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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Co-expression
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[Homology]
Score
AMS39272.1Hypothetical protein. (99 aa)    
Predicted Functional Partners:
AMS39271.1
Ferredoxin; Pfam:pfam00111 2Fe-2S iron-sulfur cluster binding domain.
  
    0.771
AMS42320.1
Hypothetical protein; Pfam:pfam01592 NifU-like N terminal domain.
  
 0.635
AMS39273.1
Ferredoxin.
  
    0.601
AMS42862.1
Cysteine desulfarase; Pfam:pfam00266 Aminotransferase class-V.
  
 0.592
AMS39268.1
Pfam:pfam02423 Ornithine cyclodeaminase/mu-crystallin family.
  
    0.547
AMS39270.1
Hypothetical protein; Pfam:pfam00171 Aldehyde dehydrogenase family; Belongs to the aldehyde dehydrogenase family.
  
    0.522
AMS39269.1
Hypothetical protein; Pfam:pfam01925 Sulfite exporter TauE/SafE.
       0.515
AMS39274.1
Aldehyde dehydrogenase; Pfam:pfam14518 Iron-containing redox enzyme.
       0.507
nuoI
NADH-quinone oxidoreductase subunit I; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
  
 
 0.472
AMS40948.1
Pfam:pfam14691 Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster.
    
 0.460
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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