ID   EASE_ARTOC              Reviewed;         612 AA.
AC   C5FTN2;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 52.
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=MCYG_06054;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; DS995705; EEQ33235.1; -; Genomic_DNA.
DR   RefSeq; XP_002846185.1; XM_002846139.1.
DR   AlphaFoldDB; C5FTN2; -.
DR   SMR; C5FTN2; -.
DR   STRING; 63405.XP_002846185.1; -.
DR   EnsemblFungi; EEQ33235; EEQ33235; MCYG_06054.
DR   GeneID; 9227067; -.
DR   eggNOG; ENOG502R8I5; Eukaryota.
DR   HOGENOM; CLU_018354_4_4_1; -.
DR   OMA; CHQGRIP; -.
DR   OrthoDB; 827142at2759; -.
DR   UniPathway; UPA00327; -.
DR   Proteomes; UP000002035; 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..612
FT                   /note="FAD-linked oxidoreductase easE"
FT                   /id="PRO_0000439135"
FT   DOMAIN          129..313
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ   SEQUENCE   612 AA;  67360 MW;  0778A91086BED686 CRC64;
     MNSNSQIRSS RLIEALHAYY SKYLVVTIRP IRYLVEPWQP CWPSEELWNS FNTSIDGKLQ
     QLKPAAHVCY EPNFDKGACD DLLRLSRDSG WRASHPGVLQ DWVWEAGESA NETCPMGSLQ
     TATAAKSCHQ GRIPLYSATV ESAQQVQQAV RFARRHNLRL VIRNTGHDLA GRSSAPDSFQ
     IHTHRLQETQ FHTDLRLNGS TASLGPAVTV GAGVMMGNLY ARAAREGYMV LGGDCPTVGV
     AGGFLQGGGV SDFLSLNQGL GVDNVLEYEI VTADGELLVA NTLQNQELFW ALRGGGGGTF
     GVVTRATMRV FPDVPAVISE VLLQAPQTNS SSWTEGLSVI LNALQSLNRD DVGGQLVIAV
     QPELAVQASI KFFFLNSTET TIIDERMKSL LTDLNRIDIQ YTLSSKALPH FSSNYRQVPD
     IHSDNDYGVI GSTVAISKEL FDSSQGPQKI ARALANLPMS PGDLLFTSNL GGRVISNGEI
     AETSMHPAWR AASQLLNYIH AVGPSIESRV NALERLTNVQ MPMLYAIDPN FRLSYRNVGD
     PNEKDFQQVY WGSNYKRLSQ IKKRWDSDGL FFSKLGVGSE LWDSEGMCRK NQSVVRQAVN
     YLMSFATSMV EG