EASC_ARTOC
ID EASC_ARTOC Reviewed; 482 AA.
AC C5FTM9;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Catalase easC {ECO:0000303|PubMed:22403186};
DE EC=1.11.-.- {ECO:0000305|PubMed:22403186};
DE AltName: Full=Ergot alkaloid synthesis protein C {ECO:0000303|PubMed:22403186};
GN Name=easC {ECO:0000303|PubMed:22403186}; ORFNames=MCYG_06051;
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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: Catalase; part of the gene cluster that mediates the
CC biosynthesis of fungal ergot alkaloid (PubMed:22403186). 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 (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=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P15202};
CC -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC {ECO:0000305|PubMed:22403186}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; DS995705; EEQ33232.1; -; Genomic_DNA.
DR RefSeq; XP_002846182.1; XM_002846136.1.
DR AlphaFoldDB; C5FTM9; -.
DR SMR; C5FTM9; -.
DR STRING; 63405.XP_002846182.1; -.
DR EnsemblFungi; EEQ33232; EEQ33232; MCYG_06051.
DR GeneID; 9227064; -.
DR eggNOG; KOG0047; Eukaryota.
DR HOGENOM; CLU_010645_2_0_1; -.
DR OMA; GSFKYVH; -.
DR OrthoDB; 507937at2759; -.
DR UniPathway; UPA00327; -.
DR Proteomes; UP000002035; Unassembled WGS sequence.
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; Reference proteome.
FT CHAIN 1..482
FT /note="Catalase easC"
FT /id="PRO_0000439124"
FT ACT_SITE 58
FT /evidence="ECO:0000250|UniProtKB:P15202"
FT BINDING 347
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 482 AA; 54898 MW; F6DB348651D64A1F CRC64;
MAPNAADKCP VMNNAAEKCP VMHSNGVSSI QSHGPRDIYT LEALSHFNRE KIPERAVHAK
GTGAYGEFEV TADISDICNV DMLLGVGKKT QCVTRFSTTG LERGSSDGVR DLKGMAVKFF
TEQGDWDWVS LNFPFFFIRD PAKFPDMIHS QRRDPQTNLL NPSMTWDFVT KNPEALHMTL
LQHSDFGTMF TWRTLSSYAG HAFKWVMPDG SFKYVHFFLA SDRGPNFTDG STAKIDPNDP
DFATKDLFEA IERGDYPTWT ANVQVIDPKD APKLGFNILD ITKHWNLGTY PKGLDTIPSR
PFGKLTLNRN VKDYFTEVEK LAFSPSNLVP GVEPSEDPIL QARMFAYPDA QRYRLGIDHL
KAPIRRKETS CKHDLGPEFD QWLSQVTSES WSHPHEDDYK FAREYYEVLP EFRSQEFQDR
MVENLYKSVA QGPEDLRKRV YETFELVSTE LARRVREGAE VIVADMAQPD SPERAQPGQQ
RL
