IACE_PESFW
ID IACE_PESFW Reviewed; 439 AA.
AC A0A1J0HSL6; W3XKM4;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Prenyltransferase iacE {ECO:0000303|PubMed:29384350};
DE EC=2.5.1.- {ECO:0000269|PubMed:29384350};
DE AltName: Full=Iso-A82775C biosynthesis cluster protein E {ECO:0000303|PubMed:29384350};
GN Name=iacE {ECO:0000303|PubMed:29384350}; ORFNames=PFICI_04042;
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP INDUCTION, PATHWAY, AND BIOTECHNOLOGY.
RC STRAIN=W106-1 / CGMCC3.15140;
RX PubMed=29384350; DOI=10.1021/acschembio.7b01059;
RA Pan Y., Liu L., Guan F., Li E., Jin J., Li J., Che Y., Liu G.;
RT "Characterization of a prenyltransferase for iso-A82775C biosynthesis and
RT generation of new congeners of chloropestolides.";
RL ACS Chem. Biol. 13:703-711(2018).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140;
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
CC -!- FUNCTION: Prenyltransferase; part of the gene cluster that mediates the
CC biosynthesis of iso-A82775C, a enylepoxycyclohexane and biosynthetic
CC precursor of the chloropestolide anticancer natural products
CC (PubMed:29384350). Within the cluster, the prenyltransferase iacE
CC prenylates siccayne to generate pestalodiol E, using dimethylallyl
CC diphosphate (DMAPP) as cosubstrate (PubMed:29384350). The probable
CC oxidoreductase iacF is then involved in the epoxidation of pestalodiol
CC F to pestalodiol F, which is further converted to pestalofone A by the
CC short-chain dehydrogenase/reductase iacG (PubMed:29384350). Iso-A82775C
CC is subsequently generated from pestalofone A by the short-chain
CC dehydrogenase/reductase iacC (PubMed:29384350). Iso-A82775C is further
CC condensed with maldoxin via a Diels-Alder reaction to produce the
CC anticancer natural products chloropestolides A to E (Probable).
CC {ECO:0000269|PubMed:29384350, ECO:0000305|PubMed:29384350}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + siccayne = diphosphate +
CC pestalodiol; Xref=Rhea:RHEA:65064, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57623, ChEBI:CHEBI:156304, ChEBI:CHEBI:156305;
CC Evidence={ECO:0000269|PubMed:29384350};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65065;
CC Evidence={ECO:0000269|PubMed:29384350};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=46.25 uM for siccayne {ECO:0000269|PubMed:29384350};
CC KM=34.52 uM for DMAPP {ECO:0000269|PubMed:29384350};
CC Vmax=358 pmol/sec/mg enzyme {ECO:0000269|PubMed:29384350};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:29384350}.
CC -!- INDUCTION: Expression is co-regulated with the other genes from the
CC iso-A82775C biosynthesis cluster and probably controlled by the
CC cluster-specific transcription factors iacI and iacK.
CC {ECO:0000269|PubMed:29384350}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of iso-A82775C, but
CC accumulates siccayne as well as chloropestolides H to K.
CC {ECO:0000269|PubMed:29384350}.
CC -!- BIOTECHNOLOGY: Iso-A82775C is a precursor for the biosynthesis of the
CC anticancer natural products chloropestolides A to E via a Diesls-Alder
CC reaction with maldoxin (PubMed:29384350). In the absence of the
CC prenyltransferase iacE, siccayne accumulates instead of iso-A82775C and
CC can also be condensed with maldoxin to produce chloropestolides H to K,
CC which show also antibacterial and anticancer properties
CC (PubMed:29384350). {ECO:0000269|PubMed:29384350}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; KU963195; APC57597.1; -; Genomic_DNA.
DR EMBL; KI912110; ETS86017.1; -; Genomic_DNA.
DR RefSeq; XP_007830814.1; XM_007832623.1.
DR AlphaFoldDB; A0A1J0HSL6; -.
DR SMR; A0A1J0HSL6; -.
DR STRING; 1229662.W3XKM4; -.
DR EnsemblFungi; ETS86017; ETS86017; PFICI_04042.
DR GeneID; 19269055; -.
DR KEGG; pfy:PFICI_04042; -.
DR eggNOG; ENOG502S2XP; Eukaryota.
DR HOGENOM; CLU_037431_0_0_1; -.
DR OMA; GVYMTMY; -.
DR OrthoDB; 1531660at2759; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd13929; PT-DMATS_CymD; 1.
DR InterPro; IPR033964; Aro_prenylTrfase.
DR InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR InterPro; IPR012148; DMATS-type_fun.
DR PANTHER; PTHR40627; PTHR40627; 1.
DR Pfam; PF11991; Trp_DMAT; 1.
DR PIRSF; PIRSF000509; Trp_DMAT; 1.
DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..439
FT /note="Prenyltransferase iacE"
FT /id="PRO_0000451377"
FT BINDING 88..89
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ SEQUENCE 439 AA; 49139 MW; 95ADD77512381436 CRC64;
MAISTPSNGV SHVAKPLPNL KEVNKGIETD SEDRAFWWGA LSEPLASLLE ANHYTKEVQL
HYLRWFYQWI LPALGPRPLD GKPYYGSWIT HDLSPFEYSL NWKEKSSKQT IRFTIEAVTK
QSGTASDPIN QLGAKEFLEA VSKDVPGMDL TRFNQFLEAT NVPNDCVDDA IAKHPAHFPR
SRVWIAFDLE HSGNLMAKSY FLPHWRAIQS GISANTIIGD TVKECNKADG SSYDGSLNAI
ESYLATFTRP EEAPQMGLLS NDCVAETPGS RLKVYFRSSA DTLAKAKDMY NLGGRLKGPK
MDASLKGISD FWYHLFGLDS SDPASDDKVC IGNHKCIFVY EMRSSQGSEP DIDVKFHIPM
WQLGKTDGQI SELLASWFES HGHPDLASRY KSDLGTAFPK HNITGKSVGT HTYISITHTP
KTGLYMTMYL SPKLPEFYY
