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
EHD21087.1FeS assembly protein SufB; KEGG: pct:PC1_2449 cysteine desulfurase activator complex subunit SufB; TIGRFAM: SUF system FeS cluster assembly, SufB; PFAM: SUF system FeS cluster assembly, SufBD. (498 aa)    
Predicted Functional Partners:
EHD21088.1
TIGRFAM: ATPase SufC, SUF system FeS cluster assembly; PFAM: ABC transporter-like; KEGG: eca:ECA1861 cysteine desulfurase ATPase; SMART: ATPase, AAA+ type, core.
 0.999
EHD21089.1
FeS assembly protein SufD; KEGG: pct:PC1_2447 cysteine desulfurase activator complex subunit SufD; TIGRFAM: SUF system FeS cluster assembly, SufD; PFAM: SUF system FeS cluster assembly, SufBD.
 
0.998
sufS
Cysteine desulfurase; Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L- selenocysteine. Selenocysteine lyase activity is however unsure in vivo.
 
 0.982
EHD21086.1
FeS assembly scaffold SufA; KEGG: pwa:Pecwa_2752 iron-sulfur cluster assembly scaffold protein; TIGRFAM: SUF system FeS cluster assembly, SufA scaffold; FeS cluster insertion; PFAM: FeS cluster biogenesis; Belongs to the HesB/IscA family.
  
 
 0.981
EHD22866.1
TIGRFAM: cysteine desulfurase, catalytic subunit CsdA; KEGG: pct:PC1_0925 cysteine sulfinate desulfinase; PFAM: Aminotransferase, class V/Cysteine desulfurase.
 
 0.962
sufE
Cysteine desulfuration protein sufE; Participates in cysteine desulfuration mediated by SufS. 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. Functions as a sulfur acceptor for SufS, by mediating the direct transfer of the sulfur atom from the S-sulfanylcysteine of SufS, an intermediate product of cysteine desulfuration process; Belongs to the SufE family.
 
 
 0.914
EHD22214.1
TIGRFAM: Cysteine desulfurase, SufS; KEGG: kva:Kvar_1657 cysteine desulfurase, SufS subfamily; PFAM: Aminotransferase, class V/Cysteine desulfurase; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family.
 
 
 0.878
iscA
Iron-binding protein iscA; Is able to transfer iron-sulfur clusters to apo-ferredoxin. Multiple cycles of [2Fe2S] cluster formation and transfer are observed, suggesting that IscA acts catalytically. Recruits intracellular free iron so as to provide iron for the assembly of transient iron-sulfur cluster in IscU in the presence of IscS, L-cysteine and the thioredoxin reductase system TrxA/TrxB.
  
 
 0.830
EHD22867.1
KEGG: eca:ECA1011 putative Fe-S metabolism associated protein; TIGRFAM: Cysteine desulfurase, sulphur acceptor subunit CsdE; PFAM: Fe-S metabolism associated SufE.
 
 
 0.790
nfuA
Fe/S biogenesis protein nfuA; Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins.
  
 
 0.788
Your Current Organism:
Brenneria sp. EniD312
NCBI taxonomy Id: 598467
Other names: B. sp. EniD312
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.