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
AARI_18610MOSC domain-containing protein; Match to PF03473. The MOSC (MOCO sulfurase C-terminal) domain is a superfamily of beta-strand-rich domains identified in the molybdenum cofactor sulfurase and several other proteins from both prokaryotes and eukaryotes. The MOSC domain is predicted to be a sulfur-carrier domain that receives sulfur abstracted by the pyridoxal phosphate-dependent NifS-like enzymes, on its conserved cysteine, and delivers it for the formation of diverse sulfur-metal clusters. (579 aa)    
Predicted Functional Partners:
AARI_09490
Putative cytochrome P450.
  
 0.969
sufU
SUF system FeS assembly protein; Identified by match to protein family TIGR01994. The SUF system is an iron-sulfur cluster assembly system that operates under iron starvation and oxidative stress. SufU may act as a scaffold on which the Fe-S cluster is built and from which it is transferred.
  
 0.925
soxA
Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine and forms equimolar amounts of formaldehyde, glycine and hydrogen peroxide.
 
 
 0.898
sir
Sulfite reductase (ferredoxin); Catalyzes the reduction of sulfite to sulphide. Involved in the sulfate assimilation pathway; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
  
 
 0.893
AARI_18350
Sulfite reductase catalyzes the reduction of sulfite to sulphide. Involved in the sulfate assimilation pathway.
   
 0.887
gltD
Glutamate synthase (NADPH) subunit beta; Glutamate synthase participates in the ammonia assimilation process by catalyzing the formation of glutamate from glutamine and 2-oxoglutarate.
   
 0.887
pyrDII
Putative dihydroorotate oxidase electron transfer subunit; Dihydroorotate oxidase catalyzes the fourth step in the de novo biosynthesis of pyrimidine, the conversion of dihydroorotate into orotate. In some organisms such as Bacillus subtilis, dihydroorotate oxidase is composed of two subunits: PyrDI and PyrDII.
  
 
 0.880
AARI_13480
Putative cysteine desulfurase; Identified by match to protein family PIRSF005572: cysteine desulfurase, NifS type. Cysteine desulfurase catalyses the following reaction: L-cysteine + [enzyme]-cysteine <=> L-alanine + [enzyme]-S-sulfanylcysteine. It is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin) and functions by mobilizing sulfur.
  
 0.863
AARI_21150
Putative cysteine desulfurase; Identified by match to protein family PIRSF005572: cysteine desulfurase, NifS type. Cysteine desulfurase catalyses the following reaction: L-cysteine + [enzyme]-cysteine <=> L-alanine + [enzyme]-S-sulfanylcysteine. It is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin) and functions by mobilizing sulfur.
  
 0.863
paaN
Phenylacetic acid degradation protein PaaN; Involved in aromatic ring opening step of the phenylacetic acid catabolic pathway.
 
 
 0.767
Your Current Organism:
Glutamicibacter arilaitensis
NCBI taxonomy Id: 861360
Other names: Arthrobacter arilaitensis CIP 108037, Arthrobacter arilaitensis Re117, G. arilaitensis Re117, Glutamicibacter arilaitensis Re117
Server load: low (18%) [HD]