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
dfxDesulfoferrodoxin; Catalyzes the reduction of superoxide to hydrogen peroxide, using electrons from NADH and NADH:rubredoxin oxidoreductase (NROR) and rubredoxin (Rd) as electron transport intermediaries between NADH and Dfx. Is a key factor in the superoxide reductase dependent part of a pathway for detoxification of reactive oxygen species (ROS) in C.acetobutylicum, an obligate anaerobic bacterium. (125 aa)    
Predicted Functional Partners:
fprA2
Predicted flavoprotein; Catalyzes the four-electron reduction of molecular oxygen to water. In fact, functions as the terminal component of an NADH oxidase (NADH:O(2) oxidoreductase) when using NADH:rubredoxin oxidoreductase (NROR) and rubredoxin (Rd) as electron transport intermediaries between NADH and FDP. Is thus able to reductively scavenge intracellular dioxygen and is part of an oxidative stress defense system in C.acetobutylicum, an obligate anaerobic bacterium. Can also serve as the terminal component of an NADH:nitric oxide oxidoreductase (NOR) with a catalytic efficiency com [...]
 
  
 0.947
rd
Rubredoxin; Rubredoxin is a small nonheme, iron protein lacking acid- labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. Functions as an intermediate component in the electron transfer chain: NADH->NROR->Rd->FprA1/2 in which Rd serves as the proximal electron donor to the FDPs that exhibit H(2)O-forming NADH oxidase activity. Also functions as the proximal electron donor to the Dfx and revRbr proteins that display superoxide reductase (SOR) and NADH peroxidase activity, respectively. Therefore, is [...]
 
  
 0.937
nroR
NAD(FAD)-dependent dehydrogenase, NirB-family (N-terminal domain); Catalyzes the NADH-dependent reduction of rubredoxin (Rd). NADPH is a very poor electron donor compared to NADH. Functions as an intermediate component in the electron transfer chain: NADH->NROR->Rd->FprA1/2. Also functions as an intermediate component in the electron transfer chains from NADH to revRbr and Dfx. Therefore, is a key electron carrier in an efficient multienzyme complex that can scavenge O(2) and reactive oxygen species (ROS), and thus plays an important role in the oxidative stress defense system in C.ace [...]
  
  
 0.894
fprA1
Flavoprotein; Catalyzes the four-electron reduction of molecular oxygen to water. In fact, functions as the terminal component of an NADH oxidase (NADH:O(2) oxidoreductase) when using NADH:rubredoxin oxidoreductase (NROR) and rubredoxin (Rd) as electron transport intermediaries between NADH and FDP. Is thus able to reductively scavenge intracellular dioxygen and is part of an oxidative stress defense system in C.acetobutylicum, an obligate anaerobic bacterium.
 
  
 0.881
CA_C2452
Flavodoxin.
  
  
 0.863
CA_C0845
Ferritin-like protein Rsg; Iron-storage protein.
 
  
 0.841
perR
Ferric uptake regulator (FUR family), YGAG B.subtilis ortholog; Represses the expression of most of the genes involved in oxidative stress response, such as rbr3A-rbr3B, dfx, rd, nror, fprA1 and fprA2, coding for reverse rubrerythrins, desulfoferrodoxin, rubredoxin, NADH-rubredoxin oxidoreductase (NROR), and oxygen-reducing flavoproteins, respectively. Thus, by controlling primarily oxygen and reactive oxygen species (ROS) scavenging, PerR plays an important role in the oxidative stress defense system in C.acetobutylicum, an obligate anaerobic bacterium. Probably acts as a peroxide sen [...]
     
 0.813
rbr3B
Rubrerythrin; Functions as the terminal component of an NADH peroxidase (NADH:H(2)O(2) oxidoreductase) when using NADH:rubredoxin oxidoreductase (NROR) as the electron transport intermediary from NADH to revRbr 2. Plays an important role in the oxidative stress defense system in C.acetobutylicum, an obligate anaerobic bacterium. Also exhibits NADH oxidase (NADH:O(2) oxidoreductase) activity in vitro, which is 100-fold lesser than that of FprA1/2 using the same electron transfer components. Therefore, its predominant function is most likely as a scavenger of its preferred substrate, H(2)O(2).
  
  
 0.784
rbr3A
Rubrerythrin; Functions as the terminal component of an NADH peroxidase (NADH:H(2)O(2) oxidoreductase) when using NADH:rubredoxin oxidoreductase (NROR) and rubredoxin (Rd) as electron transport intermediaries from NADH to revRbr 1. Plays an important role in the oxidative stress defense system in C.acetobutylicum, an obligate anaerobic bacterium. Also exhibits NADH oxidase (NADH:O(2) oxidoreductase) activity in vitro, which is 100-fold lesser than that of FprA1/2 using the same electron transfer components. Therefore, its predominant function is most likely as a scavenger of its prefer [...]
  
  
 0.784
rubY
Rubrerythrin; Functions as the terminal component of an NADH peroxidase (NADH:H(2)O(2) oxidoreductase) when using NADH:rubredoxin oxidoreductase (NROR) as the electron transport intermediary from NADH to RubY.
 
  
 0.737
Your Current Organism:
Clostridium acetobutylicum
NCBI taxonomy Id: 272562
Other names: C. acetobutylicum ATCC 824, Clostridium acetobutylicum ATCC 824, Clostridium acetobutylicum DSM 792, Clostridium acetobutylicum str. ATCC 824, Clostridium acetobutylicum strain ATCC 824
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