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
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[Homology]
Score
MCBB_0049Putative glutamine amidotransferase-like protein MJ0138; sp|Q57602|Y138_METJA;evalue=2e-089; PctID=42.44; score=330. (496 aa)    
Predicted Functional Partners:
cbiC
Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate. cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 9/10; sp|O26329|CBIC_METTH;evalue=2e-053; PctID=54.37; score=208.
 
 
 0.949
cbiL
Putative cobalt-precorrin-2 C(20)-methyltransferase; Methylates cobalt-precorrin-2 at the C-20 position to produce cobalt-precorrin-3A in the anaerobic cobalamin biosynthesis pathway. S-adenosyl-L-homocysteine + cobalt-factor III. cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 2/10; sp|Q58181|CBIL_METJA;evalue=3e-031; PctID=38.96; score=135.
 
  
 0.894
cbiJ
Cobalt-precorrin-6A reductase; Catalyzes the reduction of the macrocycle of cobalt-precorrin-6A to cobalt-precorrin-6B. precorrin-6A + NADH. cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 7/10; sp|O27083|CBIJ_METTH;evalue=9e-023; PctID=44.00; score=107.
 
  
 0.886
cbiH
Putative cobalt-factor III C(17)-methyltransferase; Methyltransferase that likely catalyzes the ring contraction and methylation of C-17 in cobalt-factor III to form cobalt-factor IV. May also convert cobalt-precorrin-3 to cobalt-precorrin-4 (By similarity). S-adenosyl-L-homocysteine + cobalt-factor IV. cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 3/10; sp|O27454|CBIH_METTH;evalue=5e-119; PctID=56.98; score=427.
 
  
 0.851
cbiF
Catalyzes the methylation of C-11 in cobalt-precorrin-4 to form cobalt-precorrin-5A. S-adenosyl-L-homocysteine + cobalt-precorrin-5A. cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 4/10; sp|Q58973|CBIF_METJA;evalue=2e-074; PctID=58.23; score=278.
 
  
 0.827
cbiD
Cobalt-precorrin-5B C(1)-methyltransferase; Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
 
  
 0.809
cobS
Adenosylcobinamide-GDP ribazoletransferase; 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.
 
  
 0.734
cobD
Putative cobalamin biosynthesis protein CobD; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
 
  
 0.700
cbiG
Cobalt-precorrin-5A hydrolase; Catalyzes the hydrolysis of the ring A acetate delta-lactone of cobalt-precorrin-5A resulting in the loss of the C-20 carbon and its attached methyl group in the form of acetaldehyde. precorrin-5B + acetaldehyde + 2 H(+). cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 5/10; sp|Q05631|CBIG_SALTY;evalue=2e-021; PctID=44.44; score=103.
 
  
 0.688
cbiT
Putative cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating); Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
 
  
 0.685
Your Current Organism:
Methanobacterium congolense
NCBI taxonomy Id: 118062
Other names: DSM 7095, M. congolense, Methanobacterium congolense Cuzin et al. 2001, OCM 786, strain C
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