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
cobTNicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase; Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). (349 aa)    
Predicted Functional Partners:
SKA68767.1
Adenosylcobinamide kinase; Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
 
 0.996
cobS
Cobalamin-5'-phosphate synthase; Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'- phosphate; Belongs to the CobS family.
 
 
 0.985
SKA68778.1
Alpha-ribazole phosphatase.
 
 
 0.972
cobQ
Adenosylcobyric acid synthase (glutamine-hydrolysing); Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily.
 
  
 0.950
SKA89189.1
Cobyrinic acid a,c-diamide synthase.
  
 0.943
SKA86067.1
Alpha-ribazole phosphatase.
 
 
 0.863
SKA67725.1
Alpha-ribazole phosphatase.
 
 
 0.851
SKA87254.1
precorrin-8X methylmutase.
 
  
 0.835
SKA68784.1
cob(I)yrinic acid a,c-diamide adenosyltransferase; Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids.
 
   
 0.746
cysG
uroporphyrin-III C-methyltransferase / precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase; Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. Belongs to the precorrin methyltransferase family. In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.
 
  
 0.573
Your Current Organism:
Thiothrix eikelboomii
NCBI taxonomy Id: 92487
Other names: ATCC 49788, Eikelboom type 021N, T. eikelboomii, Thiothrix sp. AP3, filamentous bacterium COM-A, filamentous bacterium KR-A, filamentous bacterium T1-4, filamentous bacterium T2-1, strain AP3
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.