JANC_PENJA
ID JANC_PENJA Reviewed; 327 AA.
AC A0A0E3D8L3;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Prenyl transferase janC {ECO:0000303|PubMed:26213965};
DE EC=2.5.1.- {ECO:0000305|PubMed:26213965};
DE AltName: Full=Janthitremanes biosynthesis cluster protein C {ECO:0000303|PubMed:26213965};
GN Name=janC {ECO:0000303|PubMed:26213965};
OS Penicillium janthinellum (Penicillium vitale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5079;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND PATHWAY.
RC STRAIN=PN2408;
RX PubMed=26213965; DOI=10.3390/toxins7082701;
RA Nicholson M.J., Eaton C.J., Starkel C., Tapper B.A., Cox M.P., Scott B.;
RT "Molecular cloning and functional analysis of gene clusters for the
RT biosynthesis of indole-diterpenes in Penicillium crustosum and P.
RT janthinellum.";
RL Toxins 7:2701-2722(2015).
CC -!- FUNCTION: Prenyl transferase; part of the gene cluster that mediates
CC the biosynthesis of the indole diterpenes janthitremanes such as
CC shearinine K or shearinine A (PubMed:26213965). The geranylgeranyl
CC diphosphate (GGPP) synthase janG catalyzes the first step in
CC janthitremane biosynthesis via conversion of farnesyl pyrophosphate and
CC isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP)
CC (PubMed:26213965). Condensation of indole-3-glycerol phosphate with
CC GGPP by the prenyl transferase janC then forms 3-geranylgeranylindole
CC (3-GGI) (PubMed:26213965). Epoxidation by the FAD-dependent
CC monooxygenase janM leads to a epoxidized-GGI that is substrate of the
CC terpene cyclase janB for cyclization to yield paspaline
CC (PubMed:26213965). Paspaline is subsequently converted to 13-
CC desoxypaspaline by the cytochrome P450 monooxygenase janP, via beta-PC-
CC M6 in a series of alpha-face oxidations (Probable). The cytochrome P450
CC monooxygenase janQ is proposed to carry out sequential beta-face
CC oxidation steps at C-7 and C-13 of 13-desoxypaspaline to form
CC paspalicine and paspalinine respectively (Probable). The indole
CC diterpene prenyltransferase janD may then convert paspalinine into
CC shearinine K which is substrate of janO and/or additional enzymes for
CC oxidation and cyclization to generate shearinine A (Probable).
CC {ECO:0000269|PubMed:26213965, ECO:0000305|PubMed:26213965}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:26213965}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; KF280651; AGZ20475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E3D8L3; -.
DR SMR; A0A0E3D8L3; -.
DR GO; GO:0016021; C:integral component of membrane; 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:InterPro.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Magnesium; Membrane; Metal-binding; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..327
FT /note="Prenyl transferase janC"
FT /id="PRO_0000446548"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 63
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 96
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 112
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 196
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 327 AA; 37174 MW; D43EB9FBEC9C690A CRC64;
MAFPGAGPIL GAIAVSSCLY FLFDYVPIPR WWDKNAYLIG QMHPDEITGL ECPYAYLRQI
YGKYHWAPFV HKISPTLQKD DYPKYVMVLE IMDAIHLCLM LVDDISDGSD YRKGKPAAHK
IYGPTETANR AYYRVTQILA QTTKEFPNLA PWLMGDLRDI LEGQDMSLVW RRDGIGGFPT
AAKDRAAAYR KMASLKTGAL FRLLGHLVLE NDSMDEVFTV IAWYSQLQND CKNVYSSEYA
KLKGLVAEDL HNREMTYPIV LALDAPEGHW VTRALESPSP RNIRNALKVI RSKYVRDKCT
AELAESGASV KEWLQLWGRT EKLDLKA
