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Literature summary extracted from

  • Zamani, M.; diCenzo, G.C.; Milunovic, B.; Finan, T.M.
    A putative 3-hydroxyisobutyryl-CoA hydrolase is required for efficient symbiotic nitrogen fixation in Sinorhizobium meliloti and Sinorhizobium fredii NGR234 (2017), Environ. Microbiol., 19, 218-236 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.2.4 (S)-3-hydroxyisobutyryl-CoA + H2O Sinorhizobium meliloti
-
CoA + (S)-3-hydroxyisobutyrate
-
ir
3.1.2.4 (S)-3-hydroxyisobutyryl-CoA + H2O Sinorhizobium fredii
-
CoA + (S)-3-hydroxyisobutyrate
-
ir
3.1.2.4 (S)-3-hydroxyisobutyryl-CoA + H2O Sinorhizobium fredii NGR234
-
CoA + (S)-3-hydroxyisobutyrate
-
ir
3.1.2.4 (S)-3-hydroxyisobutyryl-CoA + H2O Sinorhizobium meliloti RmP798
-
CoA + (S)-3-hydroxyisobutyrate
-
ir

Organism

EC Number Organism UniProt Comment Textmining
3.1.2.4 Sinorhizobium fredii C3KM96
-
-
3.1.2.4 Sinorhizobium fredii NGR234 C3KM96
-
-
3.1.2.4 Sinorhizobium meliloti
-
-
-
3.1.2.4 Sinorhizobium meliloti RmP798
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.2.4 (S)-3-hydroxyisobutyryl-CoA + H2O
-
Sinorhizobium meliloti CoA + (S)-3-hydroxyisobutyrate
-
ir
3.1.2.4 (S)-3-hydroxyisobutyryl-CoA + H2O
-
Sinorhizobium fredii CoA + (S)-3-hydroxyisobutyrate
-
ir
3.1.2.4 (S)-3-hydroxyisobutyryl-CoA + H2O
-
Sinorhizobium fredii NGR234 CoA + (S)-3-hydroxyisobutyrate
-
ir
3.1.2.4 (S)-3-hydroxyisobutyryl-CoA + H2O
-
Sinorhizobium meliloti RmP798 CoA + (S)-3-hydroxyisobutyrate
-
ir

Synonyms

EC Number Synonyms Comment Organism
3.1.2.4 HIB-CoA hydrolase
-
Sinorhizobium meliloti
3.1.2.4 HIB-CoA hydrolase
-
Sinorhizobium fredii
3.1.2.4 NGR_b20860
-
Sinorhizobium fredii
3.1.2.4 Smb20752
-
Sinorhizobium meliloti
3.1.2.4 VutE
-
Sinorhizobium meliloti

General Information

EC Number General Information Comment Organism
3.1.2.4 malfunction enzyme deletion results in a loss of symbiotic N2-fixation Sinorhizobium meliloti
3.1.2.4 malfunction enzyme deletion results in a loss of symbiotic N2-fixation Sinorhizobium fredii
3.1.2.4 metabolism the enzyme is required for L-valine catabolism and prevents the accumulation of toxic metabolic intermediates, particularly methacrylyl-CoA Sinorhizobium meliloti
3.1.2.4 metabolism the enzyme is required for L-valine catabolism and prevents the accumulation of toxic metabolic intermediates, particularly methacrylyl-CoA Sinorhizobium fredii
3.1.2.4 physiological function the enzyme is required for efficient symbiotic nitrogen fixation Sinorhizobium meliloti
3.1.2.4 physiological function the enzyme is required for efficient symbiotic nitrogen fixation Sinorhizobium fredii