ID   EASC_CLAFS              Reviewed;         479 AA.
AC   A8C7R6;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Catalase easC {ECO:0000303|PubMed:17720822};
DE            EC=1.11.-.- {ECO:0000305|PubMed:17720822};
DE   AltName: Full=Ergot alkaloid synthesis protein C {ECO:0000303|PubMed:17720822};
GN   Name=easC {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: Catalase; part of the gene cluster that mediates the
CC       biosynthesis of fungal ergot alkaloid (PubMed:17720822). DmaW catalyzes
CC       the first step of ergot alkaloid biosynthesis by condensing
CC       dimethylallyl diphosphate (DMAP) and tryptophan to form 4-
CC       dimethylallyl-L-tryptophan (By similarity). 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 (By similarity).
CC       The catalase easC and the FAD-dependent oxidoreductase easE then
CC       transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further
CC       oxidized by easD in the presence of NAD(+), resulting in the formation
CC       of chanoclavine-I aldehyde (By similarity). Agroclavine dehydrogenase
CC       easG then mediates the conversion of chanoclavine-I aldehyde to
CC       agroclavine via a non-enzymatic adduct reaction: the substrate is an
CC       iminium intermediate that is formed spontaneously from chanoclavine-I
CC       aldehyde in the presence of glutathione (By similarity). Further
CC       conversion of agroclavine to paspalic acid is a two-step process
CC       involving oxidation of agroclavine to elymoclavine and of elymoclavine
CC       to paspalic acid, the second step being performed by the elymoclavine
CC       oxidase cloA (PubMed:17720822). However, cloA does not encode a
CC       functional enzyme indicating that C.fusiformis terminates its ergot
CC       alkaloid pathway at elymoclavine (PubMed:17720822).
CC       {ECO:0000250|UniProtKB:Q6ZXC2, ECO:0000269|PubMed:17720822}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P15202};
CC   -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC       {ECO:0000305|PubMed:17720822}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; EU006773; ABV57821.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8C7R6; -.
DR   SMR; A8C7R6; -.
DR   UniPathway; UPA00327; -.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0035835; P:indole alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; PTHR11465; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; SSF56634; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Alkaloid metabolism; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase.
FT   CHAIN           1..479
FT                   /note="Catalase easC"
FT                   /id="PRO_0000439126"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000250|UniProtKB:P15202"
FT   BINDING         343
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P15202"
SQ   SEQUENCE   479 AA;  53982 MW;  D8CECDD76D1BE99E CRC64;
     MASQVSLTAQ GSGLSAPLNG PEHLTSTTVE NDPRLLDILS RFNREKIPER AVHARGAGAY
     GEFEVTHDVS DICDIDMLLG IGKKTPCAVR FSTTALERGS AESVRDVKGM AIKLFTGDGE
     WDWVCLNIPM FFIRDPSKFP DLVHAQRPDP ATNLANPAAW WEFVCNNHES LHMAVFLFTD
     FGTMFDYRSM SGYVSHAYKW VMPDGTWKYV HWFLASDQGP NFEQGNQTRE AAPNDSESAT
     RDLYQSLERG ECPSWTVKVQ VIDPEDAPRL AFNILDVSKH WNLGNYPPDI PVIPERCVGK
     LTLKKGPENY FEEIEKLAFS PSHLVHGVEP SEDPMLQARL FAYPDAQEHR LGPQFSDMAA
     KRTGHAANDA PKTKKPAVPL QKQSREHAEW VSQVTSSSWS QPNETDYKFP RELWAALPRL
     RGEEFQNRLV VNMAESVSQI PEDLRQKVYK TLALVAEDLA SRVESLTEEM VVPEQRPRL