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.
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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
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.
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experimentally determined
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gene neighborhood
gene co-occurrence
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thrCThreonine synthase (thrC); Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (425 aa)    
Predicted Functional Partners:
thrB
Homoserine kinase (thrB); Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily.
 
 0.999
thrA
Aspartokinase I / homoserine dehydrogenase I (thrA); Similar to SP:P00561 GB:M10644 GB:V00360 GB:V00361 PID:147979 percent identity: 62.21; identified by sequence similarity; putative; In the C-terminal section; belongs to the homoserine dehydrogenase family.
 
 0.999
ilvA
Threonine deaminase (ilvA); 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 (By similarity).
  
 
 0.984
serC
Phosphoserine aminotransferase (serC); 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.
   
 0.947
leuD
3-isopropylmalate dehydratase small subunit (leuD); Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
 
  
 0.751
HI_1632
Predicted coding region HI1632; Hypothetical protein; identified by GeneMark; putative; Belongs to the aspartokinase family.
 
 
 0.738
asd
Aspartate-semialdehyde dehydrogenase (asd); Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family.
  
 
 0.697
ilvC
Ketol-acid reductoisomerase (ilvC); 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.
 
  
 0.685
pheA
Chorismate mutase / prephenate dehydratase (pheA); Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
 
  
 0.649
hisI
phosphoribosyl-AMP cyclohydrolase / phosphoribosyl-ATP pyrophosphohydrolase (hisIE); Similar to SP:P06989 GB:D43637 GB:U02072 GB:X03974 PID:41700 percent identity: 61.22; identified by sequence similarity; putative; In the C-terminal section; belongs to the PRA-PH family.
  
  
 0.612
Your Current Organism:
Haemophilus influenzae
NCBI taxonomy Id: 71421
Other names: H. influenzae Rd KW20, Haemophilus influenzae KW20, Haemophilus influenzae Rd, Haemophilus influenzae Rd KW20
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