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
AEB83343.1PFAM: Cytochrome c, class I; KEGG: azo:azo2669 cytochrome c family protein. (345 aa)    
Predicted Functional Partners:
AEB84507.1
Gluconate 2-dehydrogenase (acceptor); KEGG: aav:Aave_3387 cytochrome c, class I; PFAM: Cytochrome c, class I.
 
 
 0.865
AEB86273.1
Cytochrome c oxidase, subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
   
 
 0.860
AEB83528.1
Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.
  
 
 0.685
AEB84033.1
PFAM: Cytochrome c, class I; KEGG: net:Neut_1584 cytochrome c, class I.
 
 
 
 0.669
AEB84506.1
KEGG: aav:Aave_3388 cytochrome c553-like protein.
 
  
 0.650
AEB83098.1
PFAM: Oxidoreductase, molybdopterin-binding domain; KEGG: ctt:CtCNB1_4018 oxidoreductase, molybdopterin binding protein.
 
 
 
 0.615
msrP
Oxidoreductase molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to [...]
   
 
 0.534
AEB84568.1
PFAM: Cytochrome c, class I; KEGG: dia:Dtpsy_2192 cytochrome c class I.
   
 
 0.531
AEB84712.1
Hydroxylamine reductase; KEGG: dia:Dtpsy_1710 cytochrome d1 heme region; PFAM: Cytochrome c, class I.
   
 
 0.531
AEB84717.1
KEGG: dia:Dtpsy_1716 hypothetical protein.
   
 
 0.531
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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