EASD_ARTBC
ID EASD_ARTBC Reviewed; 246 AA.
AC D4AK45;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Chanoclavine-I dehydrogenase easD {ECO:0000303|PubMed:22403186};
DE Short=ChaDH {ECO:0000250|UniProtKB:Q4WZ66};
DE EC=1.1.1.332 {ECO:0000269|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=ARB_04646;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
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, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
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:0000269|PubMed:22403186};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.09 mM for chanoclavine-I {ECO:0000269|PubMed:22403186};
CC KM=0.36 mM for NAD(+) {ECO:0000269|PubMed:22403186};
CC -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC {ECO:0000269|PubMed:22403186}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:22403186}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABSU01000001; EFE37118.1; -; Genomic_DNA.
DR RefSeq; XP_003017763.1; XM_003017717.1.
DR AlphaFoldDB; D4AK45; -.
DR SMR; D4AK45; -.
DR STRING; 663331.D4AK45; -.
DR EnsemblFungi; EFE37118; EFE37118; ARB_04646.
DR GeneID; 9522609; -.
DR KEGG; abe:ARB_04646; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_0_1; -.
DR OMA; KAGCAYF; -.
DR BioCyc; MetaCyc:MON-17445; -.
DR BRENDA; 1.1.1.332; 13006.
DR UniPathway; UPA00327; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0035837; P:ergot alkaloid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Alkaloid metabolism; NAD; Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..246
FT /note="Chanoclavine-I dehydrogenase easD"
FT /id="PRO_0000421748"
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 246 AA; 26236 MW; CC24ABFECBB107F6 CRC64;
MASVSSKIFA ITGGASGIGA ATCRLLAKRG AATLCVGDLC SENMKQLEND IKEINPNTKV
HCTVLDVSSS SNVDEWIKDI ITTFGDLHGA ANIAGIAQGA GLRQAPTILE EDDQQWKKVF
QVNLDGVLYS TRAQVRAMKE SSSTNPGDRS IVNVASIASM SHMPDVFAYG TSKAGCAYFT
TCVSQDVMPF GIRANTVSPE EVEETYKKEG FSVIEADDVA RTIVWLLSED SRPVFGANIN
VGACMP
