EASE_EPIFI
ID EASE_EPIFI Reviewed; 605 AA.
AC A2TBU3;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=FAD-linked oxidoreductase easE {ECO:0000303|PubMed:17308187};
DE EC=1.-.-.- {ECO:0000305|PubMed:17308187};
DE AltName: Full=Chanoclavine I synthase {ECO:0000305};
DE AltName: Full=Ergot alkaloid synthesis protein E {ECO:0000303|PubMed:17308187};
DE Flags: Precursor;
GN Name=easE {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: FAD-linked oxidoreductase; part of the gene cluster that
CC mediates the biosynthesis of fungal ergot alkaloid ergovaline, the
CC predominant ergopeptine product in E.festucae var. lolii
CC (PubMed:17308187). DmaW catalyzes the first step of ergot alkaloid
CC biosynthesis by condensing dimethylallyl diphosphate (DMAP) and
CC tryptophan to form 4-dimethylallyl-L-tryptophan (By similarity). The
CC second step is catalyzed by the methyltransferase easF that methylates
CC 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-
CC methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By
CC similarity). The catalase easC and the FAD-dependent oxidoreductase
CC easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is
CC further oxidized by easD in the presence of NAD(+), resulting in the
CC formation of chanoclavine-I aldehyde (By similarity). Agroclavine
CC dehydrogenase easG then mediates the conversion of chanoclavine-I
CC aldehyde to agroclavine via a non-enzymatic adduct reaction: the
CC substrate is an iminium intermediate that is formed spontaneously from
CC chanoclavine-I aldehyde in the presence of glutathione (By similarity).
CC The presence of easA is not required to complete this reaction (By
CC similarity). Further conversion of agroclavine to paspalic acid is a
CC two-step process involving oxidation of agroclavine to elymoclavine and
CC of elymoclavine to paspalic acid, the second step being performed by
CC the 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=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC {ECO:0000305|PubMed:17308187}.
CC -!- INDUCTION: Strongly expressed in planta but not expressed in axenic
CC culture (PubMed:17308187). {ECO:0000269|PubMed:17308187}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; EF125025; ABM91450.1; -; Genomic_DNA.
DR AlphaFoldDB; A2TBU3; -.
DR SMR; A2TBU3; -.
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; -; 1.
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 2: Evidence at transcript level;
KW Alkaloid metabolism; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..605
FT /note="FAD-linked oxidoreductase easE"
FT /evidence="ECO:0000255"
FT /id="PRO_5002646853"
FT DOMAIN 122..307
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 605 AA; 66104 MW; C02A0C9790D99E8D CRC64;
MRHFVTFVVG FLLSWGFLSS LQDPPSCRCR PWEPCWPDSH QWTSLNASID GNLVHVQPVG
SVCHDPHYDA VACGDVLDLS RNSGWRASNP ATLQDWIWET GSGDNESCLL VSSSERPQEI
PCHQGRLPLY SAAVKSTAHV QGVIRFAKDH NLRLVIKNTG HDATGRSAAP DSLQIHTYFL
KDIHYDDNFL VHGDATGSGP AVTLGAGVVH SEVYKHGIDH KYSVVGGECP TVGIVGGFLQ
GGGVSSWSGF TRGLAVDNVL EYQVVTANAE LVIANEHQNQ DLFWALRGGG GGTFGVVTQA
TVRAFPDDPT VVSTLVLSST RADTSFWVKA ISRLLSILRS CNQQNVHGQL IITRPSVDIL
NAGLTLHFSN MTNVLHAETL LQPHIASLSE DQISTTLTSK FVANINSELR LDADIHPRGI
GTLQTSMMIS NELFGSSEGP LTVAQVFGKL PIGPNDLLFT SNLGGCIAAN KGLDTAIHPA
WRSSAHLVTY VRSVEPSIEA KKLALKEITN KYMPILYSMQ PSFKVSYRNL GDPNEKNYQE
VFWGEKVYKR LASIKAKLDP DGLFISKLGV GSEDWDTEGM CYQPQNRVSQ PLRSLKYFLS
VLKDT
