PAPS_PHOAM
ID PAPS_PHOAM Reviewed; 728 AA.
AC P9WEV6;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 1.
DT 03-AUG-2022, entry version 7.
DE RecName: Full=Phomopsene synthase {ECO:0000303|PubMed:19161275};
DE Short=PS {ECO:0000303|PubMed:19161275};
DE Includes:
DE RecName: Full=Terpene cyclase {ECO:0000303|PubMed:19161275};
DE EC=4.2.3.- {ECO:0000269|PubMed:19161275, ECO:0000269|PubMed:28270685};
DE Includes:
DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:19161275};
DE Short=GGDP synthase {ECO:0000303|PubMed:19161275};
DE Short=GGS {ECO:0000303|PubMed:19161275};
DE EC=2.5.1.29 {ECO:0000269|PubMed:19161275, ECO:0000269|PubMed:28270685};
DE AltName: Full=Methyl phomopsenonate biosynthesis cluster protein PaPS {ECO:0000303|PubMed:28270685};
GN Name=PaPS {ECO:0000303|PubMed:19161275};
OS Phomopsis amygdali (Fusicoccum amygdali).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214568;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND
RP PATHWAY.
RX PubMed=19161275; DOI=10.1021/jo802319e;
RA Toyomasu T., Kaneko A., Tokiwano T., Kanno Y., Kanno Y., Niida R.,
RA Miura S., Nishioka T., Ikeda C., Mitsuhashi W., Dairi T., Kawano T.,
RA Oikawa H., Kato N., Sassa T.;
RT "Biosynthetic gene-based secondary metabolite screening: a new diterpene,
RT methyl phomopsenonate, from the fungus Phomopsis amygdali.";
RL J. Org. Chem. 74:1541-1548(2009).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28270685; DOI=10.1038/ja.2017.27;
RA Shinde S.S., Minami A., Chen Z., Tokiwano T., Toyomasu T., Kato N.,
RA Sassa T., Oikawa H.;
RT "Cyclization mechanism of phomopsene synthase: mass spectrometry based
RT analysis of various site-specifically labeled terpenes.";
RL J. Antibiot. 70:632-638(2017).
CC -!- FUNCTION: Bifunctional terpene synthase; part of the gene cluster that
CC mediates the biosynthesis of the diterpene methyl phomopsenonate
CC (PubMed:19161275, PubMed:28270685). At first, the universal precursor
CC of diterpene, geranylgeranyl diphosphate (GGPP) is provided and is
CC cyclized by the unusual bifunctional terpene synthase PaPS to give
CC phomopsene (PubMed:19161275, PubMed:28270685). The C-terminal
CC prenyltransferase domain of PaPS catalyzes formation of GGPP, whereas
CC the N-terminal terpene cyclase domain catalyzes the cyclization of GGPP
CC to phomopsene (PubMed:19161275, PubMed:28270685). Since the oxidation
CC of a methylgroup to a carboxyl group is frequently catalyzed by a
CC cytochrome P450 monooxygenase, the C-16 methyl group would be oxidized
CC by the cluster-specific cytochrome P450 monooxygenase ORF3 (Probable).
CC Subsequently, oxidation of the allylic position and methylation of the
CC carboxyl group may give methyl phomopsenonate (Probable). Although
CC further study is necessary to identify genes such as a monooxygenase
CC and a methyltransferase, the predicted functions of genes on the
CC cluster are correlated with the structure of methyl phomopsenonate
CC (Probable). {ECO:0000269|PubMed:19161275, ECO:0000269|PubMed:28270685,
CC ECO:0000305|PubMed:19161275}.
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:19161275, ECO:0000269|PubMed:28270685};
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:28270685}.
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:19161275}.
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 AlphaFoldDB; P9WEV6; -.
DR SMR; P9WEV6; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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..728
FT /note="Phomopsene synthase"
FT /id="PRO_0000450827"
FT REPEAT 381..386
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 387..392
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 393..398
FT /note="3"
FT /evidence="ECO:0000305"
FT REGION 1..327
FT /note="Terpene cyclase"
FT /evidence="ECO:0000269|PubMed:19161275,
FT ECO:0000269|PubMed:28270685"
FT REGION 328..728
FT /note="Prenyltransferase"
FT /evidence="ECO:0000269|PubMed:19161275,
FT ECO:0000269|PubMed:28270685"
FT REGION 352..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..398
FT /note="3 X 6 AA approximate tandem repeats"
FT /evidence="ECO:0000305"
FT MOTIF 94..98
FT /note="DDXXD 1"
FT /evidence="ECO:0000269|PubMed:19161275"
FT MOTIF 226..234
FT /note="NSE/DTE"
FT /evidence="ECO:0000305|PubMed:19161275"
FT MOTIF 486..490
FT /note="DDXXD 2"
FT /evidence="ECO:0000269|PubMed:19161275"
FT COMPBIAS 352..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 181..184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 230..234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 319..320
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A2PZA5"
FT BINDING 447
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 450
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 479
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 486
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 486
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 490
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 490
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 495
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 496
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 574
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 610
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 617
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 627
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 637
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 728 AA; 81975 MW; 33A45CC1D2DC6162 CRC64;
MEYRYSYVID PSSYDNQGLC NGIPLRVHRN ADIEEYATIS LRNDWRKHVG PLPLTSYGGN
LGPKYNFTAV TLPECRPDRL EIVSYIMEFA FLHDDLVDTA QVDEALALND TWRDGITEGL
DTTSAKGKKS GEGLILRNIL KEVTAIDPVR AAELMKFWKR DLDVSRDRKH FRDFDDYMEY
RIVDCASYFL IALSTFAMAL TIPAEDKDEV FTLLTRPVWA AAALTNDVQS WEKEDKLFQK
DNATDMTNGV WMLMKQYSIG VEEAKRRILG KAREHVAEFV KTLSQIHNRL DLSLDSRLFV
EAMQYMISGN LMWGISTPRY HSDQSLDEMM VARMKYGWPN HREVTKLTSD LENRGTKRTH
QDDTEGVQSV KRFNGASTKN GINGTNGING LNGINGSNGV KIKRHKNKEY SGALTKDSDL
VLNMDLNGLS SAIICAPADY IGSLPSKGIR DNVADALSIW LDVPAKELNQ IKRAINLLHN
ASLMLDDVQD GSVLRRAQPT THTVFGPAQT INSAGHQIIQ AMNEIRKLGS DDCLDIFSEE
LEKLYVGQSH DLYWVYNDSC SPTIEDYFKM VDYKTGGLFN MLARLMTAKS SSSSSPDLTA
LVGLLGRYFQ IRDDYMNLTS ADYTVEKGFC EDLDEGKFSI TLLHALSAAP EPEALLLRNL
MSGRRNDGKL SVVQKNLALS IIEGARSLEY TAAVLQKLYK AIVRELESTE RQFGENKPFR
FLLSLLKV
