ID   EASH_EPIFI              Reviewed;         185 AA.
AC   A2TBT9;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Dioxygenase easH {ECO:0000303|PubMed:17308187};
DE            EC=1.14.11.- {ECO:0000305|PubMed:17308187};
DE   AltName: Full=Ergot alkaloid biosynthesis protein H {ECO:0000303|PubMed:17308187};
DE   Flags: Fragment;
GN   Name=easH {ECO:0000303|PubMed:17308187};
OS   Epichloe festucae var. lolii (Neotyphodium lolii) (Acremonium lolii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Epichloe.
OX   NCBI_TaxID=73839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=Lp19;
RX   PubMed=17308187; DOI=10.1128/aem.00257-07;
RA   Fleetwood D.J., Scott B., Lane G.A., Tanaka A., Johnson R.D.;
RT   "A complex ergovaline gene cluster in epichloe endophytes of grasses.";
RL   Appl. Environ. Microbiol. 73:2571-2579(2007).
RN   [2]
RP   FUNCTION.
RX   PubMed=11592979; DOI=10.1073/pnas.221198698;
RA   Panaccione D.G., Johnson R.D., Wang J., Young C.A., Damrongkool P.,
RA   Scott B., Schardl C.L.;
RT   "Elimination of ergovaline from a grass-Neotyphodium endophyte symbiosis by
RT   genetic modification of the endophyte.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12820-12825(2001).
CC   -!- FUNCTION: Dioxygenase; part of the gene cluster that mediates the
CC       biosynthesis of fungal ergot alkaloid ergovaline, the predominant
CC       ergopeptine product in E.festucae var. lolii (PubMed:17308187). DmaW
CC       catalyzes the first step of ergot alkaloid biosynthesis by condensing
CC       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). The presence
CC       of easA is not required to complete this reaction (By similarity).
CC       Further conversion of agroclavine to paspalic acid is a two-step
CC       process involving oxidation of agroclavine to elymoclavine and of
CC       elymoclavine to paspalic acid, the second step being performed by the
CC       elymoclavine oxidase cloA (By similarity). Paspalic acid is then
CC       further converted to D-lysergic acid (By similarity). Ergovaline is
CC       assembled from D-lysergic acid and three different amino acids by the
CC       D-lysergyl-peptide-synthetase composed of a monomudular (lpsB) and a
CC       trimodular (lpsA) nonribosomal peptide synthetase subunit
CC       (PubMed:17308187, PubMed:11592979). {ECO:0000250|UniProtKB:Q50EL0,
CC       ECO:0000269|PubMed:11592979, ECO:0000269|PubMed:17308187}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:Q4WAW9};
CC   -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC       {ECO:0000305|PubMed:17308187}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q4WAW9}.
CC   -!- INDUCTION: Strongly expressed in planta but weakly expressed in axenic
CC       culture (PubMed:17308187). {ECO:0000269|PubMed:17308187}.
CC   -!- SIMILARITY: Belongs to the PhyH family. {ECO:0000305}.
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DR   EMBL; EF125025; ABM91453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2TBT9; -.
DR   SMR; A2TBT9; -.
DR   UniPathway; UPA00327; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035835; P:indole alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR008775; Phytyl_CoA_dOase.
DR   Pfam; PF05721; PhyH; 1.
PE   2: Evidence at transcript level;
KW   Alkaloid metabolism; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           <1..185
FT                   /note="Dioxygenase easH"
FT                   /id="PRO_0000439146"
FT   BINDING         17
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:G8GV69"
FT   BINDING         19
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:G8GV69"
FT   BINDING         93
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:G8GV69"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:ABM91453.1"
SQ   SEQUENCE   185 AA;  20234 MW;  447208BA41C01939 CRC64;
     YGAAIENGPG TQEQIWHRDQ PDYALLKAGP GTAEAMLNFF TALTDFTPDT GMTQYIWGSH
     KRVELGEPDA EHPVVFTKLK AGDTAVLSGK IVHRGSANAT PDVFRRALAL MIIPAIMTPF
     DATCHLSRHM VETMTPLAQK MVGRRSVVIP PPHTVGAALG IWCLNMREVG EQMGLKSNQP
     DKEEE