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
Xcel_2768PFAM: FAD dependent oxidoreductase; Rieske [2Fe-2S] domain protein; KEGG: mxa:MXAN_1554 iron-sulfur cluster-binding protein, Rieske family. (506 aa)    
Predicted Functional Partners:
Xcel_2011
PFAM: Cytochrome b/b6 domain; KEGG: sus:Acid_6208 cytochrome b/b6 domain- containing protein.
  
 0.985
Xcel_1218
PFAM: peptidase M16 domain protein; KEGG: dal:Dalk_4744 peptidase M16 domain protein; Belongs to the peptidase M16 family.
   
 0.980
nuoI
NADH-quinone oxidoreductase, chain 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.
  
 
 0.966
Xcel_2008
PFAM: cytochrome c oxidase subunit III; KEGG: amc:MADE_03910 cytochrome o ubiquinol oxidase subunit III (ubiquinol oxidase chain C).
  
 
 0.965
Xcel_0475
TIGRFAM: NADH-quinone oxidoreductase, chain G; PFAM: molybdopterin oxidoreductase; ferredoxin; molydopterin dinucleotide-binding region; KEGG: smd:Smed_3617 molybdopterin oxidoreductase.
  
 
 0.964
Xcel_2009
PFAM: cytochrome c class I; KEGG: tbd:Tbd_2545 putative cytochrome c.
  
 
 0.964
Xcel_0473
TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit; KEGG: scl:sce4224 NADH dehydrogenase (ubiquinone).
   
 
 0.953
Xcel_2015
Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
  
 
 0.952
nuoD
NADH dehydrogenase I, D subunit; 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 a menaquinone. 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; Belongs to the complex I 49 kDa subunit family.
   
 
 0.949
nuoC
NADH (or F420H2) dehydrogenase, subunit C; 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 a menaquinone. 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; Belongs to the complex I 30 kDa subunit family.
   
 
 0.948
Your Current Organism:
Xylanimonas cellulosilytica
NCBI taxonomy Id: 446471
Other names: X. cellulosilytica DSM 15894, Xylanimonas cellulosilytica DSM 15894, Xylanimonas cellulosilytica str. DSM 15894, Xylanimonas cellulosilytica strain DSM 15894
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