STRINGSTRING
thrC thrC ilvA-II ilvA-II cysK cysK PP_4430 PP_4430 ilvA-I ilvA-I PP_3191 PP_3191 PP_2930 PP_2930 PP_2009 PP_2009 cysM cysM PP_1113 PP_1113 PP_0662 PP_0662 trpB trpB
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:
thrCThreonine synthase. (469 aa)
ilvA-IIThreonine deaminase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. (504 aa)
cysKCysteine synthase A; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Serine family; Belongs to the cysteine synthase/cystathionine beta- synthase family. (324 aa)
PP_4430Putative threonine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. (330 aa)
ilvA-IThreonine deaminase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. (530 aa)
PP_3191Putative threonine ammonia-lyase / dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Energymetabolism : Amino acids and amines. (350 aa)
PP_2930Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. (305 aa)
PP_2009Putative 1-aminocyclopropane-1-carboxylate deaminase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. (297 aa)
cysMCysteine synthase B; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Serine family; Belongs to the cysteine synthase/cystathionine beta- synthase family. (299 aa)
PP_1113Pyridoxal-phosphate dependent enzyme family protein. (300 aa)
PP_0662Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. (462 aa)
trpBTryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (405 aa)
Your Current Organism:
Pseudomonas putida KT2440
NCBI taxonomy Id: 160488
Other names: P. putida KT2440, Pseudomonas putida (strain KT2440), Pseudomonas putida str. KT2440
Server load: low (10%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.