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ydfG

Gene
ydfG
Protein
NADP-dependent 3-hydroxy acid dehydrogenase YdfG
Organism
Escherichia coli O157:H7
Length
248 amino acids
Function
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.
Similarity
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Mass
27.263 kDa
Sequence
MIVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWCNIDILVNNAGLALGMEPAHKASIEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLVGGTEFSNVRFKGDDGKAEKTYQNTVALTPEDVSEAVWWVSTLPAHVNINTLEMMPVTQSYAGLNVHRQ

Gene
ydfG
Protein
NADP-dependent 3-hydroxy acid dehydrogenase YdfG
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Length
248 amino acids
Function
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.
Similarity
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Mass
27.247 kDa
Sequence
MIVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWSNIDILVNNAGLALGMEPAHKASIEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLVGGTEFSNVRFKGDDGKAEKTYQNTVALTPEDVSEAVWWVSTLPAHVNINTLEMMPVTQSYAGLNVHRQ

Gene
ydfG
Protein
NADP-dependent 3-hydroxy acid dehydrogenase YdfG
Organism
Escherichia coli (strain K12)
Length
248 amino acids
Function
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 (PubMed:12535615). 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 (PubMed:20400551).
Similarity
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Mass
27.249 kDa
Sequence
MIVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWCNIDILVNNAGLALGMEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLVGGTEFSNVRFKGDDGKAEKTYQNTVALTPEDVSEAVWWVSTLPAHVNINTLEMMPVTQSYAGLNVHRQ

Gene
ydfG
Protein
NADP-dependent 3-hydroxy acid dehydrogenase YdfG
Organism
Salmonella typhi
Length
248 amino acids
Function
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.
Similarity
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Mass
27.043 kDa
Sequence
MIVLVTGATAGFGECIARRFVENGHKVIATGRRHERLQALKDELGENVLTAQLDVRNRAAIEEMMASLPAQWRDIDVLVNNAGLALGLEPAHKASVEDWETMIDTNNKGLIYMTRAVLPGMVERNRGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLVGGTEFSSVRFKGDDEKAGKTYENTTALTPEDITEAVWWVATLPAHVNINTVEMMPVTQSFAGLSVHRS

Gene
ydfG
Protein
NADP-dependent 3-hydroxy acid dehydrogenase YdfG
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
248 amino acids
Function
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.
Similarity
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Mass
27.043 kDa
Sequence
MIVLVTGATAGFGECIARRFVENGHKVIATGRRHERLQALKDELGENVLTAQLDVRNRAAIEEMMASLPAQWRDIDVLVNNAGLALGLEPAHKASVEDWETMIDTNNKGLIYMTRAVLPGMVERNRGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLVGGTEFSSVRFKGDDEKAGKTYENTTALTPEDITEAVWWVATLPAHVNINTVEMMPVTQSFAGLSVHRS

Gene
ydfG
Protein
NADP-dependent 3-hydroxy acid dehydrogenase YdfG
Organism
Shigella flexneri
Length
248 amino acids
Function
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.
Similarity
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Mass
27.236 kDa
Sequence
MIVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELTDELGDNLYIAQLDVRNRAAIEEMLASLPAEWSNIDILVNNAGLALGMEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNLRTDLHGTTVRVTDIEPGLVGGTEFSNVRFKGDDGKAEKTYQNTVALTPEDVSEAVWWVSTLPAHVNINTLEMMPVTQSYAGLNVHRQ

Gene
ydfG
Protein
Uncharacterized protein YdfG
Organism
Bacillus subtilis (strain 168)
Length
147 amino acids
Mass
17.315 kDa
Sequence
MSQRVSYYEIAPEGMKIMMDMEKYTKQSSINRTTRELIKIRVSQMNGCAFCIDMHTSDARKMGETEQRIYCLHAWNECDFYSPEEKAALELSEHITLIPSKRVPDELYHRVREHYDEEQYVDLVLIINQINSWNRISIAMGNRAASK