OBLB_COCH5
ID OBLB_COCH5 Reviewed; 524 AA.
AC M2V933;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 37.
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=COCHEDRAFT_1201083;
OS Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=701091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O;
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O;
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(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: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 FAD-dependent oxidoreductase oblC
CC might be involved in a later oxidation step that produces ophiobolin A
CC (Probable). {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; KB445570; EMD96233.1; -; Genomic_DNA.
DR AlphaFoldDB; M2V933; -.
DR SMR; M2V933; -.
DR EnsemblFungi; EMD96233; EMD96233; COCHEDRAFT_1201083.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_14_4_1; -.
DR OMA; RLSYGVM; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000016936; 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..524
FT /note="Cytochrome P450 monooxygenase oblB"
FT /id="PRO_0000451170"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 466
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 524 AA; 59684 MW; CD479B64C6B61296 CRC64;
MSSIQLQKYL DLLPENAILN AGIAIAGLSA AYAIGLVIYR LYLSPISKFP GPKIAAATFW
YELYYDVIHK GQYFHKIEEM HEKYGPIVRI NPHELSIRDP DYYDELYVSG SVRPSDRYEG
FVNGVVDFEG SHLATVAHEL HRKRRKPLDP YFSRAGVNRL EPMVADLTEE LVVKRFEEFK
GTGKVVRLDH AFTAYSGDII SALCIDEPPH FTSTPDFTPS WFDLFHSGVV TLPLFMGLPW
LIHLIRLIPE SILAVIDPGA QNWNTFRMMC YDSIKDTKRE KGAQPTKDTS LLGRPTLFRH
LVNSDLPASE LSDERLLREA QVLIGSGTMT TAGTMCFLVY YIKSNPEIHR RLTEELKPIM
EGYPHKKPSW AEIEKAEYLQ AVLKEGLRLS FGTIHRRPRV SPNQPLQFKE WVIPAGVPVG
MSAYFQHTDP KIFPNPHEFN PDRWLSNVTP AMKKNYVPFS KGSRHCLGMN LAYCELNYII
ATMFRPGAVD FDLFETTELD VKPTHDMVVP LPSLKSKGFK VKFN
