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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
tdhHypothetical protein; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. (341 aa)    
Predicted Functional Partners:
kbl
Hypothetical protein; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.
 
 
 0.997
ilvA
Hypothetical protein; 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.
   
 0.907
CKO_04517
Hypothetical protein; 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.
   
 0.907
CKO_02211
Hypothetical protein; KEGG: ecj:JW0854 5.8e-159 ltaE; L-allo-threonine aldolase, PLP-dependent K01620; COG: COG2008 Threonine aldolase.
     
 0.903
CKO_01569
Hypothetical protein; KEGG: eci:UTI89_C1762 2.1e-124 ydfG; probable oxidoreductase YdfG; COG: COG4221 Short-chain alcohol dehydrogenase of unknown specificity; Psort location: Cytoplasmic, score:9.26; Belongs to the short-chain dehydrogenases/reductases (SDR) family.
    
 0.902
CKO_03383
Hypothetical protein; KEGG: sbo:SBO_0003 1.6e-213 thrC; threonine synthase K01733; COG: COG0498 Threonine synthase; Psort location: Cytoplasmic, score:8.96.
     
 0.901
bioF
Hypothetical protein; Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
 
  
 0.675
hldD
Hypothetical protein; Catalyzes the interconversion between ADP-D-glycero-beta-D- manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose; Belongs to the NAD(P)-dependent epimerase/dehydratase family. HldD subfamily.
  
  
 0.568
CKO_05079
Hypothetical protein; KEGG: ecp:ECP_3720 3.3e-181 ADP-heptose-LPS heptosyltransferase II K02843; COG: COG0859 ADP-heptose:LPS heptosyltransferase.
       0.540
CKO_01425
Hypothetical protein; KEGG: ecp:ECP_1403 0. probable pyruvate-flavodoxin oxidoreductase K03737; COG: COG1013 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit.
     
 0.502
Your Current Organism:
Citrobacter koseri
NCBI taxonomy Id: 290338
Other names: C. koseri ATCC BAA-895, Citrobacter (diversus) koseri ATCC BAA-895, Citrobacter koseri ATCC BAA-895, Citrobacter koseri str. ATCC BAA-895, Citrobacter koseri strain ATCC BAA-895
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