STRING protein interaction network
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 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
protein homology
Your Input:
Gene Fusion
hcpHybrid-cluster [4Fe-2S-2O] subunit of anaerobic terminal reductases; Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. Is also able to reduce hydroxylamine analogs such as methylhydroxylamine and hydroxyquinone. Might have a role as a scavenger of potentially toxic by-products of nitrate metabolism. Belongs to the HCP family. (550 aa)    
Predicted Functional Partners:
HCP oxidoreductase, NADH-dependent; NADH oxidoreductase acting in concert with HCP.
Nitrite reductase, formate-dependent, cytochrome; Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process. Has very low activity toward hydroxylamine. Has even lower activity toward sulfite. Sulfite reductase activity is maximal at neutral pH (By similarity).
Nitrite reductase, large subunit, NAD(P)H-binding; Nitrite reductase (NAD(P)H) subunit; Protein involved in anaerobic respiration; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
Nitrite reductase (NADH) small subunit; Required for activity of the reductase. To B.subtilis NasE.
Anaerobic nitric oxide reductase flavorubredoxin; Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the reductase at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase; In the N-terminal section; belongs to the zinc metallo- hydrolase group 3 family.
Glutamate dehydrogenase, NADP-specific; Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.
Fused nitric oxide dioxygenase/dihydropteridine reductase 2; Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. Various electron acceptors are also reduced by HMP in vitro, including dihydropterine, ferrisiderophores, ferric citrate, cytochrome c, nitrite, S-nitrosoglutathione, and alkylhydroperoxides. However, it is unknown if th [...]
Iron-sulfur cluster repair protein RIC; Di-iron-containing protein involved in the repair of iron- sulfur clusters damaged by oxidative and nitrosative stress conditions.
Putative 4Fe-4S membrane protein.
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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