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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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query proteins and first shell of interactors
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second shell of interactors
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a 3D structure is known or predicted
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Msil_2644PFAM: cytochrome bd ubiquinol oxidase subunit I; KEGG: azc:AZC_3759 cytochrome bd-type quinol oxidase subunit 1. (474 aa)    
Predicted Functional Partners:
Msil_2643
TIGRFAM: cytochrome d ubiquinol oxidase, subunit II; PFAM: cytochrome bd ubiquinol oxidase subunit II; KEGG: azc:AZC_3760 cytochrome bd-type quinol oxidase subunit 2.
 0.999
Msil_2189
TIGRFAM: cytochrome d ubiquinol oxidase, subunit II; PFAM: cytochrome bd ubiquinol oxidase subunit II; KEGG: mrd:Mrad2831_4860 cytochrome d ubiquinol oxidase, subunit II.
 0.997
Msil_2188
PFAM: cytochrome bd ubiquinol oxidase subunit I; KEGG: azc:AZC_1354 cytochrome BD2 subunit I.
  
  
 
0.907
Msil_1659
Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family.
   
 
 0.573
nuoH
NADH dehydrogenase (quinone); 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. This subunit may bind ubiquinone.
     
 0.569
nuoN
Proton-translocating NADH-quinone oxidoreductase, chain N; 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; Belongs to the complex I subunit 2 family.
     
 0.569
nuoA
NADH-ubiquinone/plastoquinone oxidoreductase chain 3; 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; Belongs to the complex I subunit 3 family.
     
 0.568
nuoK
NADH-ubiquinone oxidoreductase chain 4L; 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; Belongs to the complex I subunit 4L family.
     
 0.568
Msil_2927
NADH-ubiquinone/plastoquinone oxidoreductase chain 6; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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.
     
 0.567
Msil_2930
KEGG: bid:Bind_2386 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I).
     
 0.564
Your Current Organism:
Methylocella silvestris
NCBI taxonomy Id: 395965
Other names: M. silvestris BL2, Methylocella silvestris BL2, Methylocella silvestris str. BL2, Methylocella silvestris strain BL2, Methylocella sp. BL2
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