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{
"metadata": {
"accession": "C7XUL8",
"id": "C7XUL8_9LACO",
"source_organism": {
"taxId": "575594",
"scientificName": "Limosilactobacillus coleohominis 101-4-CHN",
"fullName": "Limosilactobacillus coleohominis 101-4-CHN"
},
"name": "Carbamoyl phosphate synthase large chain",
"description": [
"Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate",
"Small subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of the biosynthetic pathway leading to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate"
],
"length": 1058,
"sequence": "MPKRKDIHKIMVFGSGPIIIGQAAEFDYSGTQACLALKEEGYETVLVNSNPATIMTDNEIADHVYIEPLTVESVSRIIRQEYPDAILPTLGGQIGLNLAVALAKTGLLDELGIQLLGTKLDSIDQAEDRERFKELMQQLHEPVPASQTVSTVDEALAFAHQIGYPVIVRPAFTMGGTGGGMCHDDDEMKIIAANGLDLSPVTQCLIEKSIAGYKEIEFEVMRDAKDDAMVVCCMENFDPVGIHTGDSIVFAPNQTLSDREYQMLRDCALKLIRALKIEGGCNVQLALDPNSYHYDVIEVNPRVSRSSALASKATGYPIAKMAAKIAVGLTLDEIINPVTGTTYAEFEPALDYVVCKIPRWPFDKFTRADRILGSQMKATGEVMAIGKNAEEAFQKAVRSLEIDTKDFYLPAAHQATDVELEDKLVHAQDDRLFYIAEAFRRGYSIEDIHELTKINYYFLDIVQHLVELETTIENQPHDLKVLKQAKQYGFSDETIAHLWGTTVDAVRQLRLANGIVPVYKMVDTCAAEFASTTPYFYSTYDHENESHRSAKPAILVIGSGPIRIGQGVEFDYATVHCVKAIQRHGYEAIVMNSNPETVSTDFSISDKLYFEPLTLEDVLNVCDLEQPAGVIVQFGGQTAINLAAGLDQHGIKILGTSVQDLDAAEDRRVFDQVIKDLQLKQPVGLTATTHEGVIAAATKIGYPVLVRPSYVLGGKAMEIVYNETELEQYLQDNANVAADHPILIDAYLEGRECEVDAICDGTDVLLPGIMEHIERAGVHSGDSMAVYPPQSFDQDIKQQIVDATKKLCLALKCIGIMNIQFIIHNHEAYVLEVNPRASRTVPFLSKITGIEMAQVATRVILGESLKNQGYQDGLYREPQTVHVKAPVFSFNKLDDVDAFLGPEMKSTGEVMGSDETFEKALYKAFVGAKMKLPENGNVLLTIEDHDKQAILPIAQRFAKIGYRLLATSGTADFLQKNGLHVEVVDKLHEAGQHNILDAIRNEVDIVINTMGHDYQKTSDGFIIRQTAIEHNVPLLTALDTVDALLRALENRSFATQAL",
"proteome": "UP000003987",
"gene": "carB",
"go_terms": [
{
"identifier": "GO:0005524",
"name": "ATP binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0046872",
"name": "metal ion binding",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"protein_evidence": 3,
"source_database": "unreviewed",
"is_fragment": false,
"in_alphafold": true,
"in_bfvd": false,
"ida_accession": "1bca594174018b6e1f985c6e9a9d387c26b05753",
"counters": {
"domain_architectures": 23928,
"entries": 37,
"isoforms": 0,
"proteomes": 1,
"sets": 4,
"structures": 0,
"taxa": 1,
"dbEntries": {
"cathgene3d": 4,
"ssf": 4,
"pfam": 4,
"profile": 2,
"smart": 3,
"cdd": 1,
"ncbifam": 3,
"hamap": 1,
"panther": 1,
"prints": 1,
"prosite": 2,
"interpro": 11
},
"proteome": 1,
"taxonomy": 1,
"similar_proteins": 23928
}
}
}