STRINGSTRING
ilvD ilvD bcd bcd mmgB mmgB ilvC ilvC fadB fadB thrC thrC fadE fadE fadA fadA alsS alsS pta pta ilvE ilvE amyE amyE argD argD pycA pycA pyrD pyrD xynC xynC ilvA ilvA
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:
ilvDDihydroxy-acid dehydratase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the IlvD/Edd family. (558 aa)
bcdBranched-chain amino acid dehydrogenase; Catalyzes the reversible deamination of L-leucine to 4- methyl-2-oxopentanoate. (364 aa)
mmgB3-hydroxybutyryl-CoA dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (287 aa)
ilvCAcetohydroxy-acid isomeroreductase; 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. (342 aa)
fadBenoyl-CoA hydratase; Involved in the degradation of long-chain fatty acids. (258 aa)
thrCThreonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (352 aa)
fadEacyl-CoA dehydrogenase (FAD dependent); Involved in the degradation of long-chain fatty acids. (594 aa)
fadAacetyl-CoA C-acyltransferase; Involved in the degradation of long-chain fatty acids; Belongs to the thiolase-like superfamily. Thiolase family. (391 aa)
alsSAlpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (570 aa)
ptaPhosphotransacetylase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (323 aa)
ilvEKetomethiobutyrate-branched-chain/aromatic amino acid aminotransferase; Transaminates branched-chain amino acids and ketoglutarate. Involved in the final step of the methionine regeneration pathway, where ketomethiobutyrate (KMTB) is converted to methionine via a transamination. The amino donor preference is isoleucine, leucine, valine, phenylalanine, and tyrosine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (356 aa)
amyEAlpha-amylase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glycosyl hydrolase 13 family. (659 aa)
argDN-acetylornithine aminotransferase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. (385 aa)
pycAPyruvate carboxylase; Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second, leading to oxaloacetate production. Fulfills an anaplerotic function in B.subtilis as it is necessary for growth on glucose, but is not required for sporulation. (1148 aa)
pyrDDihydroorotate dehydrogenase (catalytic subunit); Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor. (311 aa)
xynCEndo-xylanase; Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA). Belongs to the glycosyl hydrolase 30 family. (422 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 (By similarity). (422 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
Server load: low (38%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.