ID   JANO_PENJA              Reviewed;         449 AA.
AC   A0A0E3D8N0;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=FAD-linked oxidoreductase janO {ECO:0000303|PubMed:26213965};
DE            EC=1.1.1.- {ECO:0000305|PubMed:26213965};
DE   AltName: Full=Janthitremanes biosynthesis cluster protein O {ECO:0000303|PubMed:26213965};
GN   Name=janO {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-linked oxidoreductase; 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; Evidence={ECO:0000305};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:26213965}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; KF280651; AGZ20488.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3D8N0; -.
DR   SMR; A0A0E3D8N0; -.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..449
FT                   /note="FAD-linked oxidoreductase janO"
FT                   /id="PRO_0000446568"
FT   DOMAIN          32..203
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ   SEQUENCE   449 AA;  50249 MW;  4E10602D006344B7 CRC64;
     MTIPELPILW RDNAPPSEYE AWRSRTFNSK RPDAQPLAII KPTTIDHIVS ATALAKENNA
     KLALRSGGHS LQCWSLRKDS ILVDLENFRY LEFDDATGVV SVTPSVTSSE LLLFLANKKR
     FFPSGHSGEV GLGGFLLQGG IGLNARSYGY ACEYLTAVDV VTVSGEVKHC SPDENADLFW
     AARGAGPEFP AIVTRFHLNT RPLLPTVKRC TYIWPAVCYE MVFKWVLEIL PTLSDDIEPT
     IFGFTLPNTP IPVIAFHAHV HAESDESAIE LLKPLHESHP AGAMVEQDCV DTSVQQEFES
     GHAIMPPGAR YFTDSVFLTP GTDIIEACRE MFTTLPAQAA GSIAYWEPMK QRTKLPEMAW
     SIHSEHYVSL MAIYGDQNQD HKQQTWILDC FKDMDRKGLL LGTYVGDAHP KDRPHHYWSD
     PAKERIQKIG VQWDPEARLR GTIFAENTL