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
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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
azo2349Conserved hypothetical membrane protein. Homology to PA0435 of Pseudomonas aeruginosa of 35% (trembl|Q9I682(SRS)). No domains predicted. Signal peptide. 3 TMHs; Conserved hypothetical protein. (520 aa)    
Predicted Functional Partners:
fyuA
Putative TonB-dependent receptor; Yersinia enterocolitica,iron-repressible outer membrane protein, FyuA. FyuA:RECEPTOR FOR THE BACTERIOCIN PESTICIN AND FOR THE SIDEROPHORE YERSINIABACTIN. TonB-dependent outer membrane receptor; Function unclear.
 
   
 0.718
azo2346
Conserved hypothetical secreted protein. Homology to RB6288 of Rhodopirellula baltica of 30% (trembl|Q7UQJ4(SRS)). No domains predicted. No TMHs. Signal P reporting signal peptide; Conserved hypothetical protein.
  
    0.699
azo1214
Conserved hypothetical membrane protein. Homology to Rgel02003151 of Rubrivivax gelatinosus of 37% (gi|47572524|ref|ZP_00242567.1|(NBCI ENTREZ)). PF06496,Protein of unknown function (DUF1097);IPR009476;This family consists of several bacterial putative membrane proteins. signal peptide. 4 TMHs; Conserved hypothetical protein.
  
     0.664
azo2345
Conserved hypothetical secreted protein. Homology to RB5328 of Rhodopirellula baltica of 47% (trembl|Q7US09(SRS)). Signal Peptide present. No TMH reported Present. Has PF07394, Protein of unknown function (DUF1501);IPR010869;This family contains a number of hypothetical bacterial proteins of unknown function approximately 400 residues long; Conserved hypothetical protein.
  
     0.620
lapP
Phenol hydroxylase P5 protein (EC 1.14.13.7) (Phenol 2-monooxygenase P5 component). Probable electron transfer from NADPH via FAD and the 2Fe-2S center to the oxygenase activity site of the enzyme; High confidence in function and specificity.
     
  0.520
poxF
Probable phenol hydroxylase (EC 1.14.13.7) (Phenol 2-monooxygenase P5 component). Probable electron transfer from NADPH via FAD and the 2Fe-2S center to the oxygenase activity site of the enzyme. InterPro: Oxidoreductase FAD and NAD(P)-binding domain hisT_truA: tRNA pseudouridine synthase A; Specificity unclear.
     
  0.520
nagAa
Naphthalene 12-dioxygenase system ferredoxin--NAD(+) reductase component COMPONENT OF NAPHTHALENE DIOXYGENASE (NDO) MULTICOMPONENT ENZYME SYSTEM WHICH CATALYZES THE INCORPORATION OF BOTH ATOMS OF MOLECULAR OXYGEN INTO NAPHTHALENE TO FORM CIS- NAPHTHALENE DIHYDRODIOL. TRANSFERS ELECTRONS FROM FERREDOXIN (NDOA) TO NADH; High confidence in function and specificity.
     
  0.520
ascD
Probable CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase. Homology to ascD of Y. pestis of 41% (sprot|ASCD_YERPE). PARTICIPATES IN THE CONVERSION OF CDP-6-DEOXY-D-GLYCERO- L-THREO-4-HEXULOSE TO 36-DIDEOXY-D-GLYCERO-D-GLYCERO-4-HEXULOSE TOGETHER WITH CDP-6-DEOXY-D-GLYCERO-L-THREO-4-HEXULOSE-3-DEHYDRASE (E1) IN TWO CONSECUTIVE STEPS. THE DETAILED MECHANISM OF E3 IS NOT YET RESOLVED. InterPro: Oxidoreductase FAD and NAD(P)-binding domain (IPR001433); NadH:cytochrome b5 reductase (CBR) (IPR000134); 2Fe-2S Ferredoxin (IPR006057); Phenol hydroylase reductase family (IPR001221) [...]
     
  0.520
azo2279
Conserved hypothetical protein. Homology to Avin02000067 of Azotobacter vinelandii of 50% (gi|23105742|ref|ZP_00092196.1|(NBCI ENTREZ)). InterPro: Ankyrin-repeat. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids.The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [...]
    
  0.515
azo3763
Hypothetical protein predicted by Glimmer/Critica; Hypothetical protein. no homology to the data bank no domains no signal peptide no TMHs.
  
     0.513
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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