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leuC leuC leuD leuD leuA leuA leuB leuB alaA_1 alaA_1 ilvC ilvC ilvH ilvH ilvB ilvB ilvD_2 ilvD_2 dat_1 dat_1 ilvA ilvA ilvK ilvK tdcB_1 tdcB_1 tdcB_2 tdcB_2 alaA_2 alaA_2
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.
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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
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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:
leuC3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (479 aa)
leuD3-isopropylmalate dehydratase small subunit; Belongs to the LeuD family. (202 aa)
leuA2-isopropylmalate synthase; Belongs to the alpha-IPM synthase/homocitrate synthase family. (399 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. Belongs to the isocitrate and isopropylmalate dehydrogenases family. (353 aa)
alaA_1Glutamate-pyruvate aminotransferase AlaA. (388 aa)
ilvCKetol-acid reductoisomerase (NADP(+)); 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. (345 aa)
ilvHAcetolactate synthase small subunit. (184 aa)
ilvBAcetolactate synthase. (569 aa)
ilvD_2Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. (574 aa)
dat_1D-alanine aminotransferase. (295 aa)
ilvAL-threonine 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. (505 aa)
ilvKBranched-chain-amino-acid aminotransferase 2. (360 aa)
tdcB_1L-threonine dehydratase catabolic TdcB. (317 aa)
tdcB_2L-threonine dehydratase catabolic TdcB. (317 aa)
alaA_2Aminotransferase. (406 aa)
Your Current Organism:
Luteitalea pratensis
NCBI taxonomy Id: 1855912
Other names: Acidobacteria bacterium DSM 100886, Acidobacteria bacterium HEG_-6_39, DSM 100886, KCTC 52215, L. pratensis, Luteitalea pratensis Vieira et al. 2017, strain HEG_-6_39
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