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EASD_CLAPU
ID   EASD_CLAPU              Reviewed;         261 AA.
AC   O94207;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 84.
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   AltName: Full=Oxidoreductase 2 {ECO:0000303|PubMed:10071219};
DE   Flags: Precursor;
GN   Name=easD {ECO:0000303|PubMed:17720822};
GN   Synonyms=cpox2 {ECO:0000303|PubMed:10071219};
OS   Claviceps purpurea (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=5111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND IDENTIFICATION IN THE EAS
RP   CLUSTER.
RC   STRAIN=P1 / 1029/N5;
RX   PubMed=10071219; DOI=10.1007/s004380050950;
RA   Tudzynski P., Hoelter K., Correia T.H., Arntz C., Grammel N., Keller U.;
RT   "Evidence for an ergot alkaloid gene cluster in Claviceps purpurea.";
RL   Mol. Gen. Genet. 261:133-141(1999).
RN   [2]
RP   BIOTECHNOLOGY.
RC   STRAIN=P1 / 1029/N5;
RX   PubMed=11778866; DOI=10.1007/s002530100801;
RA   Tudzynski P., Correia T., Keller U.;
RT   "Biotechnology and genetics of ergot alkaloids.";
RL   Appl. Microbiol. Biotechnol. 57:593-605(2001).
RN   [3]
RP   FUNCTION.
RX   PubMed=14700635; DOI=10.1016/j.chembiol.2003.11.013;
RA   Correia T., Grammel N., Ortel I., Keller U., Tudzynski P.;
RT   "Molecular cloning and analysis of the ergopeptine assembly system in the
RT   ergot fungus Claviceps purpurea.";
RL   Chem. Biol. 10:1281-1292(2003).
RN   [4]
RP   FUNCTION.
RC   STRAIN=ATCC 20102 / Farmitalia FI 32/17;
RX   PubMed=14732265; DOI=10.1016/j.fgb.2003.10.002;
RA   Wang J., Machado C., Panaccione D.G., Tsai H.-F., Schardl C.L.;
RT   "The determinant step in ergot alkaloid biosynthesis by an endophyte of
RT   perennial ryegrass.";
RL   Fungal Genet. Biol. 41:189-198(2004).
RN   [5]
RP   FUNCTION, AND IDENTIFICATION IN THE EAS CLUSTER.
RX   PubMed=15904941; DOI=10.1016/j.phytochem.2005.04.011;
RA   Haarmann T., Machado C., Lubbe Y., Correia T., Schardl C.L.,
RA   Panaccione D.G., Tudzynski P.;
RT   "The ergot alkaloid gene cluster in Claviceps purpurea: extension of the
RT   cluster sequence and intra species evolution.";
RL   Phytochemistry 66:1312-1320(2005).
RN   [6]
RP   FUNCTION.
RC   STRAIN=P1 / 1029/N5;
RX   PubMed=16538694; DOI=10.1002/cbic.200500487;
RA   Haarmann T., Ortel I., Tudzynski P., Keller U.;
RT   "Identification of the cytochrome P450 monooxygenase that bridges the
RT   clavine and ergoline alkaloid pathways.";
RL   ChemBioChem 7:645-652(2006).
RN   [7]
RP   FUNCTION.
RX   PubMed=17308187; DOI=10.1128/aem.00257-07;
RA   Fleetwood D.J., Scott B., Lane G.A., Tanaka A., Johnson R.D.;
RT   "A complex ergovaline gene cluster in epichloe endophytes of grasses.";
RL   Appl. Environ. Microbiol. 73:2571-2579(2007).
RN   [8]
RP   FUNCTION.
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).
RN   [9]
RP   FUNCTION.
RX   PubMed=17560817; DOI=10.1016/j.fgb.2007.04.008;
RA   Haarmann T., Lorenz N., Tudzynski P.;
RT   "Use of a nonhomologous end joining deficient strain (Deltaku70) of the
RT   ergot fungus Claviceps purpurea for identification of a nonribosomal
RT   peptide synthetase gene involved in ergotamine biosynthesis.";
RL   Fungal Genet. Biol. 45:35-44(2008).
RN   [10]
RP   FUNCTION.
RX   PubMed=19139103; DOI=10.1074/jbc.m807168200;
RA   Ortel I., Keller U.;
RT   "Combinatorial assembly of simple and complex D-lysergic acid alkaloid
RT   peptide classes in the ergot fungus Claviceps purpurea.";
RL   J. Biol. Chem. 284:6650-6660(2009).
RN   [11]
RP   FUNCTION.
RX   PubMed=20118373; DOI=10.1128/aem.00737-09;
RA   Lorenz N., Olsovska J., Sulc M., Tudzynski P.;
RT   "Alkaloid cluster gene ccsA of the ergot fungus Claviceps purpurea encodes
RT   chanoclavine I synthase, a flavin adenine dinucleotide-containing
RT   oxidoreductase mediating the transformation of N-methyl-
RT   dimethylallyltryptophan to chanoclavine I.";
RL   Appl. Environ. Microbiol. 76:1822-1830(2010).
RN   [12]
RP   FUNCTION.
RC   STRAIN=ATCC 20102 / Farmitalia FI 32/17;
RX   PubMed=20735127; DOI=10.1021/ja105785p;
RA   Cheng J.Z., Coyle C.M., Panaccione D.G., O'Connor S.E.;
RT   "Controlling a structural branch point in ergot alkaloid biosynthesis.";
RL   J. Am. Chem. Soc. 132:12835-12837(2010).
RN   [13]
RP   FUNCTION.
