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ADO48432.1TIGRFAM: lactoylglutathione lyase; KEGG: gloA; lactoylglutathione lyase; PFAM: Glyoxalase/bleomycin resistance protein/dioxygenase. (135 aa)    
Predicted Functional Partners:
gloB
Hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid.
 
 0.985
ADO49106.1
KEGG: enc:ECL_02726 beta-lactamase-like protein.
  
 0.947
ghrB
D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein; Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily.
   
 0.910
ADO48486.1
PFAM: Aldehyde Dehydrogenase; KEGG: kpu:KP1_2509 aldehyde dehydrogenase A; Belongs to the aldehyde dehydrogenase family.
  
 0.904
ghrA
D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein; Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively.
    
 0.901
ADO48675.1
KEGG: kva:Kvar_2900 primary-amine oxidase; PFAM: Copper amine oxidase domain-containing protein; Copper amine oxidase N3-terminal; copper amine oxidase-like domain-containing protein; Copper amine oxidase N2-terminal.
  
  
  0.823
trpB
Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
   
  0.813
ADO46858.1
Pyridoxal-5'-phosphate-dependent protein beta subunit; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
   
 
  0.807
ilvA
Threonine dehydratase, biosynthetic; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
   
 
  0.807
dsdA
TIGRFAM: D-serine ammonia-lyase; KEGG: enc:ECL_00023 D-serine deaminase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit.
     
  0.800
Your Current Organism:
Enterobacter lignolyticus
NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1
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