PCCS_PENCH
ID PCCS_PENCH Reviewed; 770 AA.
AC A0A348DU52;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Cyclopiane-type diterpene synthase {ECO:0000303|PubMed:30179018};
DE Short=CS {ECO:0000303|PubMed:30179018};
DE Includes:
DE RecName: Full=Terpene cyclase {ECO:0000303|PubMed:30179018};
DE EC=4.2.3.- {ECO:0000269|PubMed:30179018};
DE Includes:
DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:30179018};
DE Short=GGDP synthase {ECO:0000303|PubMed:30179018};
DE Short=GGS {ECO:0000303|PubMed:30179018};
DE EC=2.5.1.29 {ECO:0000269|PubMed:30179018};
GN Name=PcCS {ECO:0000303|PubMed:30179018};
OS Penicillium chrysogenum (Penicillium notatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=5076;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DOMAIN, CATALYTIC ACTIVITY,
RP AND PATHWAY.
RC STRAIN=MT-12;
RX PubMed=30179018; DOI=10.1021/acs.orglett.8b02284;
RA Mitsuhashi T., Kikuchi T., Hoshino S., Ozeki M., Awakawa T., Shi S.P.,
RA Fujita M., Abe I.;
RT "Crystalline sponge method enabled the investigation of a
RT prenyltransferase-terpene synthase chimeric enzyme, whose product exhibits
RT broadened NMR Signals.";
RL Org. Lett. 20:5606-5609(2018).
CC -!- FUNCTION: Bifunctional terpene synthase converts DMAPP and IPP, and
CC also GGPP, into a cyclopiane-type diterpene (PubMed:30179018). The C-
CC terminal prenyltransferase (PT) domain of PcCS catalyzes formation of
CC GGPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the
CC cyclization of GGPP to the cyclopiane-type diterpene (PubMed:30179018).
CC {ECO:0000269|PubMed:30179018}.
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:30179018};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC Evidence={ECO:0000269|PubMed:30179018};
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:30179018}.
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:0000305|PubMed:30179018}.
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; LC411963; BBF45518.1; -; Genomic_DNA.
DR SMR; A0A348DU52; -.
DR UniPathway; UPA00213; -.
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; Repeat; Transferase.
FT CHAIN 1..770
FT /note="Cyclopiane-type diterpene synthase"
FT /id="PRO_0000453638"
FT REGION 5..335
FT /note="Terpene cyclase"
FT /evidence="ECO:0000305|PubMed:30179018"
FT REGION 336..720
FT /note="Prenyltransferase"
FT /evidence="ECO:0000305|PubMed:30179018"
FT REGION 371..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 97..101
FT /note="DDXXD 1"
FT /evidence="ECO:0000305|PubMed:30179018"
FT MOTIF 234..242
FT /note="NSE/DTE"
FT /evidence="ECO:0000305|PubMed:30179018"
FT MOTIF 462..466
FT /note="DDXXD 2"
FT /evidence="ECO:0000305|PubMed:30179018"
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 101
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 423
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 426
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 455
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 471
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 472
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 548
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 549
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 584
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 591
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 620
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 630
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 770 AA; 87136 MW; A926747B28F70C65 CRC64;
MADKITDEYA VGIDPEIYAN NPAYSSLFNP YIHKQTIIAD HVSVQCHIDL NGIDAVGSKF
GNLNAHAGNF TSLCAPNCLP ERFALVAYTV EYAFLHDDET DNAADQEALL LENKMLHQAL
NQSGMTSVST RVSDKAQRKS EVQAKIAAEY LRLDPVFGEW FLNKWQTFTA CVKDVRSLEF
PSLDDYLEFR IVDAAADWTL YNFRWGSGIT LTPEEEKLAD PMSYVAYAEL CLVNDLFSWD
KEYASHIKSN GDVPLVNAVH IVAVTQGLTH CAAKAVVQAE VRAHEERFCQ LKEQYEATDK
PSHEVLRWLR LLEHSMAGNW VWSLCVPRYC KVDRNPYKDH LEKYGSDAVR VLTPLDRLCW
SKQEIKEMKR NQLKEPSSST YKTHFSPLEP NPGPEQTRLT ISQTQQQRPV LNPYTYINSL
PSKNVRQTLI AALNSWYKVP VKSLLIIEGA VNFLHNSSLL LDDIQDGSVL RRGRPVAHQI
FGVGQTINTA TYLMNEALYL IQMLSPSAVS AYTDEMRNLQ LGQGRDLYWS YHTHVPTPAQ
YISMVDGKTG GLFRLISRLM RSEATKNSDL DISQFATLLG RHFQIRDDYQ NLQSEDVTNP
HIVSLYAPRA NMLLQYTKNK GFCDDLDEGK VSFPVILSMQ SPGFSNTALS SVFKGSRKGE
TLSLEMKQYM LEEITARGAF SETKAVLRKL HTELLSLLME TEKKAGGVEN WALRLLIMKL
DIVEEKKVAP PKSDSHWGVN QRRAWKGGQK NGRPIDKACF LRAMEEALQK
