OBLC_COCH5
ID OBLC_COCH5 Reviewed; 483 AA.
AC M2URK9;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=FAD-dependent oxidoreductase oblC {ECO:0000303|PubMed:27116000};
DE EC=1.21.-.- {ECO:0000305|PubMed:27116000};
DE AltName: Full=Ophiobolin biosynthesis cluster protein C {ECO:0000303|PubMed:27116000};
DE Flags: Precursor;
GN Name=oblC {ECO:0000303|PubMed:27116000}; ORFNames=COCHEDRAFT_1167272;
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, 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: FAD-dependent oxidoreductase; 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:B8NI10};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:27116000}.
CC -!- SIMILARITY: Belongs to the beta-cyclopiazonate dehydrogenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB445570; EMD96236.1; -; Genomic_DNA.
DR AlphaFoldDB; M2URK9; -.
DR SMR; M2URK9; -.
DR EnsemblFungi; EMD96236; EMD96236; COCHEDRAFT_1167272.
DR eggNOG; ENOG502R1TU; Eukaryota.
DR HOGENOM; CLU_028280_0_0_1; -.
DR OMA; EWHSHAP; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000016936; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..483
FT /note="FAD-dependent oxidoreductase oblC"
FT /id="PRO_5004027862"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 483 AA; 52924 MW; 307C83AFD19F2CC9 CRC64;
MRSVTSLVSF SACLLASSVT AADTPLTVNG KKFYSQDIIT RDVVVVGGGS SGCHIAVRLQ
DAGKSVVVVE KSARLGGHVA TYTDPATRKT AEQGLVTFHN TTHVTDYLTR LDIPLAPISF
SPSTNFDYDL RTGKPVNRTY NPTQEEFAAG FAGYSAQLAK YPQLNDGTFL PYPVPEDLTM
PFGKFLEKYN LTGALMQMYN FNWGTGNFLT NPTVEQMRYW GANTVAAVTT GKFLVTARHN
SSEIYTKVGN VLGATSSVLL NSEVTYTRRS EGKTGVQLIV KTPEGSKLLV AKKLVIAIPP
KLDFVAPLDL SKTEKDLFGK YIDAGYYVGM VRNTGIPART LITNSAQDTP YNLPVLPAVN
IMNPTAIDGV WTVFSSSLQS KASFPWADDA VKADIIRSIK ALQTANPDKF QQTEPEIIEW
HSHAPYFLQV SSEEIKNGFY AKLYALQGLR NTHFTGAAWR VHDSSQIWKY TDTQVLPKLL
AGL
