Cloned (Comment) | Organism |
---|---|
gene ACIAD3089, expression in and complementation of Salmonella enterica serovar Typhimurium strain LT2 mutant strain DM12920 | Acinetobacter baylyi |
gene PA0814, expression in and complementation of Salmonella enterica serovar Typhimurium strain LT2 mutant strain DM12920 | Pseudomonas aeruginosa |
gene PA5083, expression in and complementation of Salmonella enterica serovar Typhimurium strain LT2 mutant strain DM12920 | Pseudomonas aeruginosa |
gene PFL_1385, expression in and complementation of Salmonella enterica serovar Typhimurium strain LT2 mutant strain DM12920 | Pseudomonas fluorescens |
gene PSPTO_0102, expression in and complementation of Salmonella enterica serovar Typhimurium strain LT2 mutant strain DM12920 | Pseudomonas syringae pv. tomato |
gene PSPTO_3006, expression in and complementation of Salmonella enterica serovar Typhimurium strain LT2 mutant strain DM12920 | Pseudomonas syringae pv. tomato |
gene ridA, overexpression in Escherichia coli strain BL21AI | Salmonella enterica subsp. enterica serovar Typhimurium |
Protein Variants | Comment | Organism |
---|---|---|
additional information | the ridA-deficient mutant of Salmonella enterica strain DM12920 can be complemented by Rid family enzymes from Pseudomonas aeruginosa strain PAO1 (Rid1 and Rid2), Acinetobacter baylyi strain ATCC 33305 (Rid2), Pseudomonas syringae pv. tomato strain ATCC BAA-871 (Rid2 and Rid3), Pseudomonas fluorescens strain ATCC BAA-477 (Rid3), and by ridA from the Salmonella enterica wild-type LT2 | Salmonella enterica subsp. enterica serovar Typhimurium |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-iminopropanoate + H2O | Salmonella enterica subsp. enterica serovar Typhimurium | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Pseudomonas aeruginosa | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Acinetobacter baylyi | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Pseudomonas syringae pv. tomato | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Pseudomonas fluorescens | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Pseudomonas aeruginosa ATCC 15692 | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Pseudomonas fluorescens Pf-5 | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Acinetobacter baylyi BD413 | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Pseudomonas fluorescens ATCC BAA-477 | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Pseudomonas aeruginosa 1C | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Pseudomonas syringae pv. tomato DC3000 | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Pseudomonas syringae pv. tomato ATCC BAA-871 | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Pseudomonas aeruginosa PRS 101 | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Pseudomonas aeruginosa DSM 22644 | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Pseudomonas aeruginosa CIP 104116 | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Pseudomonas aeruginosa LMG 12228 | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Acinetobacter baylyi ATCC 33305 | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Pseudomonas aeruginosa JCM 14847 | - |
pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | Pseudomonas fluorescens NRRL B-23932 | - |
pyruvate + NH3 | - |
? | |
additional information | Salmonella enterica subsp. enterica serovar Typhimurium | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Pseudomonas aeruginosa | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Acinetobacter baylyi | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Pseudomonas syringae pv. tomato | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Pseudomonas fluorescens | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Pseudomonas aeruginosa ATCC 15692 | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Pseudomonas fluorescens Pf-5 | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Acinetobacter baylyi BD413 | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Pseudomonas fluorescens ATCC BAA-477 | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Pseudomonas aeruginosa 1C | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Pseudomonas syringae pv. tomato DC3000 | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Pseudomonas syringae pv. tomato ATCC BAA-871 | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Pseudomonas aeruginosa PRS 101 | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Pseudomonas aeruginosa DSM 22644 | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Pseudomonas aeruginosa CIP 104116 | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Pseudomonas aeruginosa LMG 12228 | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Acinetobacter baylyi ATCC 33305 | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Pseudomonas aeruginosa JCM 14847 | the enzyme reduces semicarbazone formation | ? | - |
