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
ccoNProbable cytochrome c oxidase, cbb3-type, subunit I. Homology to ccoN of R. capsulatus of 62% (sprot|COX1_RHOCA). 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 OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoN: cytochrome c oxidase cbb3-type Pfam: cytochrome c and quinol oxidase polyppeptide no signal peptide 12 TMHs; Hig [...] (474 aa)    
Predicted Functional Partners:
ccoO
Probable cytochrome c oxidase, cbb3-type, subunit II Homology to ccoO of P. stutzeri of 58% (trembl|Q8KS21). 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 OR A QUINOL ARE TRANSFERRED TO THE BIMETALLIC CENTER FORMED BY A HIGH-SPIN HEME AND COPPER B. Tigrfam: ccoO: cytochrome c oxidase cbb3-type, subunit II Pfam: Cytochrome c oxidase, mono-heme subunit no signal peptide probable 1 [...]
 0.999
ccoP
Probable cytochrome c oxidase, cbb3-type,subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.
 
 0.999
ccoQ
Cbb3-type cytochrome oxidase, subunit ccoQ, 44% Identity to TrEMBL;Q8D9I3, Q7MKV5,Q9KS21. Has PF05545,Cbb3-type cytochrome oxidase component FixQ; IPR008621;This family consists of several Cbb3-type cytochrome oxidase components (FixQ/CcoQ). FixQ is found in nitrogen fixing bacteria. Since nitrogen fixation is an energy-consuming process, effective symbioses depend on operation of a respiratory chain with a high affinity for O2, closely coupled to ATP production. This requirement is fulfilled by a special three-subunit terminal oxidase (cytochrome terminal oxidase cbb3), which was firs [...]
  
 
 0.998
coxB
Conserved hypothetical 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).
  
 0.989
ccoG
Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to fixG of R. meliloti of 36% (FIXG_RHIME). Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group,originally found in bacteria, has been termed ''bacterial-type'', in which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including fo [...]
 
  
 0.964
coxA
Probable 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.
    
 0.948
petB
Ubiquinol-cytochrome c reductase cytochrome b protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
 
 0.935
coxC
Cytochrome c oxidase polypeptide III Subunits I II and III form the functional core of the enzyme complex. InterPro: Cytochrome c oxidase subunit III; High confidence in function and specificity.
    
 0.935
coxD
Putative protoheme 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.
    
 0.933
rdxA
Putative iron-sulfur 4Fe-4S ferredoxin transmembrane protein. Homology to rdxA of R. sphaeroides of 37% (SWISSPROT:RDXA_RHOSH) Involved in a membrane generated redox signal. Pfam: 4Fe-4S binding domain Probable 5 TMHs no signal peptide; Family membership.
 
  
 0.930
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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