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
cobIPrecorrin-2 C(20)-methyltransferase; Methylates precorrin-2 at the C-20 position to produce precorrin-3A. (244 aa)    
Predicted Functional Partners:
cobH
Precorrin-8X methylmutase; Unknown EC_number=5.4.99.61.
 
 
 0.999
cobJ
Precorrin-3B C(17)-methyltransferase.
 
 0.999
cobL
Precorrin-6Y C(5,15)-methyltransferase [decarboxylating].
 
 0.992
cobK
Precorrin-6A reductase.
 
 
 0.991
cysG
Siroheme synthase; 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.
  
 
 0.977
sumT_1
Uroporphyrinogen-III C-methyltransferase; Belongs to the precorrin methyltransferase family.
 
 
 0.971
CEL27336.1
cobalt-precorrin-6A synthase.
 
  
 0.963
hemX
Putative uroporphyrinogen-III C-methyltransferase.
     
  0.955
cobM
Precorrin-4 C(11)-methyltransferase.
 
 
0.945
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.
 
  
 0.900
Your Current Organism:
Pseudomonas fluorescens
NCBI taxonomy Id: 294
Other names: ATCC 13525, Bacillus fluorescens, Bacillus fluorescens liquefaciens, Bacterium fluorescen, CCEB 546, CFBP 2102, CIP 69.13, DSM 50090, IAM 12022, IFO 14160, JCM 5963, Liquidomonas fluorescens, NBRC 14160, NCCB 76040, NCIB 9046, NCIB:9046, NCIMB 9046, NCTC 10038, NRRL B-14678, P. fluorescens, Pseudomonas sp. AU2390, Pseudomonas sp. BZ64, Pseudomonas sp. FY32, Pseudomonas sp. HSA2/2016, Pseudomonas sp. HSA3/2016, Pseudomonas sp. ISSDS-433, Pseudomonas sp. JCM 17186, Pseudomonas sp. JCM 2779, Pseudomonas sp. KH-20150KS3, Pseudomonas sp. LBUM223, Pseudomonas sp. LBUM636, Pseudomonas sp. SM2/2016, RH 818, VKM B-894, bacterium P1-1, strain M. Rhodes 28/5
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.