OBLA_COCH5
ID OBLA_COCH5 Reviewed; 721 AA.
AC M2V8C1;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Ophiobolin F synthase oblA {ECO:0000303|PubMed:27116000};
DE AltName: Full=Bifunctional sesterterpene synthase oblA {ECO:0000303|PubMed:27116000};
DE AltName: Full=Ophiobolin biosynthesis cluster protein A {ECO:0000303|PubMed:27116000};
DE Includes:
DE RecName: Full=Ophiobolin F cyclase {ECO:0000303|PubMed:27116000};
DE EC=4.2.3.145 {ECO:0000269|PubMed:27116000};
DE Includes:
DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:27116000};
DE Short=GGDP synthase {ECO:0000303|PubMed:27116000};
DE Short=GGS {ECO:0000303|PubMed:27116000};
DE EC=2.5.1.29 {ECO:0000269|PubMed:27116000};
DE Includes:
DE RecName: Full=Geranylfarnesyl diphosphate synthase {ECO:0000303|PubMed:27116000};
DE Short=GFDP synthase {ECO:0000303|PubMed:27116000};
DE EC=2.5.1.81 {ECO:0000269|PubMed:27116000};
GN Name=oblA {ECO:0000303|PubMed:27116000}; ORFNames=COCHEDRAFT_1167261;
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: Bifunctional sesterterpene synthase; part of the gene cluster
CC that mediates the biosynthesis of the sesterterpenes ophiobolins,
CC fungal phytotoxins with potential anti-cancer activities
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 (By
CC similarity). Other sesterterpenoids (C(25) terpenoids) are found as
CC minor products of oblA (By similarity). The cytochrome P450
CC monooxygenase oblB then catalyzes a four-step oxidative transformation
CC of ophiobolin F to yield ophiobolin C (PubMed:27116000). The FAD-
CC dependent oxidoreductase oblC might be involved in a later oxidation
CC step that produces ophiobolin A (Probable).
CC {ECO:0000250|UniProtKB:A1C8C3, ECO:0000269|PubMed:27116000,
CC ECO:0000305|PubMed:27116000}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate =
CC (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate;
CC Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
CC Evidence={ECO:0000269|PubMed:27116000};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC Evidence={ECO:0000269|PubMed:27116000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl
CC diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate +
CC diphosphate; Xref=Rhea:RHEA:25694, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57907, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769;
CC EC=2.5.1.81; Evidence={ECO:0000269|PubMed:27116000};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25695;
CC Evidence={ECO:0000269|PubMed:27116000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E,14E)-geranylfarnesyl diphosphate + H2O =
CC diphosphate + ophiobolin F; Xref=Rhea:RHEA:41552, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57907, ChEBI:CHEBI:78293;
CC EC=4.2.3.145; Evidence={ECO:0000269|PubMed:27116000};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41553;
CC Evidence={ECO:0000269|PubMed:27116000};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q12051,
CC ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 4 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051,
CC ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:27116000}.
CC -!- DOMAIN: The conserved DDXXD motifs as well as the NSE/DTE motif are
CC important for the catalytic activity, presumably through binding to
CC Mg(2+). {ECO:0000250|UniProtKB:A1C8C3}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the terpene synthase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the FPP/GGPP synthase
CC family. {ECO:0000305}.
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DR EMBL; KB445570; EMD96232.1; -; Genomic_DNA.
DR AlphaFoldDB; M2V8C1; -.
DR SMR; M2V8C1; -.
DR STRING; 701091.M2V8C1; -.
DR EnsemblFungi; EMD96232; EMD96232; COCHEDRAFT_1167261.
DR eggNOG; KOG0777; Eukaryota.
DR HOGENOM; CLU_014015_10_0_1; -.
DR OMA; WHGLVTF; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000016936; Unassembled WGS sequence.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044687; F:geranylfarnesyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 2.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 2.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW Isoprene biosynthesis; Lyase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Reference proteome; Transferase.
FT CHAIN 1..721
FT /note="Ophiobolin F synthase oblA"
FT /id="PRO_0000451167"
FT REGION 5..325
FT /note="(7Z)-ophiobola-7,19-dien-3-ol synthase"
FT /evidence="ECO:0000250|UniProtKB:A1C8C3"
FT REGION 326..721
FT /note="Geranylfarnesyl diphosphate synthase"
FT /evidence="ECO:0000250|UniProtKB:A1C8C3"
FT REGION 348..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 97..101
FT /note="DDXXD 1"
FT /evidence="ECO:0000250|UniProtKB:A1C8C3"
FT MOTIF 229..237
FT /note="NSE/DTE"
FT /evidence="ECO:0000250|UniProtKB:A1C8C3"
FT MOTIF 471..475
FT /note="DDXXD 2"
FT /evidence="ECO:0000250|UniProtKB:A1C8C3"
FT COMPBIAS 356..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 185..188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 233..237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 316..317
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 432
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 435
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 464
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 480
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 481
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 558
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 559
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 597
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 604
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 614
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 624
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 721 AA; 81421 MW; B4D6700603312610 CRC64;
MAPSYDQPYS VLLDRNIYDP DNLCEGIDLR RHHAADLEDV GAFRCQEDWR RLVGPLERPF
RGGLGPQFSF ITVAVPNCIP ERMEITSYAL EFGFIHDDVI DEHIEDADLS DMEEGLEQGA
KTGSIDERGA SGKRVIAAQI MREMMAIDPE RAMVVAKSWA AGVQHSARRE ELTNFQTLDE
YIPYRSLDVG YMLWHGLVTF GCAITIPPEE EALCTEFLTP ALCAASLVND LFSFEKEKND
ANIQNAVYIV MKEHGCDEAE GRERLKARIR QEMAKFVQIV KDTKTRSDLS DDTKRYIDVM
QYTLSGNVVW SAQCPRYNLK AEWNELQMLR AKHGVAKYPA TFPPADGSMD HIWKKGSTQG
ESKGEKRKRQ SVNGTNGVNG TNGVKKPTIS RVGVDSLQLN EVVSLALSTD LPNLTTDVVL
QPYAYITSMP SKGFRDQAVD SINNWLKTPA KATKKIKEII NMLHTASLML DDLEDNSPLR
RGKPSTHNVY GASQTINSAT YQFTHATALA AGLSNPDCLR IFNEEINELY VGQSYDLYWT
HNIICPTFGE YLRMVDMKTG GLFRMLTRLM TAESPLNGQI SDSELNPLGC LIGRFFQIRD
DYQNLVSAEY AQQKGFAEDL DEGKYSFTLI HCIRTLEANP SLAGEQMQLR ALLMKRRVEG
KLTNEAKREI LDTMKKTQSL EYTLEVLREL HTKLDNEVGR LEKKFGDDNF ALRLMMEMLK
V
