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
cbiACobyrinic 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. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP- dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source. (451 aa)    
Predicted Functional Partners:
ADZ08388.1
Precorrin-2 C20-methyltransferase; TIGRFAM: Cobalamin (vitamin B12) biosynthesis CobI/CbiL, precorrin-2 C20-methyltransferase, core; KEGG: mst:Msp_0038 CbiL; PFAM: Tetrapyrrole methylase.
  
 0.999
cbiX
Sirohydrochlorin cobaltochelatase; Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni- sirohydrochlorin.
 
  
 0.999
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.
 
  
 0.999
cbiT
cobalt-precorrin-6Y 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.
 
  
 0.999
ADZ10437.1
Precorrin-6x reductase; KEGG: mst:Msp_1205 CbiJ; TIGRFAM: Cobalamin (vitamin B12) biosynthesis CobK/CbiJ, precorrin-6x reductase; PFAM: Cobalamin (vitamin B12) biosynthesis CobK/CbiJ, precorrin-6x reductase.
 
  
 0.999
hemA
Glutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
     
 0.999
ADZ10352.1
Precorrin-8X methylmutase CbiC/CobH; PFAM: Cobalamin (vitamin B12) biosynthesis CobH/CbiC, precorrin-8X methylmutase, core; KEGG: mst:Msp_1179 precorrin-8X methylmutase.
 
 0.996
ADZ08370.1
precorrin-3B C17-methyltransferase; TIGRFAM: Cobalamin (vitamin B12) biosynthesis CobJ/CibH, precorrin-3B C17-methyltransferase, core; KEGG: mfv:Mfer_1185 precorrin-3 methyltransferase; PFAM: Cysteine-rich small domain; Tetrapyrrole methylase.
 
  
 0.992
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.
  
 0.961
cobD
Cobalamin biosynthesis protein cbiB; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
  
 0.939
Your Current Organism:
Methanobacterium lacus
NCBI taxonomy Id: 877455
Other names: DSM 24406, JCM 17760, M. lacus, Methanobacterium lacus Borrel et al. 2012, Methanobacterium sp. 17A1, Methanobacterium sp. AL-21, strain 17A1
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