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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
AOI81565.1Cobalamin adenosyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Cob(I)alamin adenosyltransferase family. (183 aa)    
Predicted Functional Partners:
cobO
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.
    
 0.937
AOI83333.1
Adenosylcobinamide kinase/adenosylcobinamide phosphate guanyltransferase; Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
    
 0.930
cobS
Cobalamin 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.
    
 0.930
cobQ
Cobyric acid synthase; 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.
    
 0.927
AOI82442.1
Cobalamin biosynthesis protein CobN; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.924
cbiA
Cobyrinic acid a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source; Belongs to the CobB/CbiA family.
    
 0.922
AOI83335.1
Threonine-phosphate decarboxylase; Cobalamin biosynthesis protein; decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin; structurally similar to histidinol phosphate aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.918
cobD
Cobalamin biosynthesis protein CobD; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
    
 0.912
cobD-2
Cobalamin biosynthesis protein; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
    
 0.912
AOI85233.1
Cobalt chelatase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.901
Your Current Organism:
Burkholderia cepacia
NCBI taxonomy Id: 292
Other names: ATCC 25416, B. cepacia, Burkholderia cepacia genomovar I, Burkholderia sp. Bp7081, Burkholderia sp. Bp7091, Burkholderia sp. Bp7098, Burkholderia sp. Bp7108, Burkholderia sp. Bp7432, Burkholderia sp. LK29, Burkholderia sp. NCIM 5465, CCUG 12691, CCUG 13226, CFBP 2227, CIP 80.24, DSM 7288, ICMP 5796, IFO 14074, JCM 5964, NBRC 14074, NCCB 76047, NCPPB 2993, NCTC 10743, NRRL B-14810, Pseudomonas cepacia, Pseudomonas kingii, Pseudomonas multivorans, strain 717-ICPB 25, strain Ballard 717
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.