- |
|
additional information | Pseudomonas fluorescens NRRL B-23932 | the enzyme reduces semicarbazone formation | ? | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acinetobacter baylyi | Q6F828 | - |
- |
Acinetobacter baylyi ATCC 33305 | Q6F828 | - |
- |
Acinetobacter baylyi BD413 | Q6F828 | - |
- |
Pseudomonas aeruginosa | Q9HUA0 | - |
- |
Pseudomonas aeruginosa | Q9I5C5 | - |
- |
Pseudomonas aeruginosa 1C | Q9HUA0 | - |
- |
Pseudomonas aeruginosa 1C | Q9I5C5 | - |
- |
Pseudomonas aeruginosa ATCC 15692 | Q9HUA0 | - |
- |
Pseudomonas aeruginosa ATCC 15692 | Q9I5C5 | - |
- |
Pseudomonas aeruginosa CIP 104116 | Q9HUA0 | - |
- |
Pseudomonas aeruginosa CIP 104116 | Q9I5C5 | - |
- |
Pseudomonas aeruginosa DSM 22644 | Q9HUA0 | - |
- |
Pseudomonas aeruginosa DSM 22644 | Q9I5C5 | - |
- |
Pseudomonas aeruginosa JCM 14847 | Q9HUA0 | - |
- |
Pseudomonas aeruginosa JCM 14847 | Q9I5C5 | - |
- |
Pseudomonas aeruginosa LMG 12228 | Q9HUA0 | - |
- |
Pseudomonas aeruginosa LMG 12228 | Q9I5C5 | - |
- |
Pseudomonas aeruginosa PRS 101 | Q9HUA0 | - |
- |
Pseudomonas aeruginosa PRS 101 | Q9I5C5 | - |
- |
Pseudomonas fluorescens | Q4KGW9 | - |
- |
Pseudomonas fluorescens ATCC BAA-477 | Q4KGW9 | - |
- |
Pseudomonas fluorescens NRRL B-23932 | Q4KGW9 | - |
- |
Pseudomonas fluorescens Pf-5 | Q4KGW9 | - |
- |
Pseudomonas syringae pv. tomato | Q880Z0 | - |
- |
Pseudomonas syringae pv. tomato | Q88BB5 | - |
- |
Pseudomonas syringae pv. tomato ATCC BAA-871 | Q880Z0 | - |
- |
Pseudomonas syringae pv. tomato ATCC BAA-871 | Q88BB5 | - |
- |
Pseudomonas syringae pv. tomato DC3000 | Q880Z0 | - |
- |
Pseudomonas syringae pv. tomato DC3000 | Q88BB5 | - |
- |
Salmonella enterica subsp. enterica serovar Typhimurium | Q7CP78 | - |
- |
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 | Q7CP78 | - |
- |
Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 | Q7CP78 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-iminopropanoate + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Pseudomonas aeruginosa | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Acinetobacter baylyi | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Pseudomonas syringae pv. tomato | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Pseudomonas fluorescens | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Pseudomonas aeruginosa ATCC 15692 | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Pseudomonas fluorescens Pf-5 | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Acinetobacter baylyi BD413 | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Pseudomonas fluorescens ATCC BAA-477 | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Pseudomonas aeruginosa 1C | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Pseudomonas syringae pv. tomato DC3000 | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Pseudomonas syringae pv. tomato ATCC BAA-871 | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Pseudomonas aeruginosa PRS 101 | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Pseudomonas aeruginosa DSM 22644 | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Pseudomonas aeruginosa CIP 104116 | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Pseudomonas aeruginosa LMG 12228 | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Acinetobacter baylyi ATCC 33305 | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Pseudomonas aeruginosa JCM 14847 | pyruvate + NH3 | - |
? | |
2-iminopropanoate + H2O | - |
Pseudomonas fluorescens NRRL B-23932 | pyruvate + NH3 | - |
? | |
