ID   EASE_ARTBC              Reviewed;         500 AA.
AC   D4AK47;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=FAD-linked oxidoreductase easE {ECO:0000303|PubMed:22403186};
DE            EC=1.-.-.- {ECO:0000305|PubMed:22403186};
DE   AltName: Full=Chanoclavine I synthase {ECO:0000305};
DE   AltName: Full=Ergot alkaloid synthesis protein E {ECO:0000303|PubMed:22403186};
GN   Name=easE {ECO:0000303|PubMed:22403186}; ORFNames=ARB_04648;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   FUNCTION.
RX   PubMed=22403186; DOI=10.1099/mic.0.056796-0;
RA   Wallwey C., Heddergott C., Xie X., Brakhage A.A., Li S.M.;
RT   "Genome mining reveals the presence of a conserved gene cluster for the
RT   biosynthesis of ergot alkaloid precursors in the fungal family
RT   Arthrodermataceae.";
RL   Microbiology 158:1634-1644(2012).
CC   -!- FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that
CC       mediates the biosynthesis of fungal ergot alkaloid (PubMed:22403186).
CC       DmaW catalyzes the first step of ergot alkaloid biosynthesis by
CC       condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-
CC       dimethylallyl-L-tryptophan (PubMed:22403186). The second step is
CC       catalyzed by the methyltransferase easF that methylates 4-
CC       dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine,
CC       resulting in the formation of 4-dimethylallyl-L-abrine
CC       (PubMed:22403186). The catalase easC and the FAD-dependent
CC       oxidoreductase easE then transform 4-dimethylallyl-L-abrine to
CC       chanoclavine-I which is further oxidized by easD in the presence of
CC       NAD(+), resulting in the formation of chanoclavine-I aldehyde
CC       (PubMed:22403186). Chanoclavine-I aldehyde is the precursor of
CC       ergoamides and ergopeptines in Clavicipitaceae, and clavine-type
CC       alcaloids such as fumiclavine in Trichocomaceae (PubMed:22403186).
CC       However, the metabolites downstream of chanoclavine-I aldehyde in
CC       Arthrodermataceae have not been identified yet (PubMed:22403186).
CC       {ECO:0000269|PubMed:22403186}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC       {ECO:0000305|PubMed:22403186}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; ABSU01000001; EFE37120.1; -; Genomic_DNA.
DR   RefSeq; XP_003017765.1; XM_003017719.1.
DR   AlphaFoldDB; D4AK47; -.
DR   SMR; D4AK47; -.
DR   STRING; 663331.D4AK47; -.
DR   EnsemblFungi; EFE37120; EFE37120; ARB_04648.
DR   GeneID; 9522611; -.
DR   KEGG; abe:ARB_04648; -.
DR   eggNOG; ENOG502R8I5; Eukaryota.
DR   HOGENOM; CLU_018354_4_4_1; -.
DR   OMA; CHQGRIP; -.
DR   UniPathway; UPA00327; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035835; P:indole alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.465.10; -; 2.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Alkaloid metabolism; FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..500
FT                   /note="FAD-linked oxidoreductase easE"
FT                   /id="PRO_0000439134"
FT   DOMAIN          37..220
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ   SEQUENCE   500 AA;  54433 MW;  55CD3F4040B591DA CRC64;
     MLTGVLQDWV WEAGETANES CPVGSLRTAS AVNSCHQGRI PLFTVGVEST KQVQEAVRFA
     RKHNLRLVIR NTGHDLAGRS SAPDSFQIHT HHLQEIQFHA DMRLDGSNTS LGPAVTVGAG
     VMMGNLYAQA ARHGYMVLGG DCPTVGVVGG FLQGGGISDF LSLNQGFGVD NVLEYEVVTA
     DGELVVANAL QNQDLFWALR GGGGGTFGVV TRATMRVFPD VPVVISEILL EAPQAISSSW
     TQGLSIVLTA LQSLNRDNVG GQLVIAVLPK LAVQASIKFF FLDATEATVI DRRMKPFLTK
     LSRANVKYTY SSKNLPHFSS NYRQVPDIHS DNDYGVLGST VAISQQLFDS PQGPEKVATA
     LANLPVSAGD LIFTSNLGGR VISNGELAET SMHPAWRSAS QLINYVHTVE PSIEGRAKAR
     ERLTNTQMPM LYALDPNLKL SYRNVGDPNE KDFQQIYWGP NYGRLSNIKK KWDTDDLFFS
     KLGVGSERWD SEEQLCLLHA