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panB protein (Bacillus cereus) - STRING interaction network
"panB" - 3-methyl-2-oxobutanoate hydroxymethyltransferase in Bacillus cereus
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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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panB3-methyl-2-oxobutanoate hydroxymethyltransferase; Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate; Belongs to the PanB family (278 aa)    
Predicted Functional Partners:
panC
Pantothenate synthetase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate; Belongs to the pantothenate synthetase family (282 aa)
 
  0.999
panD
Aspartate 1-decarboxylase; Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine (127 aa)
 
   
  0.994
panE_1
2-dehydropantoate 2-reductase; Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid (296 aa)
   
  0.985
ilvE_2
Branched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family (298 aa)
       
  0.912
ilvE_1
Branched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family (299 aa)
       
  0.912
folK
folK- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase (171 aa)
   
  0.867
guaA
guaA_Nterm- GMP synthase (glutamine-hydrolyzing), N-terminal domain (515 aa)
 
     
  0.814
dinG
ATP-dependent helicase DinG homolog; Probable helicase involved in DNA repair and perhaps also replication (934 aa)
         
  0.765
birA
Bifunctional ligase/repressor BirA; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor (326 aa)
         
  0.724
ilvA_1
L-threonine dehydratase; 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 (420 aa)
     
   
  0.667
Your Current Organism:
Bacillus cereus
NCBI taxonomy Id: 1396
Other names: ATCC 14579, B. cereus, BCRC 10603, Bacillus cereus, Bacillus endorhythmos, Bacillus medusa, Bacillus sp. 2479, Bacillus sp. BS2(2013b), Bacillus sp. BV4, Bacillus sp. JKR50, Bacillus sp. JKR62, Bacillus sp. JP44SK22, Bacillus sp. JP44SK37, Bacillus sp. JP44SK43, Bacillus sp. JP44SK45, Bacillus sp. JSG1(2014), Bacillus sp. KER 17, Bacillus sp. MZ-01, Bacillus sp. PXDK-1, Bacillus sp. Pf-1, Bacillus sp. V3, Bacillus sp. mmm86, CCM 2010, CCRC 10603, CCUG 7414, CIP 66.24, DSM 31, IAM 12605, IFO 15305, JCM 2152, LMG 6923, NBRC 15305, NCCB 75008, NCIMB 9373, NCTC 2599, NRRL B-3711, VKM B-504
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