EASA_CLAFS
ID EASA_CLAFS Reviewed; 382 AA.
AC A8C7R3;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Probable inactive dehydrogenase easA {ECO:0000250|UniProtKB:Q6ZXC1};
DE AltName: Full=Ergot alkaloid biosynthesis protein A {ECO:0000303|PubMed:17720822};
GN Name=easA {ECO:0000303|PubMed:17720822};
OS Claviceps fusiformis (Ergot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=40602;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 26245 / DSM 2942 / CBS 164.59;
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).
CC -!- FUNCTION: Probable inactive dehydrogenase; part of the gene cluster
CC that mediates the biosynthesis of fungal ergot alkaloid
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 (By similarity). 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 (By similarity). Agroclavine
CC dehydrogenase easG then mediates the conversion of chanoclavine-I
CC aldehyde to agroclavine via a non-enzymatic adduct reaction: the
CC substrate is an iminium intermediate that is formed spontaneously from
CC chanoclavine-I aldehyde in the presence of glutathione (By similarity).
CC Further conversion of agroclavine to paspalic acid is a two-step
CC process involving oxidation of agroclavine to elymoclavine and of
CC elymoclavine to paspalic acid, the second step being performed by the
CC elymoclavine oxidase cloA (PubMed:17720822). However, cloA does not
CC encode a functional enzyme indicating that C.fusiformis terminates its
CC ergot alkaloid pathway at elymoclavine (PubMed:17720822).
CC {ECO:0000250|UniProtKB:Q6ZXC1, ECO:0000269|PubMed:17720822}.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the family, lacks the
CC conserved Tyr active site at position 176 which is replaced by a Phe
CC residue. {ECO:0000305}.
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DR EMBL; EU006773; ABV57819.1; -; Genomic_DNA.
DR AlphaFoldDB; A8C7R3; -.
DR SMR; A8C7R3; -.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR InterPro; IPR045247; Oye-like.
DR PANTHER; PTHR22893; PTHR22893; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
PE 3: Inferred from homology;
KW Flavoprotein; FMN.
FT CHAIN 1..382
FT /note="Probable inactive dehydrogenase easA"
FT /id="PRO_0000439119"
FT BINDING 25..27
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 60
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 102
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 171
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 223
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 299
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 324..325
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q4WZ70"
FT BINDING 325
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 352
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
SQ SEQUENCE 382 AA; 42938 MW; C29134064F09F31C CRC64;
MSSSNLFKPI PLGRKVLQHK VVLSPMTRFR ADNDGVPLSY VKSYYGQRAS IRGTLLITEA
VAICPRAKGF SNCPGIWHQD QIAAWKEVVD EVHSKGSVIW LQLWATGRAS DADTLKESGF
HLESSSDVPV APGEPVPRPL SEDEIESYIR DYVTGAINAV QGAGFDGIEI HGANGFLVDQ
FLQASCNTRA DQWGGSIENR SRFGLEITRR VVDAVGKDRV GVKLSPWSTF QGMGTMDDLV
AQFEHFISRL REMDIAYIHL VNTRWLEEEE PGIKTHPDVD NQTFVRMWGN KTPILLAGGY
DADSARRLVD ETYSDQNNIM VVFGRHYISN PDLPFRLRLG IPLQKYNRDT FYIPFSDEGY
LDYPFCQEFL DQQDVDQVVV AA
