STRINGSTRING
ACT05031.1 ACT05031.1 ACT05032.1 ACT05032.1 ilvD ilvD ilvA ilvA ilvC ilvC ACT05462.1 ACT05462.1 ACT05463.1 ACT05463.1 leuD leuD leuC leuC leuB leuB leuA leuA ACT05478.1 ACT05478.1 ACT05479.1 ACT05479.1 ACT08057.1 ACT08057.1 ACT08251.1 ACT08251.1 ACT08252.1 ACT08252.1
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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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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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experimentally determined
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ACT05031.1TIGRFAM: 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; KEGG: eca:ECA4229 acetolactate synthase 2 catalytic subunit. (548 aa)
ACT05032.1KEGG: eca:ECA4228 acetolactate synthase 2 regulatory subunit. (85 aa)
ilvDKEGG: ect:ECIAI39_3015 dihydroxyacid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. (616 aa)
ilvAThreonine dehydratase, biosynthetic; 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. (514 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. (492 aa)
ACT05462.1PFAM: amino acid-binding ACT domain protein; KEGG: eca:ECA3849 acetolactate synthase 1 regulatory subunit. (97 aa)
ACT05463.1TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein domain protein TPP-binding; KEGG: eca:ECA3848 acetolactate synthase catalytic subunit. (554 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. (200 aa)
leuC3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (466 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. (363 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. (524 aa)
ACT05478.1TIGRFAM: 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; KEGG: eca:ECA3829 acetolactate synthase 3 catalytic subunit. (573 aa)
ACT05479.1KEGG: eca:ECA3828 acetolactate synthase 3 regulatory subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein. (163 aa)
ACT08057.1Tartrate dehydrogenase; KEGG: reh:H16_A0477 3-isopropylmalate dehydrogenase; TIGRFAM: tartrate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase. (361 aa)
ACT08251.1TIGRFAM: acetolactate synthase, catabolic; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: eca:ECA0741 acetolactate synthase; Belongs to the TPP enzyme family. (559 aa)
ACT08252.1KEGG: yen:YE4016 alpha-acetolactate decarboxylase; TIGRFAM: alpha-acetolactate decarboxylase; PFAM: alpha-acetolactate decarboxylase. (262 aa)
Your Current Organism:
Dickeya chrysanthemi
NCBI taxonomy Id: 561229
Other names: D. chrysanthemi Ech1591, Dickeya chrysanthemi Ech1591, Dickeya dadantii Ech1591, Dickeya zeae Ech1591
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