additional information | the enzyme reduces semicarbazone formation | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Pseudomonas aeruginosa | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Acinetobacter baylyi | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Pseudomonas syringae pv. tomato | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Pseudomonas fluorescens | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA | Pseudomonas aeruginosa | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Pseudomonas aeruginosa | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Pseudomonas syringae pv. tomato | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Pseudomonas fluorescens | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-aminoacid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Acinetobacter baylyi | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Pseudomonas aeruginosa ATCC 15692 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Pseudomonas aeruginosa ATCC 15692 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA | Pseudomonas aeruginosa ATCC 15692 | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Pseudomonas fluorescens Pf-5 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Pseudomonas fluorescens Pf-5 | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Acinetobacter baylyi BD413 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-aminoacid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Acinetobacter baylyi BD413 | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA | Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Pseudomonas fluorescens ATCC BAA-477 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Pseudomonas fluorescens ATCC BAA-477 | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Pseudomonas aeruginosa 1C | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Pseudomonas aeruginosa 1C | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA | Pseudomonas aeruginosa 1C | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Pseudomonas syringae pv. tomato DC3000 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Pseudomonas syringae pv. tomato DC3000 | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA | Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Pseudomonas syringae pv. tomato ATCC BAA-871 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Pseudomonas syringae pv. tomato ATCC BAA-871 | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Pseudomonas aeruginosa PRS 101 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Pseudomonas aeruginosa PRS 101 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA | Pseudomonas aeruginosa PRS 101 | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Pseudomonas aeruginosa DSM 22644 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Pseudomonas aeruginosa DSM 22644 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA | Pseudomonas aeruginosa DSM 22644 | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Pseudomonas aeruginosa CIP 104116 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Pseudomonas aeruginosa CIP 104116 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA | Pseudomonas aeruginosa CIP 104116 | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Pseudomonas aeruginosa LMG 12228 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Pseudomonas aeruginosa LMG 12228 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA | Pseudomonas aeruginosa LMG 12228 | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Acinetobacter baylyi ATCC 33305 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-aminoacid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Acinetobacter baylyi ATCC 33305 | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Pseudomonas aeruginosa JCM 14847 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Pseudomonas aeruginosa JCM 14847 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA | Pseudomonas aeruginosa JCM 14847 | ? | - |
- |
|
additional information | the enzyme reduces semicarbazone formation | Pseudomonas fluorescens NRRL B-23932 | ? | - |
- |
|
additional information | enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA | Pseudomonas fluorescens NRRL B-23932 | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
ACIAD3089 | - |
Acinetobacter baylyi |
endoribonuclease L-PSP family protein | UniProt | Pseudomonas syringae pv. tomato |
endoribonuclease L-PSP family protein | UniProt | Pseudomonas fluorescens |
imine deaminase | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
imine deaminase | - |
Pseudomonas aeruginosa |
imine deaminase | - |
Acinetobacter baylyi |
imine deaminase | - |
Pseudomonas syringae pv. tomato |
imine deaminase | - |
Pseudomonas fluorescens |
PA0814 | - |
Pseudomonas aeruginosa |
PA5083 | - |
Pseudomonas aeruginosa |
PFL_1385 | - |
Pseudomonas fluorescens |
PSPTO_0102 | - |
Pseudomonas syringae pv. tomato |
PSPTO_3006 | - |
Pseudomonas syringae pv. tomato |
