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
azo2527Cytochrome P450s are involved in the oxidative degradation of various compounds. Particularly well known for their role in the degradation of environmental toxins and mutagens. Similar to SWISSPROT:P77902 (30% identity); TREMBL:Q59910 (32% identity); SWISSPROT:O34374 (28% identity). Pfam (PF00067): Cytochrome P450; Family membership. (387 aa)    
Predicted Functional Partners:
vanB2
Probable vanillate O-demethylase oxidoreductase (Vanillate degradation ferredoxin-like protein). Homology to vanB of P. sp HR199 of 42% (sprot|VANB_PSEUH). The vanillate demethylase (EC:1.14.13.82) consists of two proteins: an oxygenase and an oxygenase reductase (VanA and VanB). This enzyme is involved in the vanillate degradation, a key intermediate in the degradation of lignin. Pfam: Oxidoredutase FAD-binding domain; Oxidoreductase NAD-binding domain; 2Fe-2S iron-sulfur cluster binding domain no signal peptide no TMHs; Family membership.
 0.967
fdxP
Probable ferredoxin. Homology to fdxP of C. crescentus of 51% (sprot|FER2_CAUCR). Ferredons are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. InterPro: Ferredoxin (IPR001041),Adrenodoxin (IPR001055) Pfam: 2Fe-2S iron-sulfur cluster binding domain no signal peptide no TMHs; High confidence in function and specificity.
 
 0.966
vanB1
Probable vanillate O-demethylase oxidoreductase (Vanillate degradation ferredoxin-like protein). Homology to vanB of P. sp HR199 of 40% (sprot|VANB_PSEUH). The vanillate demethylase (EC:1.14.13.82) consists of two proteins: an oxygenase and an oxygenase reductase (VanA and VanB). This enzyme is involved in the vanillate degradation, a key intermediate in the degradation of lignin. InterPro: NADH:cytochrome b5 reductase (CBR)(IPR001834); Ferredoxin (IPR001041); Oxidoreductase FAD and NAD(P) binding domain (IPR001433) Pfam: Oxidoredutase FAD-binding domain; Oxidoreductase NAD-binding dom [...]
 0.962
rplF
50S ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family.
    
  0.922
aas
AAS bifunctional protein [Includes: 2-acylglycerophosphoethanolamine acyltransferase (2-acyl-GPE acyltransferase); Acyl-acyl carrier protein synthetase (Acyl-ACP synthetase)]. PLAYS A ROLE IN LYSOPHOSPHOLIPID ACYLATION. TRANSFERS FATTY ACIDS TO THE 1-POSITION VIA AN ENZYME-BOUND ACYL-ACP INTERMEDIATE IN THE PRESENCE OF ATP AND MG(2+). ITS PHYSIOLOGICAL FUNCTION IS TO REGENERATE PTDETN FROM 2-ACYL-GPE FORMED BY TRANSACYLATION REACTIONS OR DEGRADATION BY PHOSPHOLIPASE A1, TREMBL:Q8FEA6 (52% identity); SWISSPROT:P31119 (52% identity). Pfam (PF00501): AMP-binding enzyme. Pfam (PF01553): Ac [...]
  
 0.912
azo0798
Hypothetical secreted protein. No homology to the data bank. No domains predicted. No TMHs. Signal peptide present.
   
 0.903
fdx2
Fdx2 protein; Ferredoxin 2Fe-2S. Homology to fdx of E. coli of 70% (sprot|FER_ECOLI). Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Although the function of this ferredoxin is unknown it is probable that it has a role as a cellular electron transfer protein. Involved in the in vivo assembly of the Fe-S clusters in a wide variety of iron- sulfur proteins. InterPro: Ferredoxin (IPR001055); Adrenodoxin (IPR001055) Pfam: 2Fe-2S iorn-sulfur cluster binding domain no signal peptide no TMHs; High confidence in function and specificity.
  
 0.887
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
    
 0.886
azo1828
Hypothetical secreted protein. No significant homology over the entire protein length with the data bank. InterPro: Oxidoreductase FAD and NAD(P)-binding domain (IPR001433); Ferredoxin (IPR001041); NADH: cytochrome b5 reductase (IPR001834). Pfam: Oxidoreductase FAD-binding domain; Oxidoreductase NAD-binding domain; 2Fe-2S iron-sulfur cluster binding domain. signal peptide. no TMHs.
 0.838
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.
  
 0.838
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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