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cobJ protein (Pseudoflavonifractor capillosus) - STRING interaction network
"cobJ" - Precorrin-3B C(17)-methyltransferase in Pseudoflavonifractor capillosus
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
cobJPrecorrin-3B C(17)-methyltransferase; KEGG- lin-lin1162 6.6e-64 cbiH; similar to precorrin methylase K03395; COG- COG1010 Precorrin-3B methylase (247 aa)    
Predicted Functional Partners:
cobM
KEGG- mta-Moth_1092 3.6e-72 precorrin-4 C11-methyltransferase K03396; COG- COG2875 Precorrin-4 methylase (252 aa)
 
  0.999
EDN01191.1
CbiG; KEGG- pgi-PG0211 7.9e-39 cbiGF; cobalamin biosynthesis protein CbiG/precorrin-4 C11-methyltransferase K03396-K02189; COG- COG2073 Cobalamin biosynthesis protein CbiG (342 aa)
 
  0.999
cobK
Precorrin-6A reductase; KEGG- mta-Moth_1095 5.6e-35 precorrin-6x reductase K03397; COG- COG2099 Precorrin-6x reductase (251 aa)
 
  0.999
cbiT
Precorrin-6Y C5,15-methyltransferase (Decarboxylating), CbiT subunit; KEGG- ctc-CTC00734 3.6e-56 cbiT; precorrin-6B methylase/decarboxylase cbiT/cbiE K03399-K02191; COG- COG2241 Precorrin-6B methylase 1 (404 aa)
 
  0.999
cobI
Precorrin-2 C(20)-methyltransferase; KEGG- mst-Msp_0038 4.0e-34 cbiL; CbiL K03394; COG- COG2243 Precorrin-2 methylase; Psort location- Cytoplasmic, score-8.96; Belongs to the precorrin methyltransferase family (230 aa)
 
  0.999
cobH
KEGG- gme-Gmet_0477 2.4e-50 precorrin-8X methylmutase CbiC/CobH K01833; COG- COG2082 Precorrin isomerase; Psort location- Cytoplasmic, score-8.96 (216 aa)
 
  0.998
cbiD
Cobalt-precorrin-5B C(1)-methyltransferase; Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A (428 aa)
 
  0.998
cobD
Cobalamin biosynthesis protein CobD; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group (324 aa)
 
  0.997
cobB
Cobyrinate 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 (458 aa)
 
  0.997
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 (500 aa)
   
  0.995
Your Current Organism:
Pseudoflavonifractor capillosus
NCBI taxonomy Id: 411467
Other names: Bacteroides capillosus ATCC 29799, P. capillosus ATCC 29799, Pseudoflavonifractor capillosus, Pseudoflavonifractor capillosus ATCC 29799, Pseudoflavonifractor capillosus ATCC29799, Pseudoflavonifractor capillosus str. ATCC 29799, Pseudoflavonifractor capillosus strain ATCC 29799
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