STRINGSTRING
ilvA ilvA AFZ00906.1 AFZ00906.1 AFZ02289.1 AFZ02289.1 AFZ02345.1 AFZ02345.1 asd asd thrB thrB AFZ02782.1 AFZ02782.1
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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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Your Input:
ilvAL-threonine ammonia-lyase; 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. (503 aa)
AFZ00906.1L-threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase; COGs: COG0498 Threonine synthase; InterPro IPR004450:IPR001926; KEGG: npu:Npun_R0769 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; PRIAM: Threonine synthase; SPTR: Threonine synthase; TIGRFAM: Threonine synthase. (434 aa)
AFZ02289.1L-threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (363 aa)
AFZ02345.1Aspartate kinase; PFAM: ACT domain; Amino acid kinase family; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase; COGs: COG0527 Aspartokinase; InterPro IPR001048:IPR002912:IPR005260:IPR001341; KEGG: npu:Npun_R4597 aspartate kinase; PFAM: Aspartate/glutamate/uridylate kinase; Amino acid-binding ACT; SPTR: Aspartokinase; TIGRFAM: Aspartate kinase domain; Aspartate kinase, monofunctional class. (598 aa)
asdAspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family. (347 aa)
thrBHomoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. (309 aa)
AFZ02782.1PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain; COGs: COG0460 Homoserine dehydrogenase; InterPro IPR005106:IPR001342:IPR002912; KEGG: naz:Aazo_4841 homoserine dehydrogenase; PFAM: Homoserine dehydrogenase, catalytic; Aspartate/homoserine dehydrogenase, NAD-binding; Amino acid-binding ACT; SPTR: Homoserine dehydrogenase. (463 aa)
Your Current Organism:
Calothrix sp. PCC6303
NCBI taxonomy Id: 1170562
Other names: C. sp. PCC 6303, Calothrix sp. (ATCC 29156), Calothrix sp. (PCC 6303), Calothrix sp. ATCC 29156, Calothrix sp. PCC 6303
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