{"metadata":{"accession":"A0A316E6I8","id":"A0A316E6I8_9FLAO","source_organism":{"taxId":"429344","scientificName":"Maribacter polysiphoniae","fullName":"Maribacter polysiphoniae"},"name":"2-amino-3-ketobutyrate coenzyme A ligase","description":["Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA","Involved in de novo bacterial ceramide synthesis. Catalyzes the condensation of L-serine with palmitoyl-CoA (hexadecanoyl-CoA) to produce 3-oxosphinganine. Also capable of using alanine as substrate leading to the formation of 1-deoxysphinganine (1-deoxySa). Contributes to the levels of endogenous sphingolipids in its host"],"length":397,"sequence":"MYGEIKKYLTDELTSIKDDGLYKSERIITSPQAAVITLSTGDEVINFCANNYLGLSSHPDVIQAAKDTMDTHGFGMSSVRFICGTQDIHKKLERKIAEFYETEDTILYAAAFDANGGVFEPLLGPEDAIISDSLNHASIIDGVRLCKAKRYRYANSDMADLEAQLKQTQKDKVRFKIIVTDGVFSMDGLLAPLDKICDLADKYDALVMVDECHAAGFIGKHGKGTLEEKGVMGRVDIITGTLGKALGGAMGGYTTGKKEIIELLRQRSRPYLFSNSLAPSIVGASIKVFEMLANDTALRDKLQSNTEYFKKGMKEAGFDIIDGDSAIVPVMLYDAKLSQRMADLLLEEGIYVIGFYYPVVPKGKARIRVQLSAAHEIEHLNKAIKAFIKVGQQLNIV","proteome":"UP000651837","gene":"kbl","go_terms":[{"identifier":"GO:0030170","name":"pyridoxal phosphate binding","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0009058","name":"biosynthetic process","category":{"code":"P","name":"biological_process"}},{"identifier":"GO:0008890","name":"glycine C-acetyltransferase activity","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0006567","name":"L-threonine catabolic process","category":{"code":"P","name":"biological_process"}}],"protein_evidence":3,"source_database":"unreviewed","is_fragment":false,"in_alphafold":true,"ida_accession":"220d43766bfe69807874ea078bc783ea7854e968","counters":{"domain_architectures":253926,"entries":15,"isoforms":0,"proteomes":1,"sets":2,"structures":0,"taxa":1,"dbEntries":{"ssf":1,"cathgene3d":2,"cdd":1,"pfam":1,"hamap":1,"ncbifam":2,"panther":1,"interpro":6},"proteome":1,"taxonomy":1,"similar_proteins":253926}}}