OBLA_ASPCI
ID OBLA_ASPCI Reviewed; 725 AA.
AC A0A0U5G0B1;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Ophiobolin F synthase {ECO:0000303|PubMed:32725018};
DE Short=OS {ECO:0000303|PubMed:32725018};
DE AltName: Full=Aspergilol biosynthesis cluster protein AuAS {ECO:0000303|PubMed:32725018};
DE Includes:
DE RecName: Full=Ophiobolin F cyclase {ECO:0000303|PubMed:32725018};
DE EC=4.2.3.145 {ECO:0000269|PubMed:32725018};
DE Includes:
DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:32725018};
DE Short=GGDP synthase {ECO:0000303|PubMed:32725018};
DE Short=GGS {ECO:0000303|PubMed:32725018};
DE EC=2.5.1.29 {ECO:0000269|PubMed:32725018};
DE Includes:
DE RecName: Full=Geranylfarnesyl diphosphate synthase;
DE Short=GFDP synthase {ECO:0000303|PubMed:32725018};
DE EC=2.5.1.81 {ECO:0000269|PubMed:32725018};
GN Name=AcldOS {ECO:0000303|PubMed:32725018}; ORFNames=ASPCAL05226;
OS Aspergillus calidoustus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=454130;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF006504;
RX PubMed=26966204; DOI=10.1128/genomea.00102-16;
RA Horn F., Linde J., Mattern D.J., Walther G., Guthke R., Scherlach K.,
RA Martin K., Brakhage A.A., Petzke L., Valiante V.;
RT "Draft genome sequences of fungus Aspergillus calidoustus.";
RL Genome Announc. 4:0-0(2016).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN.
RX PubMed=32725018; DOI=10.1039/d0ob01470b;
RA Quan Z., Dickschat J.S.;
RT "On the mechanism of ophiobolin F synthase and the absolute configuration
RT of its product by isotopic labelling experiments.";
RL Org. Biomol. Chem. 18:6072-6076(2020).
CC -!- FUNCTION: Bifunctional sesterterpene synthase that converts isopentenyl
CC diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into ophiobolin
CC F (PubMed:32725018). The C-terminal prenyltransferase (PT) domain of
CC AcldOS converts isopentenyl diphosphate and dimethylallyl diphosphate
CC into geranylfarnesyl diphosphate (GFPP), whereas the N-terminal terpene
CC cyclase (TC) domain catalyzes the cyclization of GFPP to ophiobolin F
CC (PubMed:32725018). {ECO:0000269|PubMed:32725018}.
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:32725018};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC Evidence={ECO:0000269|PubMed:32725018};
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:32725018};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25695;
CC Evidence={ECO:0000269|PubMed:32725018};
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:32725018};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41553;
CC Evidence={ECO:0000269|PubMed:32725018};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q12051};
CC Note=Binds 4 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:32725018}.
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:0000305|PubMed:32725018}.
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; CDMC01000004; CEL04094.1; -; Genomic_DNA.
DR SMR; A0A0U5G0B1; -.
DR STRING; 454130.A0A0U5G0B1; -.
DR EnsemblFungi; CEL04094; CEL04094; ASPCAL05226.
DR OrthoDB; 981769at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000054771; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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; Repeat; Transferase.
FT CHAIN 1..725
FT /note="Ophiobolin F synthase"
FT /id="PRO_0000453703"
FT REGION 1..322
FT /note="(7Z)-ophiobola-7,19-dien-3-ol synthase"
FT /evidence="ECO:0000250|UniProtKB:A1C8C3"
FT REGION 323..725
FT /note="Geranylfarnesyl diphosphate synthase"
FT /evidence="ECO:0000250|UniProtKB:A1C8C3"
FT REGION 362..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 93..97
FT /note="DDXXD 1"
FT /evidence="ECO:0000250|UniProtKB:A1DN30"
FT MOTIF 226..234
FT /note="NSE/DTE"
FT /evidence="ECO:0000250|UniProtKB:A1DN30"
FT MOTIF 475..479
FT /note="DDXXD 2"
FT /evidence="ECO:0000250|UniProtKB:A1DN30"
FT COMPBIAS 369..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
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 182..185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 230..234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 313..314
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 436
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 439
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 468
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
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 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 484
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 485
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 562
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 563
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 601
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 608
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 618
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 628
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 725 AA; 82262 MW; 6E011D41B084ADA5 CRC64;
MEYKYSTIVD SSKWDPEGLI EGIPLRKHEA GDLEEVGSFR VQEDWRRLVG PVENPFRGSL
GPEISFITYT VPECLPERLE AISYGLDYGF LHDDEIDTKI EEAELDDVGA ALAQGGSTGK
IQEGTKSSGK RKMAAQLLRE MMALDPERAM TLAKSWAQGV QHSARRVEEK DWKSLDEYIP
FRCMDLGYMH WHGLVTFGCA ITVPEEEEEE RRTLLEPAVI ACLMTNDLFS YEKEKNDNNP
QNAVAVIMKI HKCSEEEARD ICKQRIRLEC RKYARIVKET LARTDISLDL KRYIEIMQYT
VSGNWAWSTQ CPRYHADAKF NELQMLRAEH GVAKYPARYS LENRKNGANG VNGVNGINGV
NGVNGVNGKR KRSGEETADD ARTNGNGIKK PAHVLEYRDS LVLEDIVALS LDWNLPDLSD
GVVVQPYKYL TSLPSKGFRD QAIDSLNTWL RVPTKTTKMI KDVIKMLHSA SLMLDDIEDN
SPLRRGKPST HVIYGNAQTI NSATYQYTEA TGLAARLPNP TSLRIYLEEV QQLYIGQSYD
LYWTHNALCP SIPEYLKMVD QKTGGLFRML TRLMVSESPA RSSILDQTLY PLSHLIGRFF
QIRDDYQNLA SAEYARQKGY AEDLDEGKYS FTLIHCINTL EAEASLASEK MALRAFLIKR
RVDSSLSNES KREVLDIMKK TKSLEYTLGV LRALQAELEK EVDSLEAKFG EENFSLRMML
ELLKV
