STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
BPSS1879Similar to Bacillus subtilis acetolactate synthase AlsS SWALL:ILVX_BACSU (SWALL:Q04789) (571 aa) fasta scores: E(): 2.8e-57, 32.78% id in 543 aa, and to Pseudomonas aeruginosa probable acetolactate synthase large subunit pa4180 SWALL:Q9HWK1 (EMBL:AE004834) (547 aa) fasta scores: E(): 3.5e-155, 69.57% id in 539 aa; Belongs to the TPP enzyme family. (546 aa)    
Predicted Functional Partners:
BPSS0305
Similar to Bacillus subtilis ketol-acid reductoisomerase IlvC SWALL:ILVC_BACSU (SWALL:P37253) (342 aa) fasta scores: E(): 7e-27, 36.91% id in 298 aa, and to Neisseria meningitidis ketol-acid reductoisomerase nma1763 SWALL:ILVC_NEIMA (SWALL:Q9JTI3) (337 aa) fasta scores: E(): 9.9e-31, 35.71% id in 322 aa.
 
 
 0.975
ilvC
Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
 
 
 0.969
leuB
3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.
 
 0.962
BPSS0011
Similar to Escherichia coli probable tartrate dehydrogenase YeaU or b1800 SWALL:TTUC_ECOLI (SWALL:P76251) (361 aa) fasta scores: E(): 2.2e-106, 70.95% id in 358 aa, and to Ralstonia solanacearum probable tartrate dehydrogenase oxidoreductase protein TtuC or rsp1612 or rs02169 SWALL:Q8XPM6 (EMBL:AL646086) (361 aa) fasta scores: E(): 5.3e-113, 75% id in 360 aa.
 
 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.
 
 0.930
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.
  
 0.920
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.
  
 0.920
ilvH
Similar to Escherichia coli acetolactate synthase isozyme III small subunit IlvH or BrnP or b0078 SWALL:ILVH_ECOLI (SWALL:P00894) (163 aa) fasta scores: E(): 4.8e-31, 55.82% id in 163 aa, and to Ralstonia solanacearum probable acetolactate synthase isozyme III rsc2076 or rs03641 SWALL:Q8XXN7 (EMBL:AL646068) (163 aa) fasta scores: E(): 9.5e-49, 88.34% id in 163 aa.
 
 
 0.917
BPSS1639
Similar to Leuconostoc mesenteroides citrate lyase beta chain CitE SWALL:CILB_LEUMC (SWALL:O53078) (302 aa) fasta scores: E(): 3.9e-14, 33.09% id in 284 aa, and to Yersinia pestis similar to CitE ypo1928 or y2383 SWALL:Q9ZC38 (EMBL:AL031866) (280 aa) fasta scores: E(): 1.7e-36, 46.29% id in 270 aa; Belongs to the HpcH/HpaI aldolase family.
     
  0.900
leuA
2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily.
 
 
 0.896
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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