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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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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
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Score
AEB86884.1PFAM: Nitrilase/cyanide hydratase and apolipoprotein N-acyltransferase; KEGG: dia:Dtpsy_3367 nitrilase/cyanide hydratase and apolipoprotein N-acyltransferase. (271 aa)    
Predicted Functional Partners:
AEB86885.1
TIGRFAM: Conserved hypothetical protein CHP02099; KEGG: dia:Dtpsy_3368 hypothetical protein.
 
     0.867
AEB86883.1
TIGRFAM: PAS; PFAM: ATPase-like, ATP-binding domain; PAS fold; Signal transduction histidine kinase, subgroup 1, dimerisation/phosphoacceptor domain; KEGG: dia:Dtpsy_3366 PAS/PAC sensor signal transduction histidine kinase; SMART: ATPase-like, ATP-binding domain; PAS; PAC motif; Signal transduction histidine kinase, subgroup 1, dimerisation/phosphoacceptor domain.
     
 0.799
AEB86882.1
Two component transcriptional regulator, LuxR family; KEGG: ajs:Ajs_4015 response regulator receiver protein; PFAM: Transcription regulator LuxR, C-terminal; Signal transduction response regulator, receiver domain; SMART: Signal transduction response regulator, receiver domain; Transcription regulator LuxR, C-terminal.
       0.715
glnE
(Glutamate--ammonia-ligase) adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal tra [...]
  
  
 0.682
AEB83225.1
KEGG: ajs:Ajs_0741 glutamate synthase (NADH) large subunit; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal.
 
   
 0.566
AEB85771.1
KEGG: dia:Dtpsy_2249 aminopeptidase N; TIGRFAM: Peptidase M1, alanyl aminopeptidase; PFAM: Peptidase M1, membrane alanine aminopeptidase, N-terminal.
   
 0.482
AEB86804.1
Xaa-Pro aminopeptidase; KEGG: dia:Dtpsy_3306 peptidase M24B X-Pro dipeptidase/aminopeptidase domain protein; PFAM: Peptidase M24, structural domain; Peptidase M24B, X-Pro dipeptidase/aminopeptidase P N-terminal.
 
 
 0.477
AEB82491.1
Protein of unknown function UPF0153; PFAM: Uncharacterised protein family UPF0153; KEGG: dia:Dtpsy_0043 protein of unknown function UPF0153.
   
 
 0.472
guaA
GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP.
     
 0.459
AEB84354.1
Chorismate mutase; TIGRFAM: Gamma/beta/epsilon proteobacterial P-protein, chorismate mutase domain; PFAM: Prephenate dehydratase; Chorismate mutase, type II; Amino acid-binding ACT; KEGG: dia:Dtpsy_1394 chorismate mutase; SMART: Chorismate mutase.
  
  
 0.422
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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