PRDS_PENRF
ID PRDS_PENRF Reviewed; 742 AA.
AC W6QAE7;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Conidiogenone synthase {ECO:0000303|PubMed:30343633};
DE AltName: Full=Bifunctional terpene synthase PrDS {ECO:0000303|PubMed:30343633};
DE Short=BFTS PrDS {ECO:0000303|PubMed:30343633};
DE AltName: Full=Conidiogenone biosynthesis cluster protein PrDS {ECO:0000303|PubMed:30343633};
DE AltName: Full=Diterpene synthase PrDS {ECO:0000303|PubMed:30343633};
DE Short=DS {ECO:0000303|PubMed:30343633};
DE Includes:
DE RecName: Full=Terpene cyclase {ECO:0000303|PubMed:30343633};
DE EC=4.2.3.- {ECO:0000269|PubMed:30343633};
DE Includes:
DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:30343633};
DE Short=GGDP synthase {ECO:0000303|PubMed:30343633};
DE Short=GGS {ECO:0000303|PubMed:30343633};
DE EC=2.5.1.29 {ECO:0000269|PubMed:30343633};
GN Name=PrDS {ECO:0000303|PubMed:30343633}; ORFNames=PROQFM164_S02g003147;
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164;
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=30343633; DOI=10.1080/09168451.2018.1536518;
RA Shiina T., Nakagawa K., Fujisaki Y., Ozaki T., Liu C., Toyomasu T.,
RA Hashimoto M., Koshino H., Minami A., Kawaide H., Oikawa H.;
RT "Biosynthetic study of conidiation-inducing factor conidiogenone:
RT heterologous production and cyclization mechanism of a key bifunctional
RT diterpene synthase.";
RL Biosci. Biotechnol. Biochem. 83:192-201(2019).
CC -!- FUNCTION: Bifunctional terpene synthase; part of the gene cluster that
CC mediates the biosynthesis of conidiogenone, a diterpene known to induce
CC the conidiation (PubMed:30343633). The bifunctional terpene synthase
CC PrDS converts isopentenyl diphosphate (IPP) and dimethylallyl
CC diphosphate (DMAPP) into deoxyconidiogenol (PubMed:30343633). The C-
CC terminal prenyltransferase (PT) domain of PrDS catalyzes formation of
CC GGPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the
CC cyclization of GGPP into deoxyconidiogenol (PubMed:30343633). The
CC cytochrome P450 monooxygenase PrP450 then catalyzes two rounds of
CC oxidation to furnish conidiogenone (PubMed:30343633).
CC {ECO:0000269|PubMed:30343633}.
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:30343633};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC Evidence={ECO:0000269|PubMed:30343633};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WEV7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:30343633}.
CC -!- SUBUNIT: Hexamer. {ECO:0000250|UniProtKB:A2PZA5}.
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:A1DN30}.
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; HG792016; CDM32996.1; -; Genomic_DNA.
DR SMR; W6QAE7; -.
DR STRING; 1365484.W6QAE7; -.
DR EnsemblFungi; CDM32996; CDM32996; PROQFM164_S02g003147.
DR OrthoDB; 981769at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000030686; 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 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; Repeat; Transferase.
FT CHAIN 1..742
FT /note="Conidiogenone synthase"
FT /id="PRO_0000453705"
FT REGION 1..332
FT /note="Terpene cyclase"
FT /evidence="ECO:0000250|UniProtKB:B6HFX8"
FT REGION 333..742
FT /note="Prenyltransferase"
FT /evidence="ECO:0000250|UniProtKB:B6HFX8"
FT REGION 701..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 97..101
FT /note="DDXXD 1"
FT /evidence="ECO:0000250|UniProtKB:A1DN30"
FT MOTIF 234..242
FT /note="NSE/DTE"
FT /evidence="ECO:0000250|UniProtKB:A1DN30"
FT MOTIF 453..457
FT /note="DDXXD 2"
FT /evidence="ECO:0000250|UniProtKB:A1DN30"
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 190..193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 238..242
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 328..329
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 414
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 417
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 446
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 457
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 457
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 462
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 463
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 539
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 540
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 575
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 582
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 592
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 602
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 742 AA; 83624 MW; 803F47576B24EC18 CRC64;
MGETIADVYA ESIDPEIYAN NPAYSSLFTP YIHKQTIIAD HVSVQCHIDL NGIDAVGSKF
GNLNAHAGNF TSLCAPNCLP ERLALVAYTV EYAFLHDDET DNAADQEALL LENKMLHQAI
NQSSMTSVSN RVSAKAQRKS EVQAKIAAEY LRLDPVFGEF FLKAWQTFTA SVQDVRSLEF
PSLDDYLEFR IVDAAADWTL YNFRWGSGIT LTPEEEKIAD PMSYVAYAEL CLVNDLFSWD
KEYDAHVKSN GEVPLVNAVH IVAVTQGLTH CAAKAVVQAE IRAHEERFCY LKEQYKATAS
PSDSILSWLK LLEHSMAGNW VWSLCVPRYF KVERNPYKDH LEKFGSEAVR VLTPEEHLRD
SKQEINGTKE IELQEPKSNN TAESDVLAKY TSGYPTIDEP VLNPYTYINS LPSKNVRQTM
IAALNSWYKV PVKSLLIIEG AVNFLHNSSL LLDDIQDGSV LRRGRPVAHQ IFGVGQTINT
ATYLMNEALY LVQMLSPSAV LVYTDEMRNL QLGQGRDLHW SYHTHVPTPA QYISMVDGKT
GGLFRLISRL MRSEATVNRD LDISQFATLL GRHFQIRDDY QNLQSDDYTK NKGFCDDLDE
GKLSFPIILS MQSPGFSNTA LSSVFKGSQK GETLSPEMKQ YILEEITARG AFSQTKAVLR
KLHIELLRLL METEQKAGGI ENWALRLLIM KLDLGDEKKK EAHKSDSAWK VNQRRAWKGS
QKNGRPIDKA CFLRAMEEAS QK
