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.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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cbiACobyrinic acid a,c-diamide synthase (cbiA); 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. (443 aa)    
Predicted Functional Partners:
cbiC
Cobalamin biosynthesis precorrin isomerase (cbiC); Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate. Belongs to the CobH/CbiC family.
 
 0.997
cobQ
Cobyric acid synthase (cbiP); 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 (By similarity); Belongs to the CobB/CobQ family. CobQ subfamily.
  
 0.987
cbiL
Cobalamin biosynthesis precorrin-2 methyltransferase (cbiL); Methylates cobalt-precorrin-2 at the C-20 position to produce cobalt-precorrin-3A in the anaerobic cobalamin biosynthesis pathway.
  
 0.985
cbiT
Cobalamin biosynthesis precorrin-8W decarboxylase (cbiT); Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
 
  
 0.974
cbiF
Cobalamin biosynthesis precorrin-3 methylase (cbiF); Catalyzes the methylation of C-11 in cobalt-precorrin-4 to form cobalt-precorrin-5A.
  
 0.957
MJ_0908
Cobalamin biosynthesis protein (cobN); Similar to GB:M62866 SP:P29929 PID:151154 percent identity: 37.24; identified by sequence similarity; putative; Belongs to the Mg-chelatase subunit H family.
 
 
 0.948
MJ_1441
Magnesium chelatase subunit (chlH); Similar to GB:Z68495 PID:1154627 percent identity: 35.26; identified by sequence similarity; putative; Belongs to the Mg-chelatase subunit H family.
  
 
 0.945
cbiX
Conserved hypothetical protein; 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.
    
 0.938
cbiH
Cobalamin biosynthesis precorrin-3 methylase (cbiH); 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).
 
  
 0.931
cfbD
Vanadium nitrogenase-associated protein N; 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 both the six-electron reduction of the tetrahydroporphyrin ring system and the gamma-lactamization of the c- acetamide side chain of Ni-sirohydrochlorin a,c-diamide to yield 15,17(3)-seco-F430-17(3)-acid (seco-F430), the last intermediate in the biosynthesis of the coenzyme F430; Belongs to the NifD/NifK/NifE/NifN family.
 
  
 0.907
Your Current Organism:
Methanocaldococcus jannaschii
NCBI taxonomy Id: 243232
Other names: M. jannaschii DSM 2661, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii str. DSM 2661, Methanococcus jannaschii DSM 2661
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