STRING protein interaction network
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:
some 3D structure is known or predicted
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
protein homology
Your Input:
Gene Fusion
cobSAdenosylcobinamide-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 (By similarity) (247 aa)    
Predicted Functional Partners:
Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase; Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB)
Adenosylcobinamide kinase / adenosylcobinamide-phosphate guanylyltransferase; Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate
Putative adenosylcobalamin phosphatase/alpha-ribazole phosphatase; Catalyzes the conversion of adenosylcobalamin 5'-phosphate to adenosylcobalamin (vitamin B12); involved in the assembly of the nucleotide loop of cobalamin. Also catalyzes the hydrolysis of the phospho group from alpha-ribazole 5'-phosphate to form alpha-ribazole
Cob(i)yrinic acid a,c-diamide adenosyltransferase; Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids (By similarity)
Cobalamin adenosyltransferase involved in ethanolamine utilization; Converts CNB12 to ADOB12
Fructose-6-phosphate aldolase 2; Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone and D-glyceraldehyde 3-phosphate via an aldolization reaction. Can utilize hydroxyacetone as an alternative donor substrate. Is also able to catalyze the direct self-aldol addition of glycolaldehyde. Is less catalytically efficient than the isozyme FsaA. Does not display transaldolase activity
Nucleoside triphosphate pyrophosphohydrolase; Involved in the regulation of bacterial cell survival under conditions of nutritional stress. Regulates the type II MazE-MazF toxin-antitoxin (TA) system which mediates programmed cell death (PCD). This is achieved by lowering the cellular concentration of (p)ppGpp produced by RelA under amino acid starvation, thus protecting the cell from the toxicity of MazF. Reduction of (p)ppGpp can be achieved by direct degradation of (p)ppGpp or by degradation of NTPs, which are substrates for (p)ppGpp synthesis by RelA
homocysteine-N5-methyltetrahydrofolate transmethylase, B12-dependent; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate
L,d-transpeptidase linking lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp
S-adenosylmethionine decarboxylase proenzyme; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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