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{
"metadata": {
"accession": "M1WA44",
"id": "EASC_CLAP2",
"source_organism": {
"taxId": "1111077",
"scientificName": "Claviceps purpurea (strain 20.1)",
"fullName": "Claviceps purpurea (strain 20.1) (Ergot fungus)"
},
"name": "Catalase easC",
"description": [
"Catalase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:14700635, PubMed:14732265, PubMed:15904941, PubMed:17308187, PubMed:17720822). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:14732265). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20118373, PubMed:21409592). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (PubMed:20735127, PubMed:21494745). The presence of easA is not required to complete this reaction (PubMed:21494745). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (PubMed:16538694, PubMed:17720822). Paspalic acid is then further converted to D-lysergic acid (PubMed:15904941). Ergopeptines are assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetases composed each of a monomudular and a trimodular nonribosomal peptide synthetase subunit (PubMed:14700635, PubMed:15904941). LpsB and lpsC encode the monomodular subunits responsible for D-lysergic acid activation and incorporation into the ergopeptine backbone (PubMed:14700635). LpsA1 and A2 subunits encode the trimodular nonribosomal peptide synthetase assembling the tripeptide portion of ergopeptines (PubMed:14700635). LpsA1 is responsible for formation of the major ergopeptine, ergotamine, and lpsA2 for alpha-ergocryptine, the minor ergopeptine of the total alkaloid mixture elaborated by C.purpurea (PubMed:17560817, PubMed:19139103). D-lysergyl-tripeptides are assembled by the nonribosomal peptide synthetases and released as N-(D-lysergyl-aminoacyl)-lactams (PubMed:24361048). Cyclolization of the D-lysergyl-tripeptides is performed by the Fe(2+)/2-ketoglutarate-dependent dioxygenase easH which introduces a hydroxyl group into N-(D-lysergyl-aminoacyl)-lactam at alpha-C of the aminoacyl residue followed by spontaneous condensation with the terminal lactam carbonyl group (PubMed:24361048)"
],
"length": 473,
"sequence": "MASEVSVASSGSEHSGAQKCPFQDPGLSSMDQDSRLRDILSRFNREKIPERAVHARGAGAYGEFEVTHDVSDICDIDMLLGVGKKTPCVVRFSTTTLERGSAESVRDVKGMAIKHFTQDGNWDWVCLNIPMFFIRDPSKFPDMVHAQRPDPTTNVANPSRWWEFVCNNHETLHMVMFQFSDFGTMFDYRSMSGYAAHAYKWVMPDGSWKYVHWFLASDQGPNFETGHQAKQIGADDAESATRDLYQSLERGEYPSWTVKVQVVDPEDAPKLPFNILDVTKHWNLGNYPPDIDVIPGRTLGKLTLKKGPQDYFEEIEQLAFSPSRLVHGVEASEDPMLQARLFAYPDAQKHRLGPNNLDLPANRTKKLADGSRPEKAEMAPQKVPSQEHADWVSQVKSSSWSEPNETDYKFPREFWKALPRLRGEAFQNSLVVNMAKSVSQVPADMRQKVYSTLALIADDLADRVRTMTEEIVE",
"proteome": "UP000016801",
"gene": "easC",
"go_terms": [
{
"identifier": "GO:0004096",
"name": "catalase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0020037",
"name": "heme binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0006979",
"name": "response to oxidative stress",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"protein_evidence": 3,
"source_database": "reviewed",
"is_fragment": false,
"in_alphafold": true,
"ida_accession": "34c8b4937298db05a7aa509f909728c182fbbc20",
"counters": {
"domain_architectures": 5010,
"entries": 17,
"isoforms": 0,
"proteomes": 1,
"sets": 1,
"structures": 0,
"taxa": 1,
"dbEntries": {
"profile": 1,
"smart": 1,
"cathgene3d": 1,
"ssf": 1,
"cdd": 1,
"pfam": 1,
"pirsf": 1,
"panther": 1,
"prints": 1,
"prosite": 2,
"interpro": 6
},
"proteome": 1,
"taxonomy": 1,
"similar_proteins": 5010
}
}
}
