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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from curated databases
textmining
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
mltGAminodeoxychorismate lyase; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. (347 aa)    
Predicted Functional Partners:
tmk
Thymidylate kinase; Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis; Belongs to the thymidylate kinase family.
 
  
 0.984
AMQ94553.1
DNAse; Derived by automated computational analysis using gene prediction method: Protein Homology.
      0.971
AMQ94552.1
DNA polymerase III subunit delta; Catalyzes the DNA-template-directed extension of the 3'-end of a DNA strand; the delta' subunit seems to interact with the gamma subunit to transfer the beta subunit on the DNA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.922
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis.
      0.886
mrcB
Penicillin-binding protein 1B; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits).
  
   
 0.745
fabD
Malonyl CoA-ACP transacylase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.730
topA
DNA topoisomerase I subunit omega; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus rem [...]
  
  
 0.682
AMQ94554.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.668
fabH
3-oxoacyl-ACP synthase; 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 thiolase-like superfamily. FabH family.
      0.650
minC
Septum site-determining protein MinC; Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization; Belongs to the MinC family.
  
  
 0.553
Your Current Organism:
Aggregatibacter actinomycetemcomitans
NCBI taxonomy Id: 714
Other names: A. actinomycetemcomitans, ATCC 33384, Actinobacillus (Haemophilus) actinomycetemcomitans, Actinobacillus actinomycetemcomitans, Bacterium acetinomycetum comitans, Bacterium actinomycetem comitans, Bacterium comitans, CCUG 13227, CIP 52.106, DSM 8324, Haemophilus actinomycetemcomitans, Haemophilus actinomyceticomitans, NCTC 9710
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