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
cbiG/cobJBifunctional cbiH protien and PRECORRIN-3B C17-METHYLTRANSFERASE; Citation: Debussche et al. (1993) J. Bacteriol. 175:7430-7440; Roth et al. (1993) J. Bacteriol. 175:3303-3316. (544 aa)    
Predicted Functional Partners:
cbiD
Cobalamin biosynthesis protein D; Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
 
 
 0.999
cobH
Putative Precorrin-8X methylmutase CobH; Citation: Thibaut et al. (1992) J. Bacteriol. 174:1043-1049.
 
  
 0.999
cobI/cbiL
PRECORRIN-2 C20-METHYLTRANSFERASE; Cobalamin biosynthesis; Citation: Blanche et al. (1989) J. Bacteriol. 171:4222-4231; Roth et al. (1993) J. Bacteriol. 175:3303-3316; Belongs to the precorrin methyltransferase family.
  
 0.999
cobL
Putative precorrin-6y methylase; Citation: Blanche et al. (1992) J. Bacteriol. 174:1050-1052.
 
  
 0.999
cobB
Cobyric acid synthase CobB; 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.
  
 0.999
SYNW1776
Conserved hypothetical protein.
 
  
 0.999
cobM
PUTATIVE PRECORRIN-4 C11-METHYLTRANSFERASE; Citation: Crouzet et al. (1990) J. Bacteriol. 172:5968-5979; Debussche et al. (1993) J. Bacteriol. 175:7430-7440; Belongs to the precorrin methyltransferase family.
 
 0.999
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.
 
  
 0.989
cbiA,cobB
Putative Cobyrinic acid a,c-diamide synthase; BELONGS TO THE SIRTUIN FAMILY; Citation: Tsang and Escalante-Semerena (1996) J. Bacteriol. 178:7016-7019.
 
  
 0.967
cobD
Putative cobalamin biosynthetic protein; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
 
  
 0.912
Your Current Organism:
Synechococcus sp. WH 8102
NCBI taxonomy Id: 84588
Other names: S. sp. WH 8102, Synechococcus sp. WH8102
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