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
ctaBProtoheme IX farnesyltransferase; 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. (317 aa)    
Predicted Functional Partners:
ctaG
Cytochrome c oxidase assembly protein CtaG/Cox11; Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I; Belongs to the COX11/CtaG family.
 
 0.997
ctaA
Cytochrome oxidase assembly; Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group; Belongs to the COX15/CtaA family. Type 2 subfamily.
 
 0.995
Mnod_0261
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.
 
 
 0.971
Mnod_0265
PFAM: cytochrome c oxidase subunit III; KEGG: met:M446_2344 cytochrome c oxidase subunit III.
 
  
 0.962
Mnod_2347
TIGRFAM: cytochrome c oxidase, subunit II; PFAM: cytochrome c oxidase subunit II; cytochrome c class I; KEGG: met:M446_2991 cytochrome c oxidase, subunit II.
 
 
 0.960
Mnod_0260
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).
 
  
 0.953
Mnod_2348
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.
 
 
 0.941
Mnod_6885
TIGRFAM: cytochrome c oxidase, subunit I; PFAM: cytochrome c oxidase subunit I; KEGG: met:M446_5816 cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family.
 
 
 0.939
Mnod_2359
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.
 
 
 0.938
Mnod_6886
TIGRFAM: cytochrome c oxidase, subunit II; PFAM: cytochrome c oxidase subunit II; cytochrome c class I; KEGG: met:M446_5817 cytochrome c oxidase, subunit II.
 
  
 0.936
Your Current Organism:
Methylobacterium nodulans
NCBI taxonomy Id: 460265
Other names: M. nodulans ORS 2060, Methylobacterium nodulans ORS 2060, Methylobacterium nodulans str. ORS 2060, Methylobacterium nodulans strain ORS 2060
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