PBSS_PENBI
ID PBSS_PENBI Reviewed; 732 AA.
AC A0A2Z6AQX7;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Sesterbrasiliatriene synthase PbSS {ECO:0000303|PubMed:28671289};
DE AltName: Full=Bifunctional sesterterpene synthase PbSS {ECO:0000303|PubMed:28671289};
DE Short=SS {ECO:0000303|PubMed:28671289};
DE Includes:
DE RecName: Full=Sesterbrasiliatriene cyclase {ECO:0000303|PubMed:28671289};
DE EC=4.2.3.- {ECO:0000269|PubMed:28671289};
DE Includes:
DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:28671289};
DE Short=GGDP synthase {ECO:0000303|PubMed:28671289};
DE Short=GGS {ECO:0000303|PubMed:28671289};
DE EC=2.5.1.29 {ECO:0000269|PubMed:28671289};
DE Includes:
DE RecName: Full=Geranylfarnesyl diphosphate synthase {ECO:0000303|PubMed:28671289};
DE Short=GFDP synthase {ECO:0000303|PubMed:28671289};
DE EC=2.5.1.81 {ECO:0000269|PubMed:28671289};
GN Name=PbSS;
OS Penicillium brasilianum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=104259;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 22354 / NBRC 6234 / CBS 338.59 / FRR 3454 / IMI 68220;
RX PubMed=28671289; DOI=10.1002/chem.201702766;
RA Mitsuhashi T., Rinkel J., Okada M., Abe I., Dickschat J.S.;
RT "Mechanistic Characterization of Two Chimeric Sesterterpene Synthases from
RT Penicillium.";
RL Chemistry 23:10053-10057(2017).
CC -!- FUNCTION: Bifunctional sesterterpene synthase that possesses both
CC prenyl transferase and terpene cyclase activity, converting isopentenyl
CC diphosphate and dimethylallyl diphosphate into geranylfarnesyl
CC diphosphate (GFPP) and further converting GFPP into
CC sesterbrasiliatriene. {ECO:0000269|PubMed:28671289}.
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:28671289};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC Evidence={ECO:0000269|PubMed:28671289};
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:28671289};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25695;
CC Evidence={ECO:0000269|PubMed:28671289};
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:28671289}.
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:P9WEV6}.
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; LC228601; BBD05404.1; -; Genomic_DNA.
DR SMR; A0A2Z6AQX7; -.
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 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.
PE 1: Evidence at protein level;
KW Isoprene biosynthesis; Lyase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Repeat; Transferase.
FT CHAIN 1..732
FT /note="Sesterbrasiliatriene synthase PbSS"
FT /id="PRO_0000453790"
FT REGION 1..342
FT /note="Terpene cyclase"
FT /evidence="ECO:0000305|PubMed:28671289"
FT REGION 343..732
FT /note="Prenyltransferase"
FT /evidence="ECO:0000305|PubMed:28671289"
FT REGION 371..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 105..109
FT /note="DDXXD 1"
FT /evidence="ECO:0000250|UniProtKB:P9WEV6"
FT MOTIF 238..246
FT /note="NSE/DTE"
FT /evidence="ECO:0000250|UniProtKB:P9WEV6"
FT MOTIF 492..496
FT /note="DDXXD 2"
FT /evidence="ECO:0000250|UniProtKB:P9WEV6"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 193..196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 242..246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 334..335
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 453
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 456
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
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 492
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 492
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 496
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 496
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 501
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 502
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 579
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 580
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 615
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 622
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 632
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 642
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 732 AA; 83177 MW; EB67FD9CBD4A3F3A CRC64;
MDFLSGAFHY SDSVNPSKYS PRPSDYFGTL PFRTSRFERE AADVTADYLR KWQKAVKADN
PERKDLVFHG STTTLGHFVS WAYPECIPDR VDLCTQICDF GFYWDDVTDS VNVQENAEIT
QDLALALLSE LTLGQRLEPK LEINKIVVQM LWGVLDKDRK SGLEMIKFWK GHLDGQAESA
HNNMSFEEYT KHRLSEVGAR WAVEVGCWSL GINLSREKKD SVAHFVNKGL LAAALMNDYY
SFNKEFDEHQ RAGSMDRLQN GLGILMREYG YTETEARSIL REEIRKGERA IMDGYIAWRE
SADSSSESHE LNRYIVMIIL MIGGITFWSS HASRYHRDDL ITTAGDRAMI VGKFQCSMRL
LDGYPPPNRW KSATSSNDIS GRKRKSWSDS NGVDTHGACY TNGSSNRAKR NGTEAGHKAN
GHDSMDIYTA PFLKAPSEVC EAPYEYINSL QGKNMRNKFM DALNHWLCVP APSMQIIKNI
VQMLHNSSLM LDDIEDESPL RRGQPVAHTF YGISQTINSA NFVYVKSVKE TSRLKNPICM
EIFTDELSNL HTGQSLDLYW RYHGRCPSIN EYIMMVDNKT GGLFRLMLRL MEAESPAASS
ASLVKLLTLT GRYYQIRDDY LNLTSVEYTS KKGFCEDLDE GKFSLPLLHL LNHTRHPDRI
TAPLFNRASG ARSLAREVKV HIIQAMDEAG TFEYAQGVLK YLHEEIMRTL DEVEADLGRN
TEARILLLGL GL
