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
prdXPeroxiredoxin; Belongs to the AhpC/TSA family; Contains 1 thioredoxin domain; KEGG: vvu:VV1_0453 peroxiredoxin (alkyl hydroperoxide reductase subunit C). (202 aa)    
Predicted Functional Partners:
ANS84248.1
Glutathione amide-dependent peroxidase; Catalyzes the oxidation of glutathione amide (GASH) to produce glutathione amide disulfide (GASSAG). May play a role in GASH metabolism under anaerobic conditions as a sulfide carrier necessary for cytoplasmic sulfide oxidation; Contains 1 glutaredoxin domain; Contains 1 thioredoxin domain; KEGG: vfi:VF_2300 peroxiredoxin; Peroxidases.
  
 0.973
trxB
Thioredoxin reductase (TR) that exhibits both TR and thioredoxin (Trx) activities. Contains a C-terminal functional Trx domain. Functions as an electron donor for the plastidial 2-Cys peroxiredoxin BAS1 and participates in a NADPH-dependent hydrogen peroxide scavenging system in chloroplasts in the dark; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family; Contains 1 thioredoxin domain; KEGG: vsp:VS_1186 thioredoxin reductase (NADPH).
  
 
 0.949
katE
Catalase; Decomposes hydrogen peroxide into water and oxyge; serves to protect cells from the toxic effects of hydrogen peroxide. Could protect cells in nodules which have a high potential to produce hydrogen peroxide because of the strong reducing conditions required for nitrogen fixation and the action of several proteins. Belongs to the catalase family; KEGG: vha:VIBHAR_05192 catalase.
  
 
 0.859
ANS85932.1
Thioredoxin-like protein; Belongs to the thioredoxin family; Contains 1 thioredoxin domain.
  
 0.838
ANS86000.1
Thiol:disulfide interchange protein DsbE; Involved in disulfide bond formation. Catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme. Possible subunit of a heme lyase (By similarity); Belongs to the thioredoxin family. DsbE subfamily; Contains 1 thioredoxin domain.
  
 0.838
ANS86080.1
Thiol:disulfide interchange protein; Involved in disulfide bond formation. Catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme. Possible subunit of a heme lyase (By similarity); Belongs to the thioredoxin family. DsbE subfamily; Contains 1 thioredoxin domain.
  
 0.838
fur-2
Ferric uptake regulation protein; Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes. Regulates the expression of several outer-membrane proteins including the iron transport operon (By similarity); Belongs to the Fur family.
  
  
 0.731
ANS85632.1
Nutrient stress-induced DNA-binding protein; Involved in protection of chromosomal DNA from damage under nutrient-limited and oxidative stress conditions. Binds heme (By similarity); Belongs to the Dps family.
  
  
 0.688
ANS83984.1
Putative bacterial non-heme ferritin; Iron-storage protein.
  
  
 0.661
ANS87168.1
Anaerobic nitric oxide reductas; 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 cente; electrons enter from the NorW 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 sectio; belongs to the zinc metallo-hydrolase group 3 family; Contains 1 flavodoxin-like domain; Contains 1 rubredoxin-like domain.
  
  
 0.658
Your Current Organism:
Vibrio scophthalmi
NCBI taxonomy Id: 45658
Other names: CAIM 75, CECT 4638, CIP 105211, LMG 19158, LMG:19158, V. scophthalmi, strain A089
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.