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leuA leuA serC serC tdcB tdcB glyA glyA hom hom thrB thrB ilvD ilvD ilvB ilvB ilvN ilvN ilvC ilvC leuB leuB leuC leuC leuD leuD sdaA sdaA ilvA ilvA ilvE ilvE thrC thrC serB serB
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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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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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 2 subfamily. (616 aa)
serCPhosphoserine Transaminase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. (376 aa)
tdcBTHREONINE DEHYDRATASE. (310 aa)
glyASerine Hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. (434 aa)
homHomoserine Dehydrogenase; Belongs to the homoserine dehydrogenase family. (445 aa)
thrBHomoserine Kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. (309 aa)
ilvDDIHYDROXY-ACID DEHYDRATASE; Belongs to the IlvD/Edd family. (613 aa)
ilvBACETOLACTATE SYNTHASE. (626 aa)
ilvNACETOHYDROXYACID SYNTHASE SMALL SUBUNIT. (172 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. (338 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 (By similarity); Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. (340 aa)
leuC3-ISOPROPYLMALATE DEHYDRATASE LARGE SUBUNIT; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily. (481 aa)
leuD3-ISOPROPYLMALATE DEHYDRATASE (SMALL SUBUNIT); Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (197 aa)
sdaAPROBABLE L-SERINE DEHYDRATASE (L-SERINE DEAMINASE); Belongs to the iron-sulfur dependent L-serine dehydratase family. (449 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). (436 aa)
ilvEBRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE. (379 aa)
thrCTHREONINE SYNTHASE; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (481 aa)
serBPhosphoserine Phosphatase. (446 aa)
Your Current Organism:
Corynebacterium glutamicum
NCBI taxonomy Id: 196627
Other names: C. glutamicum ATCC 13032, Corynebacterium glutamicum ATCC 13032, Corynebacterium glutamicum str. ATCC 13032, Corynebacterium glutamicum strain ATCC 13032
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