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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
AGA88347.1FAD/FMN-dependent dehydrogenase; PFAM: FAD binding domain; FAD linked oxidases, C-terminal domain. (472 aa)    
Predicted Functional Partners:
AGA88346.1
2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase; PFAM: Fumarylacetoacetate (FAA) hydrolase family.
     
 0.810
AGA88348.1
Phosphoglycerate dehydrogenase-like oxidoreductase; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain.
 
  
 0.790
plsB
PFAM: Acyltransferase; TIGRFAM: glycerol-3-phosphate O-acyltransferase; Belongs to the GPAT/DAPAT family.
  
 
 0.679
AGA86255.1
Electron transfer flavoprotein, alpha subunit; PFAM: Electron transfer flavoprotein domain; Electron transfer flavoprotein FAD-binding domain.
 
 
 0.666
AGA86254.1
Electron transfer flavoprotein, beta subunit; PFAM: Electron transfer flavoprotein domain.
 
 
 0.616
AGA88345.1
Hypothetical protein; PFAM: SdiA-regulated.
       0.577
AGA88795.1
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).
   
 
 0.575
mtnD
Hypothetical protein, contains double-stranded beta-helix domain; Catalyzes 2 different reactions between oxygene and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4- methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
  
   
 0.550
fni
Isopentenyl-diphosphate delta-isomerase; Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
  
 0.497
AGA88314.1
Fe-S oxidoreductase; PFAM: Cysteine-rich domain.
  
  
 0.497
Your Current Organism:
Pseudomonas stutzeri
NCBI taxonomy Id: 644801
Other names: P. stutzeri RCH2, Pseudomonas stutzeri RCH2, Pseudomonas stutzeri str. RCH2, Pseudomonas stutzeri strain RCH2
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.