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
cobNCobalamin biosynthesis protein CobN; With CobST catalyzes the formation of cobyrinic acid a,c-diamide from hydrogenobyrinic acid a,c-diamide in an ATP-dependent manner; involved in porphyrin and chlorophyll metabolism; vitamin B12 metabolism; Derived by automated computational analysis using gene prediction method: Protein Homology. (1206 aa)    
Predicted Functional Partners:
AKD97405.1
Cobinamide adenolsyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.995
cobB
Cobyrinic acid a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of hydrogenobyrinate, using either L- glutamine or ammonia as the nitrogen source; Belongs to the CobB/CbiA family.
 
 
 0.985
AKD97850.1
precorrin-6Y methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.983
AKD97848.1
cobalt-precorrin-6X reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.955
AKD97404.1
Magnesium chelatase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.953
AKD97835.1
ATP-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the precorrin methyltransferase family.
 
  
 0.946
AKD98429.1
Cob(I)yrinic acid a,c-diamide adenosyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Cob(I)alamin adenosyltransferase family.
    
 0.935
cobH
Catalyzes the interconversion of precorrin-8X and hydrogenobyrinate; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.928
cobM
Precorrin-4 C11-methyltransferase; Catalyzes the methylation of C-11 in precorrin-4 to form precorrin-5.
 
   
 0.921
AKD97833.1
precorrin-3B synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.879
Your Current Organism:
Rhodococcus erythropolis
NCBI taxonomy Id: 1833
Other names: ATCC 4277, Arthrobacter hydrocarboglutamicus, Arthrobacter oxamicetus, Arthrobacter oxamicetus subsp. propiophenicolus, Arthrobacter paraffineus, Arthrobacter picolinophilus, Brevibacterium healii, Brevibacterium ketoglutamicum, Brevibacterium paraffinoliticum, CIP 104179, Corynebacterium alkanum, Corynebacterium aurantiacum, Corynebacterium humiferum, Corynebacterium sp. WS2071, Corynebacterium sp. WS2072, DSM 43066, IEGM 7, IFO 15567, JCM 20419, JCM 3201, LMG 5359, LMG:5359, Mycobacterium erythropolis, NBRC 15567, NCIB 11148, NCIB 9158, NCIB:11148, NCIB:9158, NCIMB 9158, NCTC 13021, NRRL B-16025, Nocardia calcarea, Nocardioides simplex ATCC 13260, Nocardioides simplex ATCC 19565, Nocardioides simplex ATCC 19566, R. erythropolis, Rhodococcus NI86/21, Rhodococcus sp. (strain NI86/21), Rhodococcus sp. ATCC 15108, Rhodococcus sp. ATCC 15961, Rhodococcus sp. ATCC 21035, Rhodococcus sp. BG43, Rhodococcus sp. BZ4, Rhodococcus sp. NCIB 9646, Rhodococcus sp. NI86/21, Rhodococcus sp. strain NI86/21, VKM Ac-858, strain N11
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