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
CAZ95897.1Conserved protein belonging to the DUF59 family. Members of this family may all be components of ring hydroxylating complexes; Localized in the cytoplasm; Family membership. (109 aa)    
Predicted Functional Partners:
sufS
Cysteine desulfurase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.
  
 0.978
sufC
ATP-dependent transporter SufC; SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. It is part of the SufBCD complex which contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation; Localized in the cytoplasm; High confidence in function and specificity.
  
 0.964
sufB
The protein SufB is part of the SufBCD complex which acts synergistically with SufE to stimulate the cysteine desulfurase activity (SufS). The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation; Localized in the cytoplasm; High confidence in function and specificity.
   
 0.957
sufD
The protein SufD is part of the SufBCD complex which acts synergistically with sufE to stimulate the cysteine desulfurase activity (SufS). The sufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the fhuF protein; Localized in the cytoplasm; High confidence in function and specificity.
   
 0.932
sufE
The protein SufE is a component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. SufE is an homodimeric scaffold protein that accepts sulfur atom from the cysteine desulfurase SufS and donates it to SufA. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules; Localized in the cytoplasm; High confidence in function and specificity.
     0.927
CAZ95898.1
Conserved hypothetical protein; Localized in the cytoplasm.
       0.811
CAZ95899.1
Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 19 and 20; Localized in the periplasmic space; Conserved hypothetical protein.
       0.592
paaE
Phenylacetic acid degradation NADH oxidoreductase; The protein PaaE is involved in the phenylacetic acid aerobic catabolism. It is likely part of a multicomponent oxygenase involved in phenylacetyl-CoA hydroxylation. It is activated by cAMP receptor protein (CRP) and the integration host factor (IHF). Contains a N-terminal FAD-binding domain, a central feredoxin-like NAD-binding domain and a C-terminal 2Fe-2S iron-sulfur cluster binding domain; Localized in the cytoplasm; High confidence in function and specificity.
  
  
 0.560
fadN
3-Hydroxyl-CoA dehydrogenase / Enoyl-CoA hydratase; Modular protein containing a N-terminal 3-Hydroxyl-CoA dehydrogenase domain and a C-terminal Enoyl-CoA hydratase domain. In Bacillus subtilis, this protein was formerly known as YusL, and has been renamed FadN by Matsuoka et al (JBC, 2007). FadN is involved in fatty acid degradation. 3-Hydroxyl-CoA dehydrogenase catalyzes the reduction of 3-hydroxyacyl-CoA to 3-oxoacyl-CoA. It uses NAD as cofactor. Enoyl-CoA hydratase catalyzes the hydratation of 2-trans-enoyl-CoA into 3-hydroxyacyl-CoA. Localized in the cytoplasm; High confidence in [...]
  
  
 0.484
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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