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EASE_CLAP2
ID   EASE_CLAP2              Reviewed;         483 AA.
AC   M1W0X9; G8GV65;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=FAD-linked oxidoreductase easE {ECO:0000303|PubMed:10071219};
DE            EC=1.-.-.- {ECO:0000269|PubMed:20118373};
DE   AltName: Full=Chanoclavine I synthase {ECO:0000303|PubMed:20118373};
DE   AltName: Full=Ergot alkaloid synthesis protein E {ECO:0000303|PubMed:20735127};
DE   AltName: Full=Oxidoreductase 1 {ECO:0000303|PubMed:10071219};
GN   Name=easE {ECO:0000303|PubMed:20735127};
GN   Synonyms=ccsA {ECO:0000303|PubMed:20118373},
GN   cpox1 {ECO:0000303|PubMed:10071219}; ORFNames=CPUR_04079;
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=1111077;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=20.1;
RA   Florea S., Oeser B., Tudzynski P., Schardl C.L.;
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1;
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA   Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA   Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA   O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA   Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA   Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA   Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA   Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA   Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT   Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
RN   [3]
RP   IDENTIFICATION IN THE EAS CLUSTER, AND FUNCTION.
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   [4]
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   [5]
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   [6]
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   [7]
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   [8]
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   [9]
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   [10]
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   [11]
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   [12]
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   [13]
RP   FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
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   [14]
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   [15]
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   [16]
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   [17]
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: FAD-linked oxidoreductase; 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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC       {ECO:0000269|PubMed:20118373}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of clavine alkaloids but
CC       also of more complex alkaloids such as ergopeptines (PubMed:20118373).
CC       Accumulates N-methyl-dimethylallyltryptophan (Me-DMAT) and traces of
CC       dimethylallyltryptophan (DMAT) (PubMed:20118373).
CC       {ECO:0000269|PubMed:20118373}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AET79192.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; JN186799; AET79192.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CAGA01000020; CCE30231.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1W0X9; -.
DR   SMR; M1W0X9; -.
DR   STRING; 1111077.M1W0X9; -.
DR   EnsemblFungi; CCE30231; CCE30231; CPUR_04079.
DR   VEuPathDB; FungiDB:CPUR_04079; -.
DR   eggNOG; ENOG502QQWK; Eukaryota.
DR   HOGENOM; CLU_018354_4_4_1; -.
DR   OrthoDB; 827142at2759; -.
DR   BioCyc; MetaCyc:MON-17449; -.
DR   UniPathway; UPA00327; -.
DR   Proteomes; UP000016801; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035835; P:indole alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.465.10; -; 2.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   1: Evidence at protein level;
KW   Alkaloid metabolism; FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..483
FT                   /note="FAD-linked oxidoreductase easE"
FT                   /id="PRO_0000439133"
FT   DOMAIN          10..193
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ   SEQUENCE   483 AA;  52072 MW;  35BAAD3C9AB48E84 CRC64;
     MERRQSICPQ GRLPFYSAVV RSTSDIQASV RFASRHNLRL VIKNTGHDSA GRSSAPHSFQ
     IHTSLLQNIS LHKNFIARGS TTGRGPAVTL GAGVMQWQAY VHGAKNGYTI LGGECPTVGA
     IGGFLQGGGV SSIHSFTRGL AVDQVLEYQV VSAKGDLITA NEDNNQDLFW ALKGGGGGTF
     GVVTEATVRV FSDDPVTVTS TKIEAAAANV LFWKEGVHEL LRLLQRFNNL HVAGQLVISA
     PTKDSLQAGL ELHFANLTDE TQAIQLLRSE ARALETHGIS ASTSVRVQRK ASSELRMKPD
     LYPPHYGILE ASVLISAATF HANDGPALIA SKLSGLTLKP NDILFTSNLG GRVSENTAIE
     IALHPAWREA AQLVTLVRVV EPSIEGKLSA LNDLTARDVP ILYSIDPAAK ISYRNLGDPQ
     EKEFQARYWG ADNYARLAAT KAAWDPSHLF MTSLGVGSEV WDAEGICRKR RGFRAKASSL
     IGM
 
 
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