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
ALV26070.1Allophanate hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. (291 aa)    
Predicted Functional Partners:
ALV26071.1
Allophanate hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
ALV29687.1
Urea carboxylase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
0.995
ALV26067.1
Lactam utilization protein LamB; Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
 
  
 0.986
ALV30066.1
Allophanate hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
0.939
pxpA
Hypothetical protein; Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
 
  
 0.925
ALV29686.1
Catalyzes the hydrolysis of allophanate; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.923
ALV26068.1
Biotin attachment protein; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
 
    0.913
ureC
Urease subunit alpha; Ureases catalyze the hydrolysis of urea into ammonia and carbon dioxide; in Helicobacter pylori the ammonia released plays a key role in bacterial survival by neutralizing acids when colonizing the gastric mucosa; the holoenzyme is composed of 3 ureC (alpha) and 3 ureAB (gamma/beta) subunits; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.907
ureB
Urease subunit beta; Ureases catalyze the hydrolysis of urea into ammonia and carbon dioxide; in Helicobacter pylori and Yersinia enterocolitica the ammonia released plays a key role in bacterial survival by neutralizing acids when colonizing the gastric mucosa; the holoenzyme is composed of 3 UreC (alpha) and 3 UreAB (gamma/beta); in Brucella suis the urease encoded by this operon (one of two urease-encoding operons found in its genome) is involved with urease activity, optimum growth, resistance to low-pH killing in-vitro and persistence in-vivo, while the other operon does not seem [...]
     
 0.906
ureA
Urease subunit gamma; UreA, with UreB and UreC catalyzes the hydrolysis of urea into ammonia and carbon dioxide; nickel metalloenzyme; accessory proteins UreD, UreE, UreF, and UreG are necessary for assembly of the metallocenter; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the urease gamma subunit family.
     
 0.900
Your Current Organism:
Pannonibacter phragmitetus
NCBI taxonomy Id: 121719
Other names: Achromobacter group B, Achromobacter group E, Achromobacter sp. LMG 5410, Achromobacter sp. LMG 5411, Achromobacter sp. LMG 5430, Achromobacter sp. LMG 5431, DSM 14782, LMG 22736, LMG:22736, NCAIM B02025, NCTC 13350, P. phragmitetus, Pannonibacter phragmitetus Borsodi et al. 2003, alpha proteobacterium C6-19, alpha proteobacterium C6/17, alpha proteobacterium C6/8, strain C6/19
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