close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
Taci_0126cob(I)alamin adenosyltransferase; KEGG: gme:Gmet_1573 cob(I)yrinic acid a,c-diamide adenosyltransferase; TIGRFAM: cob(I)alamin adenosyltransferase; PFAM: ATP:corrinoid adenosyltransferase BtuR/CobO/CobP. (171 aa)    
Predicted Functional Partners:
cobQ
Cobyric acid synthase CobQ; 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.
 
 0.988
Taci_1719
Adenosylcobinamide-phosphateguanylyltransferase; PFAM: cobalbumin biosynthesis protein; KEGG: gur:Gura_4188 adenosylcobinamide-phosphate guanylyltransferase.
 
  
 0.973
cobD
Cobalamin biosynthesis protein CobD; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
 
  
 0.969
cobS
Cobalamin-5-phosphate synthase CobS; 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.
 
 
 0.965
Taci_0552
TIGRFAM: ATP/cobalamin adenosyltransferase; PFAM: cobalamin adenosyltransferase; KEGG: kpn:KPN_03215 propanediol utilization: B12 related; Belongs to the Cob(I)alamin adenosyltransferase family.
    
 0.931
Taci_1676
PFAM: CobB/CobQ domain protein glutamine amidotransferase; KEGG: dps:DP0218 cobyrinic acid A,C-diamide synthase (CobB).
  
 
 0.922
Taci_0082
PFAM: cobalamin adenosyltransferase; KEGG: maq:Maqu_1230 cobalamin adenosyltransferase.
     
 0.916
Taci_0049
PFAM: Uroporphyrin-III C/tetrapyrrole (Corrin/Porphyrin) methyltransferase; Precorrin-6x reductase CbiJ/CobK; cobalamin (vitamin B12) biosynthesis CbiG protein; KEGG: dde:Dde_3181 precorrin-3 methyltransferase.
 
   
 0.867
Taci_0051
TIGRFAM: precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; PFAM: Methyltransferase type 12; Methyltransferase type 11; methyltransferase small; protein-L-isoaspartate(D- aspartate) O-methyltransferase; KEGG: dde:Dde_0803 precorrin-6Y C5,15- methyltransferase (decarboxylating).
     
 0.694
Taci_0043
TIGRFAM: uroporphyrin-III C-methyltransferase; PFAM: Uroporphyrin-III C/tetrapyrrole (Corrin/Porphyrin) methyltransferase; Uroporphyrinogen III synthase HEM4; KEGG: dvm:DvMF_2767 uroporphyrin-III C- methyltransferase.
    
 0.654
Your Current Organism:
Thermanaerovibrio acidaminovorans
NCBI taxonomy Id: 525903
Other names: T. acidaminovorans DSM 6589, Thermanaerovibrio acidaminovorans DSM 6589, Thermanaerovibrio acidaminovorans str. DSM 6589, Thermanaerovibrio acidaminovorans strain DSM 6589
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.