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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
iscS1nifS protein, class-V aminotransferase (nifS-1); Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. (392 aa)    
Predicted Functional Partners:
iscU1
nifU protein (nifU-1); A scaffold on which IscS assembles Fe-S clusters. Subsequently gives the nascent cluster to other proteins. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters (By similarity). Belongs to the NifU family.
  
 0.999
thiI
Conserved hypothetical protein; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
 
 0.978
AF_0565
nifU protein (nifU-2); Similar to GB:L42023 PID:1003638 PID:1222302 PID:1204625 PID:1573346 percent identity: 55.65; identified by sequence similarity; putative.
  
 0.976
AF_0531
Molybdenum cofactor biosynthesis protein (moeB); Similar to PID:1653525 percent identity: 43.96; identified by sequence similarity; putative.
   
 0.962
AF_0553
Thiamine biosynthesis protein (thiF); Similar to SP:P30138 PID:396331 PID:414234 GB:U00096 PID:1790425 percent identity: 38.75; identified by sequence similarity; putative.
   
 0.962
AF_0188
Conserved hypothetical protein; Similar to GB:L42023 SP:P44841 PID:1005651 PID:1220807 PID:1204969 percent identity: 38.57; identified by sequence similarity; putative; Belongs to the sulfur carrier protein TusA family.
   
 
 0.950
iscS2
nifS protein, class-V aminotransferase (nifS-2); Catalyzes the removal of elemental sulfur from cysteine to produce alanine (Probable). Binds 1 2Fe-2S cluster per subunit in a crystal formed under reducing conditions; this subunit provides 1 ligand while IscU provides the other 3 ligands. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters.
  
  
0.901
AF_0632
nifU protein (nifU-3); Similar to PID:1653754 percent identity: 47.37; identified by sequence similarity; putative.
  
 
 0.864
AF_1203
Molybdopterin oxidoreductase, molybdopterin binding subunit; Similar to SP:P31075 GB:X65042 PID:48526 percent identity: 30.05; identified by sequence similarity; putative.
    
 0.836
AF_0184
Predicted coding region AF_0184; Hypothetical protein; identified by GeneMark; putative.
 
     0.814
Your Current Organism:
Archaeoglobus fulgidus
NCBI taxonomy Id: 224325
Other names: A. fulgidus DSM 4304, Archaeoglobus fulgidus DSM 4304, Archaeoglobus fulgidus VC-16, Archaeoglobus fulgidus str. DSM 4304, Archaeoglobus fulgidus strain DSM 4304
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