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phnH phnH phnG phnG phnC phnC pykF pykF phnN phnN phnM phnM phnL phnL phnI phnI phnP phnP adeD adeD pykA pykA mtn mtn
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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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colored nodes:
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
phnHRibophosphonate triphosphate synthase subunit; Together with PhnG, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate. (194 aa)
phnGRibophosphonate triphosphate synthase subunit; Together with PhnH, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate. (150 aa)
phnCPhosphonate ABC transporter ATPase; Part of the ABC transporter complex PhnCDE involved in phosphonates, phosphate esters, phosphite and phosphate import. Responsible for energy coupling to the transport system. (262 aa)
pykFPyruvate kinase I (formerly F), fructose stimulated; Protein involved in glycolysis, fermentation and anaerobic respiration. (470 aa)
phnNRibose 1,5-bisphosphokinase; Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP). Accepts ATP but not GTP as a phosphoryl donor, and uses ribose 1,5-bisphosphate but not ribose, ribose 1-phosphate, or ribose 5-phosphate as a phosphoryl acceptor. (185 aa)
phnMRibophosphonate triphosphate hydrolase; Catalyzes the hydrolysis of alpha-D-ribose 1- methylphosphonate triphosphate (RPnTP) to form alpha-D-ribose 1- methylphosphonate phosphate (PRPn) and diphosphate. Belongs to the metallo-dependent hydrolases superfamily. (378 aa)
phnLRibophosphonate triphosphate synthase subunit; Together with PhnG, PhnH and PhnI is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate; Belongs to the ABC transporter superfamily. (226 aa)
phnIRibophosphonate triphosphate synthase complex putative catalytic subunit; Together with PhnG, PhnH and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate. PhnI alone has nucleosidase activity, catalyzing the hydrolysis of ATP or GTP forming alpha-D-ribose 5-triphosphate and adenine or guanine, respectively. (354 aa)
phnP5-phospho-alpha-D-ribosyl 1,2-cyclic phosphate phosphodiesterase; Catalyzes the hydrolysis of the cyclic ribose-phosphate to form alpha-D-ribose 1,5-bisphosphate. (252 aa)
adeDCryptic adenine deaminase; Protein involved in metabolic process; Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family. (588 aa)
pykAPyruvate kinase II, glucose stimulated; Protein involved in glycolysis, fermentation and anaerobic respiration. (480 aa)
mtn5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5- deoxyribose and adenine. Thus, is required for in vivo function of the radical SAM enzymes biotin synthase and lipoic acid synthase, that are inhibited by 5'-deoxyadenosine accumulati [...] (232 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 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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