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dmdA dmdA ilvH ilvH ilvG ilvG ilvD_1 ilvD_1 dat dat tdcB tdcB leuA_1 leuA_1 thrC_1 thrC_1 leuA_2 leuA_2 ilvD_2 ilvD_2 ilvC ilvC AMV26552.1 AMV26552.1 ilvA ilvA thrC_2 thrC_2 hicd hicd ilvB ilvB AMV28415.1 AMV28415.1 AMV28416.1 AMV28416.1 thrC_3 thrC_3 ilvB1 ilvB1 ilvE ilvE dmlA dmlA dmdB dmdB
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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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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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Your Input:
dmdA2,3-dimethylmalate dehydratase large subunit; Belongs to the aconitase/IPM isomerase family. (434 aa)
ilvHPutative acetolactate synthase small subunit. (168 aa)
ilvGAcetolactate synthase isozyme 2 large subunit; Belongs to the TPP enzyme family. (630 aa)
ilvD_1Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. (651 aa)
datD-alanine aminotransferase. (282 aa)
tdcBL-threonine dehydratase catabolic TdcB. (318 aa)
leuA_12-isopropylmalate synthase; Belongs to the alpha-IPM synthase/homocitrate synthase family. (534 aa)
thrC_1Threonine synthase. (407 aa)
leuA_22-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. (528 aa)
ilvD_2Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. (560 aa)
ilvCKetol-acid reductoisomerase. (349 aa)
AMV26552.1SMP-30/Gluconolaconase/LRE-like region. (324 aa)
ilvAL-threonine dehydratase biosynthetic IlvA; 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. (506 aa)
thrC_2Threonine synthase. (464 aa)
hicdHomoisocitrate dehydrogenase. (91 aa)
ilvBAcetolactate synthase isozyme 1 large subunit. (187 aa)
AMV28415.1Hypothetical protein; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain. (160 aa)
AMV28416.1Enterobactin/ferric enterobactin esterase. (359 aa)
thrC_3Threonine synthase. (423 aa)
ilvB1Acetolactate synthase large subunit IlvB1. (589 aa)
ilvEBranched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (288 aa)
dmlAD-malate dehydrogenase. (354 aa)
dmdB2,3-dimethylmalate dehydratase small subunit; Belongs to the LeuD family. (189 aa)
Your Current Organism:
Gemmata sp. SHPL17
NCBI taxonomy Id: 1630693
Other names: G. sp. SH-PL17, Gemmata sp. SH-PL17
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