STRINGSTRING
thrA thrA thrB thrB thrC thrC dapB dapB dapD dapD dapA dapA lysA lysA asd asd dapF dapF 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.
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:
thrABifunctional: aspartokinase I (N-terminal); homoserine dehydrogenase I (C-terminal); Protein involved in threonine biosynthetic process, methionine biosynthetic process and homoserine biosynthetic process. (820 aa)
thrBHomoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. Is also able to phosphorylate the hydroxy group on gamma-carbon of L-homoserine analogs when the functional group at the alpha-position is a carboxyl, an ester, or even a hydroxymethyl group. Neither L-threonine nor L-serine are substrates of the enzyme. (310 aa)
thrCL-threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. To a lesser extent, is able to slowly catalyze the deamination of L-threonine into alpha-ketobutyrate and that of L-serine and 3-chloroalanine into pyruvate. Is also able to rapidly convert vinylglycine to threonine, which proves that the pyridoxal p-quinonoid of vinylglycine is an intermediate in the TS reaction. (428 aa)
dapBDihydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. Can use both NADH and NADPH as a reductant, with NADH being twice as effective as NADPH. Belongs to the DapB family. (273 aa)
dapD2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase; Protein involved in lysine biosynthetic process via diaminopimelate; Belongs to the transferase hexapeptide repeat family. (274 aa)
dapADihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). Belongs to the DapA family. (292 aa)
lysADiaminopimelate decarboxylase, PLP-binding; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. Is not active against the DD- or LL-isomers of diaminopimelate; Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily. (420 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. (367 aa)
dapFDiaminopimelate epimerase; Involved in the succinylase branch of the L-lysine biosynthesis and in the biosynthesis of the pentapeptide incorporated in the peptidoglycan moiety. Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso- diaminoheptanedioate (meso-DAP). (274 aa)
lysCLysine-sensitive aspartokinase 3; Aspartokinase III, lysine sensitive; Protein involved in lysine biosynthetic process via diaminopimelate and homoserine biosynthetic process. (449 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
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.