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thrC thrC hom hom ilvA ilvA BPSL2102 BPSL2102 ilvA-2 ilvA-2 serC-2 serC-2 serC serC thrB thrB BPSL1714 BPSL1714 ltaE ltaE leuD leuD
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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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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[Homology]
Score
thrCThreonine synthase; Similar to Corynebacterium glutamicum threonine synthase ThrC or cgl2220 SWALL:THRC_CORGL (SWALL:P23669) (481 aa) fasta scores: E(): 8.6e-100, 57.97% id in 483 aa, and to Ralstonia solanacearum probable threonine synthase protein rsc1328 or rs02850 SWALL:Q8XZR7 (EMBL:AL646064) (481 aa) fasta scores: E(): 5.1e-144, 76.55% id in 482 aa. (483 aa)    
Predicted Functional Partners:
hom
Similar to Pseudomonas aeruginosa homoserine dehydrogenase Hom or pa3736 SWALL:DHOM_PSEAE (SWALL:P29365) (434 aa) fasta scores: E(): 1e-98, 63.12% id in 442 aa, and to Ralstonia solanacearum probable homoserine dehydrogenase oxidoreductase protein rsc1327 or rs02849 SWALL:Q8XZR8 (EMBL:AL646064) (439 aa) fasta scores: E(): 8.2e-121, 78.73% id in 442 aa.
 
 
 0.991
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.
  
 
 0.946
BPSL2102
Putative threonine dehydratase; Similar to Escherichia coli, and Escherichia coli O157:H7 threonine dehydratase catabolic TdcB or b3117 or z4469 or ecs3997 SWALL:THD2_ECOLI (SWALL:P05792) (329 aa) fasta scores: E(): 1.8e-29, 36.9% id in 317 aa, and to Streptomyces coelicolor putative threonine dehydratase sco0821 or scf43a.11C SWALL:Q9XAA4 (EMBL:AL096837) (325 aa) fasta scores: E(): 8.4e-34, 37.81% id in 320 aa.
  
 
 0.946
ilvA-2
Putative 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.
  
 
 0.946
serC-2
Putative phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
   
 0.937
serC
Phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
   
 0.937
thrB
Homoserine kinase; Similar to Methylobacillus flagellatum homoserine kinase ThrB SWALL:KHSE_METFL (SWALL:Q9RAM6) (319 aa) fasta scores: E(): 2e-31, 44.2% id in 319 aa, and to Pseudomonas aeruginosa homoserine kinase pa5495 SWALL:KHSE_PSEAE (SWALL:P29364) (316 aa) fasta scores: E(): 6.4e-25, 43.08% id in 318 aa; Belongs to the pseudomonas-type ThrB family.
 
  
 0.935
BPSL1714
Similar to Aeromonas jandaei L-allo-threonine aldolase LtaA SWALL:LTAA_AERJA (SWALL:O07051) (338 aa) fasta scores: E(): 4.2e-54, 50.59% id in 334 aa, and to Escherichia coli low-specificity L-threonine aldolase LtaE or b0870 SWALL:LTAE_ECOLI (SWALL:P75823) (333 aa) fasta scores: E(): 6.7e-41, 40.58% id in 340 aa. Note: this CDS is longer in its N-terminal region than most of its database matches.
  
 0.923
ltaE
L-allo-threonine aldolase; Similar to Escherichia coli low-specificity L-threonine aldolase LtaE or b0870 SWALL:LTAE_ECOLI (SWALL:P75823) (333 aa) fasta scores: E(): 1.4e-68, 58.98% id in 334 aa, and to Salmonella typhimurium LT2 L-allo-threonine aldolase LtaA SWALL:Q8ZQF1 (EMBL:AE008737) (333 aa) fasta scores: E(): 1.3e-70, 61.07% id in 334 aa.
  
 0.923
leuD
3-isopropylmalate dehydratase small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
 
  
 0.915
Your Current Organism:
Burkholderia pseudomallei
NCBI taxonomy Id: 272560
Other names: B. pseudomallei K96243, Burkholderia pseudomallei K96243, Burkholderia pseudomallei str. K96243, Burkholderia pseudomallei strain K96243
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