{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P39831","secondaryAccessions":["P77149","P78161","P78162"],"uniProtkbId":"YDFG_ECOLI","entryAudit":{"firstPublicDate":"1995-02-01","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"1997-11-01","entryVersion":171,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12535615"}],"value":"NADP-dependent 3-hydroxy acid dehydrogenase YdfG"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12535615"}],"value":"L-allo-threonine dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12535615"}],"value":"1.1.1.381"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"20400551"}],"value":"Malonic semialdehyde reductase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"20400551"}],"value":"1.1.1.298"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21349860"}],"value":"Serine 3-dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21349860"}],"value":"SerDH"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12535615"}],"value":"1.1.1.276"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAC74612.1"}],"value":"ydfG"},"orderedLocusNames":[{"value":"b1539"},{"value":"JW1532"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12535615"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20400551"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21349860"}],"value":"NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids (PubMed:12535615, PubMed:21349860). Catalyzes the NADP-dependent oxidation of L-allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone (PubMed:12535615). The highest catalytic efficiency is observed with L-allo-threonine, but the enzyme also acts in vitro on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate (PubMed:12535615, PubMed:21349860). It cannot use L-threonine, D-allo-threonine, DL-threo-3-phenyl-serine, malonate, DL-malate, citrate, isocitrate, DL-lactate, DL-tartrate, gluconate, glycerol or glycolate (PubMed:12535615). It is specific for NADP(+) and cannot use NAD(+) (PubMed:12535615). In addition, is able to detoxify malonic semialdehyde (3-oxopropanoate) by catalyzing the reduction of malonic semialdehyde to 3-hydroxypropionic acid (PubMed:20400551). This function overlaps with that of RutE, as both enzymes can reduce malonic semialdehyde to 3-hydroxypropionic acid, and YdfG is likely to be involved in the Rut pathway for pyrimidine degradation under certain circumstances (PubMed:20400551)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-allo-threonine + NADP(+) = aminoacetone + CO2 + NADPH","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43524"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58320"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:58585"}],"ecNumber":"1.1.1.381","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12535615"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-allo-threonine + NADP(+) = (2S)-2-amino-3-oxobutanoate + NADPH + 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as substrate (PubMed:21349860). kcat is 4.20 sec(-1) with L-serine as substrate (PubMed:12535615). kcat is 3.9 sec(-1) with L-serine as substrate (PubMed:21349860). kcat is 3.50 sec(-1) with D-serine as substrate (PubMed:12535615). kcat is 6.55 sec(-1) with D-threonine as substrate (PubMed:12535615). kcat is 5.76 sec(-1) with L-allo-threonine as substrate (PubMed:12535615). kcat is 1.17 sec(-1) with L-glycerate as substrate (PubMed:12535615). kcat is 2.01 sec(-1) with D-glycerate as substrate (PubMed:12535615). kcat is 4.03 sec(-1) with L-3-hydroxyisobutyrate as substrate (PubMed:12535615). kcat is 3.78 sec(-1) with D-3-hydroxyisobutyrate as substrate (PubMed:12535615)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12535615"}],"value":"Optimum pH is about 8.5 for the oxidation of L-serine (PubMed:12535615). Stable from pH 6.5 to 10.0 (PubMed:12535615)."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12535615"}],"value":"Still active after heating at 55 degrees Celsius for 80 minutes."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12535615"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21349860"}],"value":"Homotetramer (PubMed:12535615, PubMed:21349860). 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