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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
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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experimentally determined
co-expression
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[Homology]
Score
LP43_1875Hypothetical protein. (177 aa)    
Predicted Functional Partners:
LP43_1870
Cytochrome c oxidase polypeptide 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).
 
 0.982
ctaA
Heme A synthase, cytochrome oxidase biogenesis protein Cox15-CtaA.
 
 0.974
LP43_1874
Cytochrome oxidase biogenesis protein Surf1.
 
 
 0.970
ctaG
Cytochrome oxidase biogenesis protein Cox11-CtaG.
 
 0.948
ctaB
Heme O synthase, protoheme IX farnesyltransferase COX10-CtaB; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
 
  
 0.887
LP43_1873
Cytochrome c oxidase polypeptide III.
 
  
 0.850
LP43_1871
Cytochrome c oxidase polypeptide 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.
 
 
 0.840
mauD
Methylamine utilization protein MauD.
   
 
 0.619
LP43_1878
Hypothetical protein.
 
    0.579
nuoB
NADH-ubiquinone oxidoreductase chain B; 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.
    
   0.452
Your Current Organism:
Methylophaga thiooxydans
NCBI taxonomy Id: 392484
Other names: DSM 22068, M. thiooxydans, Methylophaga thiooxidans, Methylophaga thiooxydans corrig. Boden et al. 2011, VKM B-2586, strain DMS010
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