JANM_PENJA
ID JANM_PENJA Reviewed; 475 AA.
AC A0A0E3D8L5;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=FAD-dependent monooxygenase janM {ECO:0000303|PubMed:26213965};
DE EC=1.-.-.- {ECO:0000305|PubMed:26213965};
DE AltName: Full=Janthitremanes biosynthesis cluster protein M {ECO:0000303|PubMed:26213965};
GN Name=janM {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: FAD-dependent monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the indole diterpenes janthitremanes such
CC as 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:A6T923};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:26213965}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; KF280651; AGZ20480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E3D8L5; -.
DR SMR; A0A0E3D8L5; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Glycoprotein; Membrane; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..475
FT /note="FAD-dependent monooxygenase janM"
FT /id="PRO_0000446563"
FT TRANSMEM 8..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 35..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 131
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 225..227
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 299
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 309..313
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 475 AA; 53222 MW; AB77C491613C4873 CRC64;
MSKSEFQVII VGGSIGGLTL AHCLRRAGID HIILEKSSSP APQIGASIGI LPNGARILDQ
LQLWSEVEDY IEPLSTATIG LPDGFSFSSS YPQIINERFG FPIAFLDRQL LLEILYQRYP
DRSKIRLEEK VTAVETSDSG ATVTTSNGSV YRGGLVVGAD GVHSIVRREI WRASKKLSSG
LTAEFRCIFG ISSAIKGLNV GEQVNALFDG LTIVTIHGKN GRVYWFVIQK LDKKYIYPNC
PRYTKHDTTV AAEQLRNIQF YRDITFGQVW ENRETASMTV LEENTFKTWH YGRLVLLGDS
VHKMTPNIGQ GANMAIEDAA ALTNLLHNLQ KISGTLSSTA AQIETILRQY RRIRYERVES
IYRDSRFLVR FQARDGLLNI LLSRYYAPYA GDLPADMASK TIADGVMCDF LPPPKRSGDG
WKRYRRDGQL RGWRFHAMLC ILMLAILYTW VGRTNLDSIV FSACGSLFQK LSVPT
