{"metadata":{"accession":"I7GCS8","id":"I7GCS8_MYCS2","source_organism":{"taxId":"246196","scientificName":"Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)","fullName":"Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)"},"name":"NADP-dependent 3-hydroxy acid dehydrogenase YdfG","description":["NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L-allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimidine degradation since both are able to detoxify malonic semialdehyde"],"length":268,"sequence":"MPVPAPSPDARAVVTGASQNIGEALATELAARGHHLIITARREEVLTSLAQRLTERYGVTVEVRAVDLTDPAARATLCDELAEREISILCANAGTATFGAVKDLDPAGEKAQVQLNVLGVHDLVLAVLPGMVARRAGGILISGSAAGNSPIPNNATYAASKAFANTFSESLRGELTGVGVHVTLLAPGPVRTELPDPSEQSLVERLIPDFLWIDTEYTAKLSLDGLEHNKMRVVPGVTSKAMSVASGYAPRAIVTPIVGAVYKKLGGG","proteome":null,"gene":"MSMEI_4605","go_terms":null,"protein_evidence":3,"source_database":"unreviewed","is_fragment":false,"in_alphafold":true,"in_bfvd":false,"ida_accession":"a0c95b509a3fe852564663f48768d986938c9d65","counters":{"domain_architectures":599639,"entries":11,"isoforms":0,"proteomes":0,"sets":1,"structures":0,"taxa":1,"dbEntries":{"cathgene3d":1,"ssf":1,"pfam":1,"ncbifam":1,"panther":1,"pirsf":1,"prints":1,"prosite":1,"interpro":3},"proteome":0,"taxonomy":1,"similar_proteins":599639}}}