ID   EASG_CLAFS              Reviewed;         289 AA.
AC   A8C7S1;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Agroclavine dehydrogenase {ECO:0000250|UniProtKB:P0CT21};
DE            EC=1.5.1.46 {ECO:0000250|UniProtKB:P0CT21};
DE   AltName: Full=Ergot alkaloid biosynthesis protein G {ECO:0000303|PubMed:17720822};
GN   Name=easG {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].
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: Agroclavine dehydrogenase; 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:17720822). 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       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 (PubMed:17720822). However, cloA does not
CC       encode a functional enzyme indicating that C.fusiformis terminates its
CC       ergot alkaloid pathway at elymoclavine (PubMed:17720822).
CC       {ECO:0000250|UniProtKB:P0CT21, ECO:0000269|PubMed:17720822}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=agroclavine + NADP(+) = didehydroagroclavine + H(+) + NADPH;
CC         Xref=Rhea:RHEA:34059, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:65036, ChEBI:CHEBI:65042; EC=1.5.1.46;
CC         Evidence={ECO:0000250|UniProtKB:P0CT21};
CC   -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC       {ECO:0000305|PubMed:17720822}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P0CT21}.
CC   -!- SIMILARITY: Belongs to the fgaFS/easG family. {ECO:0000305}.
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DR   EMBL; EU006773; ABV57825.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8C7S1; -.
DR   SMR; A8C7S1; -.
DR   UniPathway; UPA00327; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035835; P:indole alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR   InterPro; IPR019901; Ergot_alkaloid_biosynthesis.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF13460; NAD_binding_10; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR03649; ergot_EASG; 1.
PE   3: Inferred from homology;
KW   Alkaloid metabolism; NADP; Oxidoreductase.
FT   CHAIN           1..289
FT                   /note="Agroclavine dehydrogenase"
FT                   /id="PRO_0000439143"
SQ   SEQUENCE   289 AA;  31815 MW;  CD4571162A7DB9D9 CRC64;
     MTILLTGGSG KTAGHIANLL KEAKLPFIVG SRSSNPHTVE RHRTFDWLDE ATFNNVLSVD
     EGMEPVSVVW LVSPPILDLA PPVIRFIDFA SSRGVKRFVL LSASTVEKGG PAMGLIHAHL
     DTIEGVSYTV LRPSWFMENF STRGEFPCDT IREEDTIYSA AKDGKIPFIS VADIARVALR
     ALTAPALHNK DHVLLGPELL TYDDVAEILT RVVGRNIHHV RLTESELAAK LQERGMPADE
     AAMHASLDSI VEAGAEEKLN TEVKDLTGEE PRHFADFVSD NKNVWLMRD