EASA_EPIFI
ID EASA_EPIFI Reviewed; 380 AA.
AC A2TBU0;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Probable inactive reductase easA {ECO:0000250|UniProtKB:Q6ZXC1};
DE AltName: Full=Ergot alkaloid synthesis protein A {ECO:0000303|PubMed:17308187};
GN Name=easA {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: Probable inactive dehydrogenase; part of the gene cluster
CC that 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 -!- INDUCTION: Strongly expressed in planta but not expressed in axenic
CC culture (PubMed:17308187). {ECO:0000269|PubMed:17308187}.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the family, lacks the
CC conserved Tyr active site at position 176 which is replaced by a Phe
CC residue. {ECO:0000305}.
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DR EMBL; EF125025; ABM91449.1; -; Genomic_DNA.
DR AlphaFoldDB; A2TBU0; -.
DR SMR; A2TBU0; -.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR InterPro; IPR045247; Oye-like.
DR PANTHER; PTHR22893; PTHR22893; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
PE 2: Evidence at transcript level;
KW Alkaloid metabolism; Flavoprotein; FMN; NADP.
FT CHAIN 1..380
FT /note="Probable inactive reductase easA"
FT /id="PRO_0000439120"
FT BINDING 25..27
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 60
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 102
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 171
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 223
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 299
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 324..325
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 325
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 352
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
SQ SEQUENCE 380 AA; 42697 MW; 5F8AFA2A447D6FE2 CRC64;
MSTSNLFTPL QFGKCLLQHK LVLSPMTRFR ADNEGVPLPY VKTYYCQRAS LPGTLLLTEA
TAISRRARGF PNVPGIWSQE QIAGWKEVVD AVHAKGSYIW LQLWATGRAA EVGVLKANGF
DLVSSSAVPV SPGEPTPRAL SDDEINSYIG DFVQAAKNAV LEAGFDGVEL HGANGFLIDQ
FLQSPCNQRT DQWGGCIENR SRFGLEITRR VIDAVGKDHV GMKLSTWSTF QGMGTMDDLI
PQFEHFIMRL REIGIAYLHL ANSRWVEEED PTIRTHPDIH NETFVRMWGK EKPVLLAGGY
GPESAKLVVD ETYSDHKNIG VVFGRHYISN PDLPFRLKMG LPLQKYNRET FYIPFSDEGY
LDYPYSEEYI TENKKQAVLA
