{"metadata":{"accession":"A0A7U9DKB5","id":"A0A7U9DKB5_STRLI","source_organism":{"taxId":"1200984","scientificName":"Streptomyces lividans 1326","fullName":"Streptomyces lividans 1326"},"name":"threonine ammonia-lyase","description":["Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA"],"length":325,"sequence":"MTTTTPPVTLDDVRSAAARIKGVAHRTPVLRSRTLDALVGAEVHLKCENQQRVGAFKFRGAYNAASRLTPEQLARGIAAYSSGNHAQAVALAARELGTTAVIVMPEDAPPSKRDATAGYGAEIVTYDRYTGDRVAVAEALAADRGLTLIPPYEHPHVIAGQGTAALELVEETGELDALVAPVGGGGLIAGSATAVKALHPGMRVIGVEPEAGDDTRRSLAAGRRVSVPVPRTIADGQALPTPGELTFSLNRRLLDGIVLVSDDEIRDAMRFAFERLKTVLEPSGATPLAALMNGRIDALPRRVGVILSGGNVDAARFAELCGAPR","proteome":null,"gene":"SLI_0805","go_terms":[{"identifier":"GO:0030170","name":"pyridoxal phosphate binding","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0006520","name":"amino acid metabolic process","category":{"code":"P","name":"biological_process"}}],"protein_evidence":3,"source_database":"unreviewed","is_fragment":false,"in_alphafold":true,"in_bfvd":false,"ida_accession":"8bc361cd7c1d6142f8798dedc919bc5496ed8194","counters":{"domain_architectures":181949,"entries":9,"isoforms":0,"proteomes":0,"sets":2,"structures":0,"taxa":1,"dbEntries":{"ssf":1,"cdd":1,"cathgene3d":1,"panther":1,"pfam":1,"prosite":1,"interpro":3},"proteome":0,"taxonomy":1,"similar_proteins":181949}}}