ID   EASE_CLAFS              Reviewed;         581 AA.
AC   A8C7R9;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=FAD-linked oxidoreductase easE {ECO:0000303|PubMed:17720822};
DE            EC=1.-.-.- {ECO:0000305|PubMed:17720822};
DE   AltName: Full=Chanoclavine I synthase {ECO:0000305};
DE   AltName: Full=Ergot alkaloid synthesis protein E {ECO:0000303|PubMed:17720822};
DE   Flags: Precursor;
GN   Name=easE {ECO:0000303|PubMed:17720822};
OS   Claviceps fusiformis (Ergot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=40602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 26245 / DSM 2942 / CBS 164.59;
RX   PubMed=17720822; DOI=10.1128/aem.01040-07;
RA   Lorenz N., Wilson E.V., Machado C., Schardl C.L., Tudzynski P.;
RT   "Comparison of ergot alkaloid biosynthesis gene clusters in Claviceps
RT   species indicates loss of late pathway steps in evolution of C.
RT   fusiformis.";
RL   Appl. Environ. Microbiol. 73:7185-7191(2007).
CC   -!- FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that
CC       mediates the biosynthesis of fungal ergot alkaloid (PubMed:17720822).
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 (By similarity). 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 (By similarity).
CC       The catalase easC and the FAD-dependent oxidoreductase easE then
CC       transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further
CC       oxidized by easD in the presence of NAD(+), resulting in the formation
CC       of chanoclavine-I aldehyde (By similarity). Agroclavine dehydrogenase
CC       easG then mediates the conversion of chanoclavine-I aldehyde to
CC       agroclavine via a non-enzymatic adduct reaction: the substrate is an
CC       iminium intermediate that is formed spontaneously from chanoclavine-I
CC       aldehyde in the presence of glutathione (By similarity). Further
CC       conversion of agroclavine to paspalic acid is a two-step process
CC       involving oxidation of agroclavine to elymoclavine and of elymoclavine
CC       to paspalic acid, the second step being performed by the elymoclavine
CC       oxidase cloA (PubMed:17720822). However, cloA does not encode a
CC       functional enzyme indicating that C.fusiformis terminates its ergot
CC       alkaloid pathway at elymoclavine (PubMed:17720822).
CC       {ECO:0000250|UniProtKB:O94206, ECO:0000269|PubMed:17720822}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC       {ECO:0000305|PubMed:17720822}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; EU006773; ABV57823.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8C7R9; -.
DR   SMR; A8C7R9; -.
DR   UniPathway; UPA00327; -.
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; Glycoprotein; Oxidoreductase;
KW   Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..581
FT                   /note="FAD-linked oxidoreductase easE"
FT                   /id="PRO_5002719458"
FT   DOMAIN          122..306
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        369
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   581 AA;  64134 MW;  FA2CF426DEF8A4BD CRC64;
     MYRLLGPLAC LALAWFFTWA PSGRCRCRPW ETCWPSVADW SALNESMQGN LIRIRPVASV
     CHGSEYEAAA CANVSNMVVD SGWRASNPRT LQDWIWETGN TAQESCFDTT WPGYHHRTSD
     CHQGRIPLYS AIVESTSDIQ SCVKFANHHN LRLVIKNSGH DTAGRSSAPH SFQISTSSLK
     TISLHENFVP RGSTTGHGPA VTLGAGVMQW EVYAHGVKNA YTILGGECPT VGAVGAFLQG
     GGVSSIKSFT KGLAVDNVLE FQVVTSNADL VTANENENQD LFWALRGGGG GTFGFVAQAT
     IRVFPDDPVT VATTTIKAAV TNTMFWTEGV RELFRLVQHF NDMHIPGQLV MTRPTTDSMQ
     ATLELHFANT TDEAHVTRLL NSQLRPLTLH HISTSTLVRV QERESSELRT KPDIYPPHYG
     IVAGSVLISA ATLRKAQGQS HVASKLSQLP LGSNDIMFTS NLGGRVFENS AIDISLHPAW
     REAAHLITLV RAVEPTIEDR DSQVSYRNLG DPQEKEFRDR YWGTANYARL AAIKAKWDPH
     ELFMSKLGVG SENWDEEGIC RKSLGFVERL SAILKLERWK N