STRINGSTRING
Bsel_0752 Bsel_0752 ilvD ilvD tdh tdh Bsel_1819 Bsel_1819 ilvA ilvA Bsel_1960 Bsel_1960 Bsel_2170 Bsel_2170 serC serC ilvE ilvE Bsel_2528 Bsel_2528 Bsel_2529 Bsel_2529 ilvC ilvC leuA leuA leuB leuB leuC leuC leuD leuD Bsel_3261 Bsel_3261 Bsel_3262 Bsel_3262 thrB thrB
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:
Bsel_0752KEGG: mxa:MXAN_1432 L-allo-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; aminotransferase class I and II. (342 aa)
ilvDTIGRFAM: dihydroxy-acid dehydratase; KEGG: mca:MCA2082 dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. (583 aa)
tdhL-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. (346 aa)
Bsel_1819Pyridoxal phosphate-dependent acyltransferase; Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. (393 aa)
ilvAThreonine dehydratase; 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. (422 aa)
Bsel_1960KEGG: dol:Dole_2663 branched-chain amino acid aminotransferase; TIGRFAM: branched-chain amino acid aminotransferase; PFAM: aminotransferase class IV. (355 aa)
Bsel_2170KEGG: sfu:Sfum_3649 D-3-phosphoglycerate dehydrogenase; TIGRFAM: D-3-phosphoglycerate dehydrogenase; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding; D-isomer specific 2-hydroxyacid dehydrogenase catalytic region; amino acid-binding ACT domain protein. (536 aa)
serCPhosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. (359 aa)
ilvEBranched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (301 aa)
Bsel_2528KEGG: sfu:Sfum_3023 acetolactate synthase, large subunit, biosynthetic type; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region. (579 aa)
Bsel_2529KEGG: sfu:Sfum_3022 acetolactate synthase, small subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein. (173 aa)
ilvCKetol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. (333 aa)
leuA2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. (520 aa)
leuB3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. (368 aa)
leuC3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (471 aa)
leuD3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. (194 aa)
Bsel_3261KEGG: gur:Gura_2178 homoserine dehydrogenase; PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase NAD-binding. (433 aa)
Bsel_3262Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (353 aa)
thrBHomoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. (305 aa)
Your Current Organism:
Bacillus selenitireducens
NCBI taxonomy Id: 439292
Other names: Bacillus selenitireducens MLS10, [. selenitireducens MLS10, [Bacillus] selenitireducens MLS10
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.