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Mfla_2033 protein (Methylobacillus flagellatus) - STRING interaction network
"Mfla_2033" - Pyridoxal-dependent decarboxylase in Methylobacillus flagellatus
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Mfla_2033Pyridoxal-dependent decarboxylase (490 aa)    
Predicted Functional Partners:
Mfla_1912
YjeF-related protein-like protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (487 aa)
   
        0.896
Mfla_2032
2OG-Fe(II) oxygenase (212 aa)
              0.859
Mfla_0486
Amylo-alpha-1,6-glucosidase (711 aa)
   
        0.717
Mfla_2573
Isochorismatase hydrolase (207 aa)
     
        0.674
Mfla_2540
Isochorismatase hydrolase (198 aa)
     
        0.674
Mfla_1417
Malto-oligosyltrehalose trehalohydrolase (629 aa)
     
        0.671
glgB
Glycogen branching enzyme; Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position (725 aa)
     
        0.671
Mfla_0879
Glycogen/starch/alpha-glucan phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (846 aa)
     
        0.669
Mfla_0879
Glycogen/starch/alpha-glucan phosphorylase (846 aa)
     
        0.669
dnaJ
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] (373 aa)
     
 
    0.655
Your Current Organism:
Methylobacillus flagellatus
NCBI taxonomy Id: 265072
Other names: M. flagellatus, M. flagellatus KT, Methylobacillus, Methylobacillus flagellatus, Methylobacillus flagellatus KT, Methylobacillus flagellatus str. KT, Methylobacillus flagellatus strain KT
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