PVCPS_TALVE
ID PVCPS_TALVE Reviewed; 963 AA.
AC A0A348FUE1;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Copalyl diphosphate synthase {ECO:0000303|PubMed:28869716};
DE Short=CPS {ECO:0000303|PubMed:28869716};
DE AltName: Full=Bifunctional diterpene synthase PvCPS {ECO:0000303|PubMed:28869716};
DE Includes:
DE RecName: Full=Type II terpene cyclase {ECO:0000303|PubMed:28869716};
DE EC=5.5.1.12 {ECO:0000269|PubMed:28869716, ECO:0000269|PubMed:31978464};
DE Includes:
DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:28869716};
DE Short=GGDP synthase {ECO:0000303|PubMed:28869716};
DE Short=GGS {ECO:0000303|PubMed:28869716};
DE EC=2.5.1.29 {ECO:0000269|PubMed:28869716, ECO:0000269|PubMed:31978464};
GN Name=PvCPS {ECO:0000303|PubMed:28869716};
OS Talaromyces verruculosus (Penicillium verruculosum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=198730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN, FUNCTION, CATALYTIC ACTIVITY,
RP AND MUTAGENESIS OF ASP-313 AND ASP-727.
RC STRAIN=TPU1311;
RX PubMed=28869716; DOI=10.1002/cbic.201700445;
RA Mitsuhashi T., Okada M., Abe I.;
RT "Identification of chimeric alpha-beta-gamma diterpene synthases possessing
RT both Type II terpene cyclase and prenyltransferase activities.";
RL ChemBioChem 18:2104-2109(2017).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 660-963, SUBUNIT, DOMAIN,
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=31978464; DOI=10.1016/j.jsb.2020.107463;
RA Ronnebaum T.A., Gupta K., Christianson D.W.;
RT "Higher-order oligomerization of a chimeric alpha-beta-gamma bifunctional
RT diterpene synthase with prenyltransferase and class II cyclase activities
RT is concentration-dependent.";
RL J. Struct. Biol. 210:107463-107463(2020).
CC -!- FUNCTION: Bifunctional terpene synthase that possesses both
CC prenyltransferase and type II terpene cyclase activity, converting
CC isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP)
CC into geranylgeranyl diphosphate (GGPP) and further converting GGPP into
CC copalyl diphosphate, respectively. {ECO:0000269|PubMed:28869716,
CC ECO:0000269|PubMed:31978464}.
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:28869716, ECO:0000269|PubMed:31978464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC Evidence={ECO:0000269|PubMed:28869716, ECO:0000269|PubMed:31978464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (+)-copalyl
CC diphosphate; Xref=Rhea:RHEA:24316, ChEBI:CHEBI:58635,
CC ChEBI:CHEBI:58756; EC=5.5.1.12;
CC Evidence={ECO:0000269|PubMed:28869716, ECO:0000269|PubMed:31978464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24317;
CC Evidence={ECO:0000269|PubMed:28869716, ECO:0000269|PubMed:31978464};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for DMAPP (for prenyltransferase activity)
CC {ECO:0000269|PubMed:31978464};
CC KM=190 uM for IPP (for prenyltransferase activity)
CC {ECO:0000269|PubMed:31978464};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:31978464}.
CC -!- DOMAIN: The bifunctional copalyl diphosphate synthase is composed of an
CC N-terminal type II terpene cyclase (TC) catalytic domain and a C-
CC terminal prenyltransferase (PT) catalytic domain which are separated by
CC a linker region. {ECO:0000269|PubMed:28869716}.
CC -!- DOMAIN: The conserved DXDD and DDXXD motifs are important for the
CC catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305|PubMed:28869716, ECO:0000305|PubMed:31978464}.
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; LC316181; BBF88128.1; -; Genomic_DNA.
DR PDB; 6V0K; X-ray; 2.41 A; A/B=660-963.
DR PDB; 7S09; X-ray; 3.10 A; A/B=659-963.
DR PDB; 7S0A; X-ray; 2.80 A; A/B=659-963.
DR PDB; 7S0H; X-ray; 3.15 A; A/B=659-963.
DR PDB; 7S0L; X-ray; 2.65 A; A/B=659-963.
DR PDB; 7S0M; X-ray; 2.00 A; A/B=659-963.
DR PDBsum; 6V0K; -.
DR PDBsum; 7S09; -.
DR PDBsum; 7S0A; -.
DR PDBsum; 7S0H; -.
DR PDBsum; 7S0L; -.
DR PDBsum; 7S0M; -.
DR SMR; A0A348FUE1; -.
DR GO; GO:0016853; F:isomerase 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:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Isoprene biosynthesis; Magnesium; Metal-binding;
KW Multifunctional enzyme; Transferase.
