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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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from curated databases
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Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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Tpau_2694Rieske (2Fe-2S) iron-sulfur domain protein; PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: mab:MAB_1967c ubiquinol-cytochrome c reductase iron-sulfur subunit (Rieske iron-sulfur protein). (399 aa)    
Predicted Functional Partners:
Tpau_2692
KEGG: mjl:Mjls_3302 cytochrome c oxidase, subunit III; PFAM: cytochrome c oxidase subunit III.
 
 
 0.999
Tpau_2693
PFAM: cytochrome c class I; KEGG: rop:ROP_08590 menaquinol-cytochrome c reductase cytochrome c subunit.
 
 0.999
Tpau_2695
PFAM: Cytochrome b/b6 domain; KEGG: rer:RER_35980 menaquinol-cytochrome c reductase cytochrome b subunit.
 
 0.999
Tpau_1537
PFAM: cytochrome c oxidase subunit II; KEGG: nfa:nfa17080 putative cytochrome c oxidase subunit II.
 
 0.996
Tpau_1538
Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family.
 
 0.996
Tpau_2942
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.
 
 0.993
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.
   
 0.983
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.
  
 0.983
Tpau_3172
KEGG: rha:RHA1_ro05913 NADH dehydrogenase subunit E; TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit.
   
 0.982
Tpau_1739
PFAM: peptidase M16 domain protein; KEGG: rha:RHA1_ro06734 metalloendopeptidase; Belongs to the peptidase M16 family.
   
 0.978
Your Current Organism:
Tsukamurella paurometabola
NCBI taxonomy Id: 521096
Other names: T. paurometabola DSM 20162, Tsukamurella paurometabola ATCC 8368, Tsukamurella paurometabola DSM 20162, Tsukamurella paurometabola str. DSM 20162, Tsukamurella paurometabola strain DSM 20162
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