STRINGSTRING
aaxC protein (Chlamydia trachomatis) - STRING interaction network
"aaxC" - annotation not available in Chlamydia trachomatis
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
aaxCannotation not available (483 aa)    
Predicted Functional Partners:
aaxB
annotation not available (195 aa)
         
  0.933
aaxA
Porin; Facilitates L-arginine uptake, as part of the AaxABC system. The arginine uptake by the bacterium in the macrophage may be a virulence factor against the host innate immune response (466 aa)
         
  0.787
fabH
3-oxoacyl-[acyl-carrier-protein] synthase 3; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched- chain and/or straight-chain of fatty acids; Belongs to the FabH family (327 aa)
         
  0.671
aroD
3-dehydroquinate dehydratase; Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3- dehydroshikimate; Belongs to the type-I 3-dehydroquinase family (478 aa)
     
      0.640
O172_02050
annotation not available (352 aa)
   
        0.600
aroC
Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system (357 aa)
     
      0.518
dapB
4-hydroxy-tetrahydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy- tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate (253 aa)
         
  0.484
O172_02030
annotation not available (261 aa)
              0.474
aroA_1
annotation not available (440 aa)
              0.456
bioF
annotation not available (377 aa)
         
  0.439
Your Current Organism:
Chlamydia trachomatis
NCBI taxonomy Id: 813
Other names: ATCC VR-571B, C. trachomatis, Chlamydia trachomatis, Chlamydozoon trachomatis, DSM 19440, Rickettsia trachomae, Rickettsia trachomatis, strain A/Har-13
Server load: low (11%) [HD]