RX   PubMed=21409592; DOI=10.1007/s00294-011-0336-4;
RA   Goetz K.E., Coyle C.M., Cheng J.Z., O'Connor S.E., Panaccione D.G.;
RT   "Ergot cluster-encoded catalase is required for synthesis of chanoclavine-I
RT   in Aspergillus fumigatus.";
RL   Curr. Genet. 57:201-211(2011).
RN   [14]
RP   FUNCTION.
RX   PubMed=21494745; DOI=10.1039/c0ob01215g;
RA   Matuschek M., Wallwey C., Xie X., Li S.M.;
RT   "New insights into ergot alkaloid biosynthesis in Claviceps purpurea: an
RT   agroclavine synthase EasG catalyses, via a non-enzymatic adduct with
RT   reduced glutathione, the conversion of chanoclavine-I aldehyde to
RT   agroclavine.";
RL   Org. Biomol. Chem. 9:4328-4335(2011).
RN   [15]
RP   FUNCTION.
RX   PubMed=24361048; DOI=10.1016/j.chembiol.2013.11.008;
RA   Havemann J., Vogel D., Loll B., Keller U.;
RT   "Cyclolization of D-lysergic acid alkaloid peptides.";
RL   Chem. Biol. 21:146-155(2014).
CC   -!- FUNCTION: Chanoclavine-I dehydrogenase; part of the gene cluster that
CC       mediates the biosynthesis of fungal ergot alkaloid (PubMed:10071219,
CC       PubMed:14732265, PubMed:14700635, PubMed:15904941, PubMed:17308187,
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 (PubMed:14732265). 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 (PubMed:20118373,
CC       PubMed:21409592). Agroclavine dehydrogenase easG then mediates the
CC       conversion of chanoclavine-I aldehyde to agroclavine via a non-
CC       enzymatic adduct reaction: the substrate is an iminium intermediate
CC       that is formed spontaneously from chanoclavine-I aldehyde in the
CC       presence of glutathione (PubMed:20735127, PubMed:21494745). The
CC       presence of easA is not required to complete this reaction
CC       (PubMed:21494745). Further conversion of agroclavine to paspalic acid
CC       is a two-step process involving oxidation of agroclavine to
CC       elymoclavine and of elymoclavine to paspalic acid, the second step
CC       being performed by the elymoclavine oxidase cloA (PubMed:16538694,
CC       PubMed:17720822). Paspalic acid is then further converted to D-lysergic
CC       acid (PubMed:15904941). Ergopeptines are assembled from D-lysergic acid
CC       and three different amino acids by the D-lysergyl-peptide-synthetases
CC       composed each of a monomudular and a trimodular nonribosomal peptide
CC       synthetase subunit (PubMed:14700635, PubMed:15904941). LpsB and lpsC
CC       encode the monomodular subunits responsible for D-lysergic acid
CC       activation and incorporation into the ergopeptine backbone
CC       (PubMed:14700635). LpsA1 and A2 subunits encode the trimodular
CC       nonribosomal peptide synthetase assembling the tripeptide portion of
CC       ergopeptines (PubMed:14700635). LpsA1 is responsible for formation of
CC       the major ergopeptine, ergotamine, and lpsA2 for alpha-ergocryptine,
CC       the minor ergopeptine of the total alkaloid mixture elaborated by
CC       C.purpurea (PubMed:17560817, PubMed:19139103). D-lysergyl-tripeptides
CC       are assembled by the nonribosomal peptide synthetases and released as
CC       N-(D-lysergyl-aminoacyl)-lactams (PubMed:24361048). Cyclolization of
CC       the D-lysergyl-tripeptides is performed by the Fe(2+)/2-ketoglutarate-
CC       dependent dioxygenase easH which introduces a hydroxyl group into N-(D-
CC       lysergyl-aminoacyl)-lactam at alpha-C of the aminoacyl residue followed
CC       by spontaneous condensation with the terminal lactam carbonyl group
CC       (PubMed:24361048). {ECO:0000250|UniProtKB:Q50EL0,
CC       ECO:0000269|PubMed:10071219, ECO:0000269|PubMed:14700635,
CC       ECO:0000269|PubMed:14732265, ECO:0000269|PubMed:15904941,
CC       ECO:0000269|PubMed:16538694, ECO:0000269|PubMed:17560817,
CC       ECO:0000269|PubMed:19139103, ECO:0000269|PubMed:20118373,
CC       ECO:0000269|PubMed:20735127, ECO:0000269|PubMed:21409592,
CC       ECO:0000269|PubMed:21494745, ECO:0000269|PubMed:24361048,
CC       ECO:0000305|PubMed:17308187, ECO:0000305|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:10071219}.
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; AJ011966; CAB39316.1; -; Genomic_DNA.
DR   AlphaFoldDB; O94207; -.
DR   SMR; O94207; -.
DR   VEuPathDB; FungiDB:CPUR_04080; -.
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_0000439127"
FT   ACT_SITE        166
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"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   261 AA;  27619 MW;  52F2978F64D5D992 CRC64;
     MPSMTSKVFA ITGGASGIGA ATCRLLAERD AAVICLADVS STNFTSLQES IAKSNPSTLV
     HCTELDVRSA DKVDQWLQSI VSTHGDLHGA ANVAGIAQGA GLRATPTILE ENDAEWSRIL
     DVNLNGVFYS TRAQVRVMKD LPPGHRSIVN VASIAAFSHV PDVYAYGTSK SACAYLTTCI
     AADVFWSGIR VNCVSPGITN TPMLPQFEPK AKSLDAIKDM YRDQGYPTGE ADGVARTIVW
     LLSEDSIPVY GANINVGACP P
 
 
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