EASC_TRIVH
ID EASC_TRIVH Reviewed; 478 AA.
AC D4D445;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 52.
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=TRV_01859;
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: 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; ACYE01000098; EFE43379.1; -; Genomic_DNA.
DR RefSeq; XP_003023997.1; XM_003023951.1.
DR AlphaFoldDB; D4D445; -.
DR SMR; D4D445; -.
DR EnsemblFungi; EFE43379; EFE43379; TRV_01859.
DR GeneID; 9582690; -.
DR KEGG; tve:TRV_01859; -.
DR HOGENOM; CLU_010645_2_0_1; -.
DR UniPathway; UPA00327; -.
DR Proteomes; UP000008383; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:EnsemblFungi.
DR GO; GO:0004096; F:catalase activity; IEA:EnsemblFungi.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001315; P:age-dependent response to reactive oxygen species; IEA:EnsemblFungi.
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 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..478
FT /note="Catalase easC"
FT /id="PRO_0000439125"
FT REGION 459..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 54
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 478 AA; 54314 MW; 7E2E846A4470F822 CRC64;
MAPNAADKCP VMGNSGEKCP VMSSSTQSRG PRDIYTLEAL SHFNREKIPE RAVHAKGTGA
YGEFEVTADI SDICNIDMLL GVGKKTQCVT RFSTTGLERG SSDGVRDLKG MAVKFFTEQG
DWDWVSLNFP FFFIRDPAKF PDMIHSQRRD PQTNLLNPNM TWDFVTKNPE ALHMTLLQHS
DFGTMFTWRT LSSYVGHAFK WVMPDGSFKY VHFFLASDRG PNFTDGSTAK VDPNDPDFAT
KDLFEAIERG DYPSWTANVQ VVDPKDAPKL GFNILDLTKH WNLGTYPKGL DTIPSRPFGK
LTLNRNVKDY FSEVEKLAFS PSNLVPGVEP SEDPILQARM FAYPDAQRYR LGIDHLKAPL
RRKETACQHD LGPEFEKWLS QVTSEAWSHP HEDDYKFARE YYEVLPEFRS QEFQDRMVEN
LCKSIAPGPE ELRKRVYDTF ELVSSELARR LREGAEAIVA EKARPDSPSR AQPGQLRL
