ID   EASD_TRIVH              Reviewed;         265 AA.
AC   D4D446;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Chanoclavine-I dehydrogenase easD {ECO:0000303|PubMed:22403186};
DE            Short=ChaDH {ECO:0000305};
DE            EC=1.1.1.332 {ECO:0000305|PubMed:22403186};
DE   AltName: Full=Ergot alkaloid synthesis protein D {ECO:0000303|PubMed:22403186};
DE   Flags: Precursor;
GN   Name=easD {ECO:0000303|PubMed:22403186}; ORFNames=TRV_01860;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   FUNCTION.
RX   PubMed=22403186; DOI=10.1099/mic.0.056796-0;
RA   Wallwey C., Heddergott C., Xie X., Brakhage A.A., Li S.M.;
RT   "Genome mining reveals the presence of a conserved gene cluster for the
RT   biosynthesis of ergot alkaloid precursors in the fungal family
RT   Arthrodermataceae.";
RL   Microbiology 158:1634-1644(2012).
CC   -!- FUNCTION: Chanoclavine-I dehydrogenase; part of the gene cluster that
CC       mediates the biosynthesis of fungal ergot alkaloid (PubMed:22403186).
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 (PubMed:22403186). 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
CC       (PubMed:22403186). The catalase easC and the FAD-dependent
CC       oxidoreductase easE then transform 4-dimethylallyl-L-abrine to
CC       chanoclavine-I which is further oxidized by easD in the presence of
CC       NAD(+), resulting in the formation of chanoclavine-I aldehyde
CC       (PubMed:22403186). Chanoclavine-I aldehyde is the precursor of
CC       ergoamides and ergopeptines in Clavicipitaceae, and clavine-type
CC       alcaloids such as fumiclavine in Trichocomaceae (PubMed:22403186).
CC       However, the metabolites downstream of chanoclavine-I aldehyde in
CC       Arthrodermataceae have not been identified yet (PubMed:22403186).
CC       {ECO:0000269|PubMed:22403186}.
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:D4AK45};
CC   -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC       {ECO:0000305|PubMed:22403186}.
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; ACYE01000098; EFE43380.1; -; Genomic_DNA.
DR   RefSeq; XP_003023998.1; XM_003023952.1.
DR   AlphaFoldDB; D4D446; -.
DR   SMR; D4D446; -.
DR   EnsemblFungi; EFE43380; EFE43380; TRV_01860.
DR   GeneID; 9582691; -.
DR   KEGG; tve:TRV_01860; -.
DR   HOGENOM; CLU_010194_1_0_1; -.
DR   UniPathway; UPA00327; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
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   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Alkaloid metabolism; NAD; Oxidoreductase; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..265
FT                   /note="Chanoclavine-I dehydrogenase easD"
FT                   /id="PRO_0000439130"
FT   ACT_SITE        169
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q12634"
FT   BINDING         16..40
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q12634"
SQ   SEQUENCE   265 AA;  28601 MW;  E0C7310BDCADB266 CRC64;
     MSFVSSKIFA ITGGASGIGA ATCRLLAKRG AATLCVGDLC SENMKLLEKD IKKINPDTKV
     HCTVLDVSSS SNVDEWIQDI ITTFGDLHGA ANIAGIAQGA GLRQAPTILE DDDQQWKKVF
     QVNLDGVLYS TRAQVRAMKE FSSTNPGDRS IVNVASIASM SHMPDVFAYG TSKAGCAYFT
     TFEVTLFALG YFSNIMGMLE GITRTPMLPR FVPSAKTQEE VEETYKKEGF SVIEADDVAR
     TIVWLLSEDS RPVFGANINV GACMP