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InterPro-Version: 108.0
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{
"metadata": {
"accession": "X1WI34",
"id": "X1WI34_HUMAN",
"source_organism": {
"taxId": "9606",
"scientificName": "Homo sapiens",
"fullName": "Homo sapiens (Human)"
},
"name": "Mitochondrial amidoxime reducing component 2",
"description": [
"Catalyzes the reduction of N-oxygenated molecules, acting as a counterpart of cytochrome P450 and flavin-containing monooxygenases in metabolic cycles. As a component of prodrug-converting system, reduces a multitude of N-hydroxylated prodrugs particularly amidoximes, leading to increased drug bioavailability. May be involved in mitochondrial N(omega)-hydroxy-L-arginine (NOHA) reduction, regulating endogenous nitric oxide levels and biosynthesis. Postulated to cleave the N-OH bond of N-hydroxylated substrates in concert with electron transfer from NADH to cytochrome b5 reductase then to cytochrome b5, the ultimate electron donor that primes the active site for substrate reduction"
],
"length": 172,
"sequence": "GHMVTARQEPRLVLISIIYENNCLIFRAPDMDQLVLPSKQPSSNKLHNCRIFGLDIKGRDCGNEAAKWFTNFLKTEAYRLVQFETNMKGRTSRKLLPTLDQNFQVAYPDYCPLLIMTDASLVDLNTRMEKKMKMENFRPNIVVTGCDAFEEDTWDELLIGSVEVKKVMACPR",
"proteome": "UP000005640",
"gene": "MTARC2",
"go_terms": [
{
"identifier": "GO:0003824",
"name": "catalytic activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0030151",
"name": "molybdenum ion binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0030170",
"name": "pyridoxal phosphate binding",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"protein_evidence": 1,
"source_database": "unreviewed",
"is_fragment": true,
"in_alphafold": true,
"in_bfvd": false,
"ida_accession": "0b0205da14fc2aee6cf754d0f9bc7ba3066cf796",
"counters": {
"domain_architectures": 16466,
"entries": 7,
"isoforms": 0,
"proteomes": 1,
"sets": 1,
"structures": 0,
"taxa": 1,
"dbEntries": {
"pfam": 2,
"ssf": 1,
"profile": 1,
"panther": 1,
"interpro": 2
},
"proteome": 1,
"taxonomy": 1,
"similar_proteins": 16466
}
}
}