EASE_TRIVH
ID EASE_TRIVH Reviewed; 604 AA.
AC D4D448;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=FAD-linked oxidoreductase easE {ECO:0000303|PubMed:22403186};
DE EC=1.-.-.- {ECO:0000305|PubMed:22403186};
DE AltName: Full=Chanoclavine I synthase {ECO:0000305};
DE AltName: Full=Ergot alkaloid synthesis protein E {ECO:0000303|PubMed:22403186};
DE Flags: Precursor;
GN Name=easE {ECO:0000303|PubMed:22403186}; ORFNames=TRV_01862;
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: FAD-linked oxidoreductase; 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC {ECO:0000305|PubMed:22403186}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; ACYE01000098; EFE43382.1; -; Genomic_DNA.
DR RefSeq; XP_003024000.1; XM_003023954.1.
DR AlphaFoldDB; D4D448; -.
DR SMR; D4D448; -.
DR EnsemblFungi; EFE43382; EFE43382; TRV_01862.
DR GeneID; 9582693; -.
DR KEGG; tve:TRV_01862; -.
DR HOGENOM; CLU_018354_4_4_1; -.
DR UniPathway; UPA00327; -.
DR Proteomes; UP000008383; 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 3: Inferred from homology;
KW Alkaloid metabolism; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..604
FT /note="FAD-linked oxidoreductase easE"
FT /id="PRO_5003055965"
FT DOMAIN 125..308
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 604 AA; 66578 MW; 39BEC8900B2CD63A CRC64;
MQFLLWSTGL VALLSWLIYT QETQSASCRC RPWESCWPSE ELWNSFNTSV DGKLHRLRPA
AHVCYGPSFN RSACDNILLL SRDSGWRASN PGVLQDWVWE AGETANESCP VGSLRTASAV
NSCHQGRIPL FTVGVESTKQ VQEAVRFARK HKLRLVIRNT GHDLAGRSSA PDSFQIHTHR
LQEIQFHADM RLDGSNTSLG PAVTVGAGVM MGDLYAQAAR HGYMVLGGDC PTVGVVGGFL
QGGGISDFLS LNQGFGVDNV LEYEVVTADG ELVVANALQN QDLFWALRGG GGGTFGVVTR
ATMRVFPDVP VVISEILLEA PQAISSSWTQ GLSIVLTALQ SLNHDNVGGQ LVIAVLPNLA
VQASIKFFFL DATEAAVIDR RMKPFLTKLS RANVKYTYSS KNLPHFSSNY RQVPDIHSDN
DYGVLGSTVA ISQQLFDSPQ GPEKVAKALA NLPVSAGDLI FTSNLGGRVI RNGELAETSM
HPAWRSASQL INYVHTVEPS IEGRAKARER LTNTQMPMLY ALDPNIKLSY RNVGDPNEKD
FQQIYWGPNY GRLSNIKKKW DTDDLFFSKL GVGSERWDSE ESDEVYFFSY FYLEGINTLK
VARR
