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Pnec_0337 Pnec_0337 Pnec_0444 Pnec_0444 Pnec_0810 Pnec_0810 Pnec_0811 Pnec_0811 ilvC ilvC leuA leuA Pnec_0838 Pnec_0838 leuB leuB leuD leuD leuC leuC ilvD ilvD ilvE ilvE ilvA ilvA
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Pnec_0337PFAM: thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein TPP binding domain protein; KEGG: rpa:RPA4054 possible acetolactate synthase large subunit; Belongs to the TPP enzyme family. (601 aa)
Pnec_0444PFAM: aminotransferase class I and II; KEGG: pnu:Pnuc_0437 aminotransferase AlaT. (295 aa)
Pnec_0810TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein TPP binding domain protein; KEGG: pnu:Pnuc_1063 acetolactate synthase, large subunit, biosynthetic type. (595 aa)
Pnec_0811TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: pnu:Pnuc_1062 acetolactate synthase 3 regulatory subunit. (163 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)
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. (515 aa)
Pnec_0838KEGG: pnu:Pnuc_1028 tartrate dehydrogenase. (120 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. (356 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. (215 aa)
leuC3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (469 aa)
ilvDKEGG: pnu:Pnuc_0680 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. (563 aa)
ilvEBranched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (307 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. (506 aa)
Your Current Organism:
Polynucleobacter necessarius
NCBI taxonomy Id: 452638
Other names: P. necessarius STIR1, Polynucleobacter necessarius STIR1, Polynucleobacter necessarius subsp. necessarius STIR1
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