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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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cobD_1L_thr_O3P_dcar: threonine-phosphate decarboxylase. (357 aa)    
Predicted Functional Partners:
hisE
histidine_hisI: phosphoribosyl-ATP diphosphatase; In the N-terminal section; belongs to the PRA-CH family.
 
  
 0.990
cobD
Cobalamin biosynthesis protein CobD; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
 
  
 0.985
cobQ
Cobyric acid synthase CobQ; 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.
  
 0.981
hisB
Histidine biosynthesis bifunctional protein hisB; In the N-terminal section; belongs to the histidinol- phosphatase family.
  
 0.976
pduX
GHMP kinase N terminal domain protein.
 
 
 0.971
cobB
Cobyrinic 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; Belongs to the CobB/CbiA family.
  
 0.932
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
  
 0.922
cbiC
cobalt-precorrin-8X methylmutase.
  
 0.920
tyrA
T-protein.
  
  
 0.918
hisH
Imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
 
  
 0.903
Your Current Organism:
Yersinia rohdei
NCBI taxonomy Id: 29485
Other names: ATCC 43380, CCUG 38833, CDC 3022-85, CIP 103163, JCM 7376, LMG 8454, LMG:8454, Y. rohdei, strain H271-36/78
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