ID   EASD_CLAFS              Reviewed;         261 AA.
AC   A8C7R7;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Chanoclavine-I dehydrogenase easD {ECO:0000250|UniProtKB:Q4WZ66};
DE            Short=ChaDH {ECO:0000250|UniProtKB:Q4WZ66};
DE            EC=1.1.1.332 {ECO:0000250|UniProtKB:Q4WZ66};
DE   AltName: Full=Ergot alkaloid synthesis protein D {ECO:0000303|PubMed:17720822};
DE   Flags: Precursor;
GN   Name=easD {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: Chanoclavine-I dehydrogenase; 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:O94207, ECO:0000269|PubMed:17720822}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chanoclavine-I + NAD(+) = chanoclavine-I aldehyde + H(+) +
CC         NADH; Xref=Rhea:RHEA:33891, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:71487, ChEBI:CHEBI:72949;
CC         EC=1.1.1.332; Evidence={ECO:0000250|UniProtKB:Q4WZ66};
CC   -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC       {ECO:0000305|PubMed:17720822}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:D4AK45}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; EU006773; ABV57822.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8C7R7; -.
DR   SMR; A8C7R7; -.
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   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Alkaloid metabolism; Glycoprotein; NAD; Oxidoreductase; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..261
FT                   /note="Chanoclavine-I dehydrogenase easD"
FT                   /id="PRO_0000439131"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q12634"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   261 AA;  27894 MW;  ED83E6CDA7F75DF6 CRC64;
     MSSVSAKIFA VTGGASGIGA ATCRLLAERG AAVICVADVN CTDFASLQES IAQINASTLV
     QCTKVDVSSV QDVNLWLHGI VSKHGDLHGA ANVAGIAQAA GLRTKLTILE EDDAEWRRVL
     DINLNGVFYS TRAEVKVMRD LPLAHRSIVN VASIAAFSHV PDVYAYGTSK NACAYLTTCI
     AADVFWSGIR VNCVSPGITN TPLLPQFEPK VKTLDEIRKL YREQGYPTSE AEDVARTIVW
     LLSEDSRPVY GANINVGACP P