STRINGSTRING
hom hom lysC lysC thrC thrC ilvI ilvI ABZ96827.1 ABZ96827.1 ilvC ilvC ilvB1 ilvB1 leuA2 leuA2 thrB thrB leuC1 leuC1 leuD1 leuD1 leuA1 leuA1 ilvA ilvA leuC2 leuC2 leuD2 leuD2 leuA leuA serA2 serA2 serA1 serA1 leuB leuB ilvH ilvH ilvB2 ilvB2 serC serC metK metK ABZ99321.1 ABZ99321.1 metF metF ilvD ilvD ilvE ilvE metH metH asd asd
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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
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
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homHomoserine dehydrogenase (HDH); Function of homologous gene experimentally demonstrated in an other organism; enzyme. (427 aa)
lysCAspartokinase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the aspartokinase family. (404 aa)
thrCThreonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (449 aa)
ilvIAHAS; Acetohydroxy-acid synthase large subunit; ALS; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (587 aa)
ABZ96827.1Alanine--valine transaminase; Transaminase C; Valine--pyruvate aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (424 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. (333 aa)
ilvB1AHAS-I; Acetohydroxy-acid synthase I large subunit; ALS-I; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (573 aa)
leuA22-isopropylmalate synthase (Alpha-isopropylmalate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the alpha-IPM synthase/homocitrate synthase family. (394 aa)
thrBHomoserine kinase (HSK; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. (317 aa)
leuC13-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (467 aa)
leuD13-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. (208 aa)
leuA12-isopropylmalate synthase (Alpha-isopropylmalate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the alpha-IPM synthase/homocitrate synthase family. (511 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. (425 aa)
leuC23-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (464 aa)
leuD23-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. (208 aa)
leuA2-isopropylmalate synthase (Alpha-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. (500 aa)
serA2D-3-phosphoglycerate dehydrogenase (PGDH); Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L- serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. (407 aa)
serA1D-3-phosphoglycerate dehydrogenase (PGDH); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. (328 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. (359 aa)
ilvHAHAS; Acetohydroxy-acid synthase small subunit; ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. (162 aa)
ilvB2AHAS; Acetohydroxy-acid synthase large subunit; ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. (575 aa)
serCPhosphoserine aminotransferase (PSAT); Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. (365 aa)
metKS-adenosylmethionine synthetase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. (388 aa)
ABZ99321.1Putative aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (397 aa)
metF5,10-methylenetetrahydrofolate reductase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the methylenetetrahydrofolate reductase family. (295 aa)
ilvDDihydroxy-acid dehydratase (DAD); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family. (558 aa)
ilvEBranched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (307 aa)
metHMethionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. (1250 aa)
asdAspartate semialdehyde dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the aspartate-semialdehyde dehydrogenase family. (349 aa)
Your Current Organism:
Leptospira biflexa
NCBI taxonomy Id: 456481
Other names: L. biflexa serovar Patoc strain 'Patoc 1 (Paris)', Leptospira biflexa serovar Patoc str. ATCC 23582, Leptospira biflexa serovar Patoc strain 'Patoc 1 (Paris)', Leptospira biflexa serovar Patoc strain Patoc 1
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