTITTAGS LCFICYHIVV NPAIKKRLQE DLKLIMANYP
AKKPTWAELE TATYLQAVIK EGLRLSFGTM HRRTRVSPKQ PLQFRQWTIP AGVPVGMSAY
YAHRDPSVFP RPDEFLPERW LSNVTPEMSR NYVPFSRGSR RCLGMNLAYA EINHVIATLF
RPGGPDFKLY ETSEKDVKPA HDLIVPLPSL ESKGFRVIFR
