close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
CKO_00864Hypothetical protein; KEGG: ecp:ECP_1975 1.9e-199 putative acyl-CoA dehydrogenase K00257; COG: COG1960 Acyl-CoA dehydrogenases; Psort location: Cytoplasmic, score:8.96. (376 aa)    
Predicted Functional Partners:
CKO_03340
Hypothetical protein; KEGG: fnu:FN1424 3.4e-26 acyl-CoA dehydrogenase, short-chain specific K00248; COG: COG2025 Electron transfer flavoprotein, alpha subunit.
 
 0.994
fadB
Hypothetical protein; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
 0.982
fadJ
Hypothetical protein; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
 0.965
nuoC
Hypothetical protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 30 kDa subunit family.
   
 0.957
CKO_04125
Hypothetical protein; KEGG: fnu:FN1424 5.0e-08 acyl-CoA dehydrogenase, short-chain specific K00248; COG: COG2025 Electron transfer flavoprotein, alpha subunit; Psort location: Cytoplasmic, score:8.96.
 
 
 0.947
fixA
Hypothetical protein; Required for anaerobic carnitine reduction. May bring reductant to CaiA.
 
 
 0.937
CKO_00862
Hypothetical protein; KEGG: ecc:c2467 1.0e-152 bhbD; putative 3-hydroxyacyl-CoA dehydrogenase K00074; COG: COG1250 3-hydroxyacyl-CoA dehydrogenase.
 
 0.930
caiD
Hypothetical protein; Catalyzes the reversible dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA.
 
 0.926
fadA
Hypothetical protein; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed.
 
 
 0.829
CKO_04222
Hypothetical protein; KEGG: eci:UTI89_C3247 5.2e-190 yqeF; probable acetyl-CoA acetyltransferase K00626; COG: COG0183 Acetyl-CoA acetyltransferase; Psort location: Cytoplasmic, score:9.97; Belongs to the thiolase-like superfamily. Thiolase family.
 
 
 0.814
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
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.