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thrB thrB thrC thrC pfs pfs metQ metQ metI metI metN metN ybdH ybdH ybdL ybdL malY malY yebR yebR luxS luxS metK metK metC metC asd asd nlpA nlpA metR metR metE metE metJ metJ metB metB metL metL metF metF metA metA metH metH lysC lysC
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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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:
thrBHomoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. (310 aa)
thrCThreonine synthase; Function experimentally demonstrated in the studied species; enzyme. (428 aa)
pfs5'-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 accumulatio [...] (232 aa)
metQDL-methionine transporter subunit; Function experimentally demonstrated in the studied species; transporter; Belongs to the nlpA lipoprotein family. (271 aa)
metIDL-methionine transporter subunit; Function experimentally demonstrated in the studied species; transporter. (217 aa)
metNDL-methionine transporter subunit; Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system. (343 aa)
ybdHPutative oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (362 aa)
ybdLMethionine aminotransferase, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (386 aa)
malYBifunctional beta-cystathionase, PLP-dependent and regulator of maltose regulon; Function experimentally demonstrated in the studied species; enzyme. (390 aa)
yebRConserved hypothetical protein; Homologs of previously reported genes of unknown function. (183 aa)
luxSS-ribosylhomocysteinase; Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). Belongs to the LuxS family. (171 aa)
metKMethionine adenosyltransferase 1; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. (384 aa)
metCCystathionine beta-lyase, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (395 aa)
asdAspartate-semialdehyde dehydrogenase, NAD(P)-binding; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family. (367 aa)
nlpACytoplasmic membrane lipoprotein-28; Function experimentally demonstrated in the studied species; lipoprotein; Belongs to the nlpA lipoprotein family. (272 aa)
metRDNA-binding transcriptional activator, homocysteine-binding; Function experimentally demonstrated in the studied species; regulator; Belongs to the LysR transcriptional regulatory family. (317 aa)
metE5-methyltetrahydropteroyltriglutamate- homocysteine S-methyltransferase; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation; Belongs to the vitamin-B12 independent methionine synthase family. (753 aa)
metJDNA-binding transcriptional repressor, S-adenosylmethionine-binding; This regulatory protein, when combined with SAM (S- adenosylmethionine) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis; Belongs to the MetJ family. (151 aa)
metBCystathionine gamma-synthase, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (386 aa)
metLFused aspartokinase II; Function experimentally demonstrated in the studied species; enzyme; In the C-terminal section; belongs to the homoserine dehydrogenase family. (810 aa)
metF5,10-methylenetetrahydrofolate reductase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the methylenetetrahydrofolate reductase family. (296 aa)
metAHomoserine transsuccinylase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. (309 aa)
metHhomocysteine-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. (1227 aa)
lysCAspartokinase III; Function experimentally demonstrated in the studied species; enzyme; Belongs to the aspartokinase family. (449 aa)
Your Current Organism:
Escherichia coli UMN026
NCBI taxonomy Id: 585056
Other names: E. coli UMN026
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