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.
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
AMS40030.1Glyoxalase; Pfam:pfam12681 Glyoxalase-like domain. (134 aa)    
Predicted Functional Partners:
gloB
Hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid.
   
 0.908
AMS41368.1
Putative metal-binding hydrolase; Pfam:pfam00753 Metallo-beta-lactamase superfamily.
   
 0.908
AMS40087.1
Pfam:pfam02826 D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain.
    
 0.901
AMS44390.1
Pfam:pfam02826 D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain.
    
 0.901
AMS42202.1
Glyoxalase; Pfam:pfam00903 Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily.
     
  0.900
AMS42681.1
Lactoylglutathione lyase; Pfam:pfam12681 Glyoxalase-like domain.
     
  0.900
trpB
Tryptophan synthase subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
   
  0.820
AMS41455.1
Serine dehydratase; Pfam:pfam00291 Pyridoxal-phosphate dependent enzyme.
   
 
  0.803
ilvA
Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
   
 
  0.803
AMS43637.1
Pyridoxal-5-phosphate-dependent protein subunit beta; Pfam:pfam00291 Pyridoxal-phosphate dependent enzyme.
   
 
  0.803
Your Current Organism:
Aminobacter aminovorans
NCBI taxonomy Id: 83263
Other names: A. aminovorans, ATCC 23314, ATCC 29600, Aminobacter heintzii, CCUG 2081, CIP 106737, Chelatobacter heintzii, DSM 10368, DSM 7048, JCM 7852, KCTC 2477, LMG 2122, LMG:2122, NCCB 26039, NCIB 9039, NCIB:9039, NCIMB 9039, NCTC 10684, Pseudomonas aminovorans, VKM B-2058
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