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
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
APR71911.12Fe-2S ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (106 aa)    
Predicted Functional Partners:
APR69932.1
Pyridine nucleotide-disulfide oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.983
APR69891.1
FAD-dependent oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.944
APR69931.1
Cytochrome; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the cytochrome P450 family.
 
 0.925
fdx-2
Ferredoxin, 2Fe-2S type, ISC system; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
  0.919
fdx
Ferredoxin, 2Fe-2S type, ISC system; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
  0.918
nuoC
NADH-quinone oxidoreductase subunit C/D; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
  
 
 0.907
nfuA
Fe/S biogenesis protein NfuA; Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins.
  
 0.768
iscU
Fe-S cluster assembly scaffold IscU; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters.
  
 0.759
hscB
Fe-S protein assembly co-chaperone HscB; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family.
 
  
 0.697
iscX
Fe-S assembly protein IscX; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.694
Your Current Organism:
Acinetobacter haemolyticus
NCBI taxonomy Id: 29430
Other names: A. haemolyticus, ATCC 17906, Achromobacter haemolyticus, Acinetobacter genomosp. 4, Acinetobacter genomospecies 4, Acinetobacter haematolyticus, CCUG 888, CIP 64.3, DSM 6962, LMG 996, LMG:996, NCCB 85026, NCTC 12155, NCTC:12155, strain B40, strain Mannheim 2446/60
Server load: medium (60%) [HD]