FT CHAIN 1..963
FT /note="Copalyl diphosphate synthase"
FT /id="PRO_0000453797"
FT REGION 1..539
FT /note="Type II terpene cyclase (TC)"
FT /evidence="ECO:0000305|PubMed:28869716,
FT ECO:0000305|PubMed:31978464"
FT REGION 227..292
FT /note="Substrate binding"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT REGION 540..659
FT /note="Linker"
FT /evidence="ECO:0000305|PubMed:28869716,
FT ECO:0000305|PubMed:31978464"
FT REGION 627..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..963
FT /note="Geranylfarnesyl diphosphate synthase (PT)"
FT /evidence="ECO:0000305|PubMed:28869716,
FT ECO:0000305|PubMed:31978464"
FT MOTIF 311..314
FT /note="DXDD"
FT /evidence="ECO:0000305|PubMed:28869716,
FT ECO:0000305|PubMed:31978464"
FT MOTIF 333..341
FT /note="NSE/DTE"
FT /evidence="ECO:0000305|PubMed:28869716,
FT ECO:0000305|PubMed:31978464"
FT MOTIF 727..731
FT /note="DDXXD 1"
FT /evidence="ECO:0000305|PubMed:28869716,
FT ECO:0000305|PubMed:31978464"
FT MOTIF 851..855
FT /note="DDXXD 2"
FT /evidence="ECO:0000305|PubMed:28869716,
FT ECO:0000305|PubMed:31978464"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 337..341
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 521..522
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 688
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 691
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 720
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 727
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 727
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 731
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 731
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 736
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 737
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 814
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 815
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 848
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 855
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 865
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 875
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT MUTAGEN 313
FT /note="D->A: Impairs type II TC activity, but retains the
FT PT activity, producing GGPP."
FT /evidence="ECO:0000269|PubMed:28869716"
FT MUTAGEN 727
FT /note="D->A: Impairs PT, but retains the type II TC
FT activity, converting GGPP into copalyl diphosphate."
FT /evidence="ECO:0000269|PubMed:28869716"
FT HELIX 669..675
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 677..683
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 690..702
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 706..731
FT /evidence="ECO:0007829|PDB:7S0M"
FT STRAND 734..736
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 743..746
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 748..766
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 767..769
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 772..798
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 804..813
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 815..828
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 837..857
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 859..865
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 869..872
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 878..886
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 892..899
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 904..916
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 919..943
FT /evidence="ECO:0007829|PDB:7S0M"
FT HELIX 950..959
FT /evidence="ECO:0007829|PDB:7S0M"
SQ SEQUENCE 963 AA; 108180 MW; E863C6B3F07E2318 CRC64;
MSPMDLQESA AALVRQLGER VEDRRGFGFM SPAIYDTAWV SMISKTIDDQ KTWLFAECFQ
YILSHQLEDG GWAMYASEID AILNTSASLL SLKRHLSNPY QITSITQEDL SARINRAQNA
LQKLLNEWNV DSTLHVGFEI LVPALLRYLE DEGIAFAFSG RERLLEIEKQ KLSKFKAQYL
YLPIKVTALH SLEAFIGAIE FDKVSHHKVS GAFMASPSST AAYMMHATQW DDECEDYLRH
VIAHASGKGS GGVPSAFPST IFESVWPLST LLKVGYDLNS APFIEKIRSY LHDAYIAEKG
ILGFTPFVGA DADDTATTIL VLNLLNQPVS VDAMLKEFEE EHHFKTYSQE RNPSFSANCN
VLLALLYSQE PSLYSAQIEK AIRFLYKQFT DSEMDVRDKW NLSPYYSWML MTQAITRLTT
LQKTSKLSTL RDDSISKGLI SLLFRIASTV VKDQKPGGSW GTRASKEETA YAVLILTYAF
YLDEVTESLR HDIKIAIENG CSFLSERTMQ SDSEWLWVEK VTYKSEVLSE AYILAALKRA
ADLPDENAEA APVINGISTN GFEHTDRING KLKVNGTNGT NGSHETNGIN GTHEIEQING
VNGTNGHSDV PHDTNGWVEE PTAINETNGH YVNGTNHETP LTNGISNGDS VSVHTDHSDS
YYQRSDWTAD EEQILLGPFD YLESLPGKNM RSQLIQSFNT WLKVPTESLD VIIKVISMLH
TASLLIDDIQ DQSILRRGQP VAHSIFGTAQ AMNSGNYVYF LALREVQKLQ NPKAISIYVD
SLIDLHRGQG MELFWRDSLM CPTEEQYLDM VANKTGGLFC LAIQLMQAEA TIQVDFIPLV
RLLGIIFQIC DDYLNLKSTA YTDNKGLCED LTEGKFSFPI IHSIRSNPGN RQLINILKQK
PREDDIKRYA LSYMESTNSF EYTRGVVRKL KTEAIDTIQG LEKHGLEENI GIRKILARMS
LEL
