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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
CCO57621.1Putative phosphatase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (213 aa)    
Predicted Functional Partners:
cobT
Putative Nicotinate mononucleotide:5, 6-dimethylbenzimidazole phosphoribosyltransferase (CobT); Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
 
 
 0.994
cobS-2
Putative Cobalamin (vitamin B12) biosynthesis CobS, cobalamin-5-phosphate 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.
 
 
 0.994
cobP
Bifunctional adenosylcobalamin biosynthesis protein cobP; Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
 
  
 0.952
CCO57622.1
Putative Peptidase M3B, oligoendopeptidase-related clade 3; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
       0.804
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.
 
  
 0.732
CCO61050.1
Putative Phosphoglycerate mutase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the phosphoglycerate mutase family.
  
     0.620
CCO60326.1
Putative threonine-phosphate decarboxylase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
 
  
 0.612
cobD
Putative Cobalamin (vitamin B12) biosynthesis CbiB; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
 
   
 0.528
cbiA
Putative Cobyrinic 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; Belongs to the CobB/CbiA family.
 
  
 0.463
CCO56470.1
Putative Cobalamin (vitamin B12) biosynthesis CbiB; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
 
   
 0.443
Your Current Organism:
Vibrio nigripulchritudo
NCBI taxonomy Id: 28173
Other names: ATCC 27043, Beneckea nigrapulchrituda, Beneckea nigripulchritudo, CAIM 323, CCUG 28586, CIP 103195, LMG 3896, LMG:3896, V. nigripulchritudo
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