ID   EASD_ARTOC              Reviewed;         264 AA.
AC   C5FTN0;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
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=MCYG_06052;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; DS995705; EEQ33233.1; -; Genomic_DNA.
DR   RefSeq; XP_002846183.1; XM_002846137.1.
DR   AlphaFoldDB; C5FTN0; -.
DR   SMR; C5FTN0; -.
DR   STRING; 63405.XP_002846183.1; -.
DR   EnsemblFungi; EEQ33233; EEQ33233; MCYG_06052.
DR   GeneID; 9227065; -.
DR   eggNOG; KOG4169; Eukaryota.
DR   HOGENOM; CLU_010194_1_0_1; -.
DR   OMA; KAGCAYF; -.
DR   OrthoDB; 1226147at2759; -.
DR   UniPathway; UPA00327; -.
DR   Proteomes; UP000002035; 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   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Alkaloid metabolism; NAD; Oxidoreductase; Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..264
FT                   /note="Chanoclavine-I dehydrogenase easD"
FT                   /id="PRO_0000439129"
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   264 AA;  28214 MW;  79E457CF201A19CB CRC64;
     MASVSSKIFA ITGGASGIGA ATCHLLARRG AAALCIGDLS NENMKQLEKS IREINPETKV
     HCTVLDVSSS SEVDKWVKDI ISTFGDLHGA ANVAGIAQGA GMRQIPTLLE EDDEQWKKVF
     QVNLDGILYA TRAQVRAMKD SSSTSPGDRS IVNVASIASM AHMPDVFAYG TSKAGCAYFT
     TCVAQDVIPL GIRANTVSPG ITRTPMLPRF VPNAKTQEEV EETYKKEGFS VIEADDVART
     IVWLLSEDSR PVFGTNINVG ACMP