PCHDS_PENRW
ID PCHDS_PENRW Reviewed; 732 AA.
AC B6HFX8;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Conidiogenone synthase {ECO:0000303|PubMed:30343633};
DE AltName: Full=Bifunctional terpene synthase PchDS {ECO:0000303|PubMed:30343633};
DE Short=BFTS PchDS {ECO:0000303|PubMed:30343633};
DE AltName: Full=Conidiogenone biosynthesis cluster protein PchDS {ECO:0000303|PubMed:30343633};
DE AltName: Full=Diterpene synthase PchDS {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=PchDS {ECO:0000303|PubMed:30343633};
GN ORFNames=Pc20g10860, PCH_Pc20g10860;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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 PchDS converts isopentenyl diphosphate (IPP) and dimethylallyl
CC diphosphate (DMAPP) into deoxyconidiogenol (PubMed:30343633). The C-
CC terminal prenyltransferase (PT) domain of PchDS 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 PchP450 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; AM920435; CAP86415.1; -; Genomic_DNA.
DR RefSeq; XP_002563575.1; XM_002563529.1.
DR SMR; B6HFX8; -.
DR STRING; 1108849.XP_002563575.1; -.
DR EnsemblFungi; CAP86415; CAP86415; PCH_Pc20g10860.
DR GeneID; 8308896; -.
DR KEGG; pcs:Pc20g10860; -.
DR VEuPathDB; FungiDB:PCH_Pc20g10860; -.
DR eggNOG; KOG0777; Eukaryota.
DR HOGENOM; CLU_014015_10_0_1; -.
DR OMA; HITHYIG; -.
DR OrthoDB; 981769at2759; -.
DR BioCyc; PCHR:PC20G10860-MON; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000000724; Contig Pc00c20.
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..732
FT /note="Conidiogenone synthase"
FT /id="PRO_0000453704"
FT REGION 1..311
FT /note="Terpene cyclase"
FT /evidence="ECO:0000305|PubMed:30343633"
FT REGION 312..732
FT /note="Prenyltransferase"
FT /evidence="ECO:0000305|PubMed:30343633"
FT REGION 348..370
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 213..221
FT /note="NSE/DTE"
FT /evidence="ECO:0000250|UniProtKB:A1DN30"
FT MOTIF 441..445
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 169..172
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 217..221
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 307..308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 402
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 405
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 434
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 441
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 441
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 445
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 445
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 450
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 451
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 529
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 530
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 565
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 572
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"
SQ SEQUENCE 732 AA; 82997 MW; FFC38EA978D574D2 CRC64;
MADKITDEYA VGIDPEIYAN NPAYSSLFNP YIHKQTIIAD HVSVQCHIDL NGIDAVGSKF
GNLNAHAGNF TSLCAPNCLP ERFALVAYTV EYAFLHDALN QSGMTSVSTR VSDKAQRKSE
VQAKIAAEYL RLDPVFGEWF LNKWQTFTAC VKDVRSLEFP SLDDYLEFRI VDAAADWTLY
NFRWGSGITL TPEEEKIADP MSYVAYAELC LVNDLFSWDK EYASHIKSNG DVPLVNAVHI
VAVTQGLTHC AAKAVVQAEV RAHEERFCQL KEQYEATDKP SHEVLRWLRL LEHSMAGNWV
WSLCVPRYCK VDRNPYKDHL EKYGSDAVRV LTPLDRLCWP KQEIKDMKQS ELKDPSSSTY
KSHFSPLEPN PGPEQMRLTI SQTQQQRPVL NPYTYINSLP SKNVRQTLIA ALNSWYKVPV
KSLLIIEGAV NFLHNSSLLL DDIQDGSFLR RGRPVAHQIF GVGQTINTAT YLMNEALYLI
QMLSPSAVSV YTEIDEMRNL QLGQGRDLYW SYHTHVPTPA QYISMVDGKT GGLFRLISRL
MRSEATKNSD LDISQFATLL GRHFQIRDDY QNLQSEDYTK NKGFCDDLDE GKLSFPIILS
MQSPGFSNTA LSSVFKGSQK GQTLSLEMKQ YMLEEITARG AFSETKAVLR KLHTELLRLL
IETEKKAGGV ENWALRLLIM KLDIAEEKKV APPKSDSHWG VNQRRAWKGC QKNGRPIDKA
CFLRAMEETL QK