Rid1 | - |
Pseudomonas aeruginosa |
Rid2 | - |
Pseudomonas aeruginosa |
Rid2 | - |
Acinetobacter baylyi |
Rid2 | - |
Pseudomonas syringae pv. tomato |
Rid3 | - |
Pseudomonas syringae pv. tomato |
Rid3 | - |
Pseudomonas fluorescens |
ridA | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
YjgF_endoribonc domain-containing protein | UniProt | Pseudomonas aeruginosa |
YjgF_endoribonc domain-containing protein | UniProt | Acinetobacter baylyi |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
in vivo assay at | Salmonella enterica subsp. enterica serovar Typhimurium |
37 | - |
in vivo assay at | Pseudomonas aeruginosa |
37 | - |
in vivo assay at | Acinetobacter baylyi |
37 | - |
in vivo assay at | Pseudomonas syringae pv. tomato |
37 | - |
in vivo assay at | Pseudomonas fluorescens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.7 | - |
assay at | Salmonella enterica subsp. enterica serovar Typhimurium |
8.7 | - |
assay at | Pseudomonas aeruginosa |
8.7 | - |
assay at | Acinetobacter baylyi |
8.7 | - |
assay at | Pseudomonas syringae pv. tomato |
8.7 | - |
assay at | Pseudomonas fluorescens |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the Rid family, subfamily Rid1, of enzymes. Proteins from Rid1, 2, 3 subfamilies have different substrate specificities, deamination of iminoarginine separates Rid subfamilies | Salmonella enterica subsp. enterica serovar Typhimurium |
evolution | the enzyme belongs to the Rid family, subfamily Rid1, of enzymes. Proteins from Rid1, 2, 3 subfamilies have different substrate specificities, deamination of iminoarginine separates Rid subfamilies | Pseudomonas aeruginosa |
evolution | the enzyme belongs to the Rid family, subfamily Rid1, of enzymes. Proteins from Rid1, 2, 3 subfamilies have different substrate specificities, deamination of iminoarginine separates Rid subfamilies | Acinetobacter baylyi |
evolution | the enzyme belongs to the Rid family, subfamily Rid1, of enzymes. Proteins from Rid1, 2, 3 subfamilies have different substrate specificities, deamination of iminoarginine separates Rid subfamilies | Pseudomonas syringae pv. tomato |
evolution | the enzyme belongs to the Rid family, subfamily Rid1, of enzymes. Proteins from Rid1, 2, 3 subfamilies have different substrate specificities, deamination of iminoarginine separates Rid subfamilies | Pseudomonas fluorescens |
malfunction | Salmonella enterica strains lacking gene ridA have a growth defect in minimal medium containing 5 mM serine or 0.25 mM cysteine due to the accumulation of 2-aminoacrylate (2AA) | Salmonella enterica subsp. enterica serovar Typhimurium |
physiological function | Acinetobacter baylyi strain ATCC 33305 enzyme Rid2 can complement the Salmonella enterica strain lacking gene ridA, the mutant has a growth defect in minimal medium containing 5 mM serine or 0.25 mM cysteine due to the accumulation of 2-aminoacrylate (2AA) | Acinetobacter baylyi |
physiological function | Pseudomonas aeruginosa strain PAO1 enzyme Rid1 can complement the Salmonella enterica strain lacking gene ridA, the mutant has a growth defect in minimal medium containing 5 mM serine or 0.25 mM cysteine due to the accumulation of 2-aminoacrylate (2AA) | Pseudomonas aeruginosa |
physiological function | Pseudomonas aeruginosa strain PAO1 enzyme Rid2 can complement the Salmonella enterica strain lacking gene ridA, the mutant has a growth defect in minimal medium containing 5 mM serine or 0.25 mM cysteine due to the accumulation of 2-aminoacrylate (2AA) | Pseudomonas aeruginosa |
physiological function | Pseudomonas fluorescens strain ATCC BAA-477 enzyme Rid3 can complement the Salmonella enterica strain lacking gene ridA, the mutant has a growth defect in minimal medium containing 5 mM serine or 0.25 mM cysteine due to the accumulation of 2-aminoacrylate (2AA) | Pseudomonas fluorescens |
physiological function | Pseudomonas syringae pv. tomato enzyme Rid2 can complement the Salmonella enterica strain lacking gene ridA, the mutant has a growth defect in minimal medium containing 5 mM serine or 0.25 mM cysteine due to the accumulation of 2-aminoacrylate (2AA) | Pseudomonas syringae pv. tomato |
physiological function | Pseudomonas syringae pv. tomato enzyme Rid3 can complement the Salmonella enterica strain lacking gene ridA, the mutant has a growth defect in minimal medium containing 5 mM serine or 0.25 mM cysteine due to the accumulation of 2-aminoacrylate (2AA) | Pseudomonas syringae pv. tomato |