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
azo0250Hypothetical flavodoxin reductase. Homology to the N-terminal part of bb4317 of B. bronchisptica of 40% (trembl|Q7WFF6). InterPro: Oxidoreductase FAD and NAD(P)-binding domain ((IPR001433); NADH: cytochrome b5 reductase (CBR) (IPR001834) Pfam: Oxidorectase FAD-binding domain; Oxidoreductase NAD-binding domain no signal peptide no TMHs. (242 aa)    
Predicted Functional Partners:
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.
 
  
 0.768
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.
  
  
  0.756
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) [...]
 
  
 0.710
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.
 
  
 0.660
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.
 
  
 0.660
oxoR
Reductase component OxoR, of the 2-oxo-1,2-dihydroquinoline 8 monooxygenase protein. Enzyme involved in the second step of quinoline degradation by P. putida 86. Involved in bacterial aromatic compounds degradation; High confidence in function and specificity.
  
  
  0.642
mhpB
2,3-dihydroxyphenylpropionate 1,2-dioxygenase; Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6- ketononatrienedioate, respectively; Belongs to the LigB/MhpB extradiol dioxygenase family.
  
  
  0.588
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.
  
  
 
0.567
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 [...]
  
  
 
0.560
azo0251
Conserved hypothetical membrane protein, 38% similarity to trEMBL;Q7WDT1,Putative membrane protein [BB4906] [Bordetella bronchiseptica (Alcaligenes bronchisepticus)]. TMHMM2 predicts 6 TMH's present. No signal peptide present; Family membership.
       0.534
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.