STRINGSTRING
AFY99285.1 AFY99285.1 ilvA ilvA ilvC ilvC AFY99979.1 AFY99979.1 AFZ00011.1 AFZ00011.1 AFZ00155.1 AFZ00155.1 AFZ00208.1 AFZ00208.1 AFZ00221.1 AFZ00221.1 AFZ00906.1 AFZ00906.1 ilvD ilvD AFZ02219.1 AFZ02219.1 AFZ02289.1 AFZ02289.1 AFZ02307.1 AFZ02307.1 AFZ02310.1 AFZ02310.1 AFZ02345.1 AFZ02345.1 asd asd leuC leuC AFZ02570.1 AFZ02570.1 AFZ02727.1 AFZ02727.1 thrB thrB AFZ02758.1 AFZ02758.1 AFZ02782.1 AFZ02782.1 AFZ03077.1 AFZ03077.1 leuA leuA leuB leuB pdxA pdxA AFZ04053.1 AFZ04053.1 ilvE ilvE leuA-2 leuA-2
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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
Your Input:
AFY99285.12-isopropylmalate synthase; PFAM: HMGL-like; LeuA allosteric (dimerisation) domain; TIGRFAM: 2-isopropylmalate synthase/homocitrate synthase family protein; COGs: COG0119 Isopropylmalate/homocitrate/citramalate synthase; InterPro IPR000891:IPR013709:IPR005675; KEGG: npu:Npun_F4065 putative alpha-isopropylmalate/homocitrate synthase family transferase; PFAM: 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; Pyruvate carboxyltransferase; PRIAM: (R)-citramalate synthase; SMART: 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; SPTR: 2-isopropylmalate synt [...] (538 aa)
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)
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. (331 aa)
AFY99979.1Phosphoenolpyruvate synthase; PFAM: PEP-utilising enzyme, mobile domain; PEP-utilising enzyme, TIM barrel domain; Pyruvate phosphate dikinase, PEP/pyruvate binding domain; TIGRFAM: phosphoenolpyruvate synthase; COGs: COG0574 Phosphoenolpyruvate synthase/pyruvate phosphate dikinase; InterPro IPR002192:IPR008279:IPR000121; KEGG: ana:alr3397 phosphoenolpyruvate synthase; PFAM: PEP-utilising enzyme; PEP-utilising enzyme, mobile domain; Pyruvate phosphate dikinase, PEP/pyruvate-binding; PRIAM: Pyruvate, water dikinase; SPTR: Phosphoenolpyruvate synthase. (771 aa)
AFZ00011.1Phosphoserine aminotransferase apoenzyme; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. (389 aa)
AFZ00155.1PFAM: ACT domain; Small subunit of acetolactate synthase; TIGRFAM: acetolactate synthase, small subunit; COGs: COG0440 Acetolactate synthase small (regulatory) subunit; InterPro IPR004789:IPR002912:IPR019455; KEGG: npu:Npun_F1890 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT; PRIAM: Acetolactate synthase; SPTR: Acetolactate synthase, small subunit; TIGRFAM: Acetolactate synthase, small subunit. (172 aa)
AFZ00208.1PFAM: PEP-utilising enzyme, mobile domain; Domain of unknown function (DUF205); Pyruvate phosphate dikinase, PEP/pyruvate binding domain; COGs: COG0574 Phosphoenolpyruvate synthase/pyruvate phosphate dikinase; InterPro IPR002192:IPR008279; KEGG: npu:Npun_F1309 pyruvate phosphate dikinase, PEP/pyruvate-binding; PFAM: Pyruvate phosphate dikinase, PEP/pyruvate-binding; PEP-utilising enzyme, mobile domain; SPTR: Pyruvate phosphate dikinase, PEP/pyruvate-binding. (961 aa)
AFZ00221.1PFAM: HMGL-like; TIGRFAM: homocitrate synthase NifV; COGs: COG0119 Isopropylmalate/homocitrate/citramalate synthase; InterPro IPR013477:IPR000891; KEGG: npu:Npun_F0430 trans-homoaconitate synthase; PFAM: Pyruvate carboxyltransferase; PRIAM: Homocitrate synthase; SPTR: Homocitrate synthase; TIGRFAM: Homocitrate synthase NifV-type; Belongs to the alpha-IPM synthase/homocitrate synthase family. (378 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)
ilvDPFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; COGs: COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; HAMAP: Dihydroxy-acid dehydratase; InterPro IPR004404:IPR000581; KEGG: ana:alr2771 dihydroxy-acid dehydratase; PFAM: Dihydroxy-acid/6-phosphogluconate dehydratase; PRIAM: Dihydroxy-acid dehydratase; SPTR: Dihydroxy-acid dehydratase; TIGRFAM: Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. (562 aa)
AFZ02219.1Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterPro IPR012001:IPR012000:IPR011766:IPR012846; KEGG: npu:Npun_R1735 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enz [...] (633 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)
AFZ02307.1Acetolactate synthase; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterPro IPR012001:IPR012000:IPR011766; KEGG: npu:Npun_F2094 thiamine pyrophosphate binding domain-containing protein; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; PRIAM: Acetolactate synthase; SPTR: Thiamine py [...] (598 aa)
AFZ02310.1Valine-pyruvate aminotransferase apoenzyme; PFAM: Aminotransferase class I and II; COGs: COG3977 Alanine-alpha-ketoisovalerate (or valine-pyruvate) aminotransferase; InterPro IPR004839; KEGG: naz:Aazo_0165 class I/II aminotransferase; PFAM: Aminotransferase, class I/classII; PRIAM: Valine--pyruvate transaminase; SPTR: Aminotransferase, class I and II. (427 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)
leuC3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (468 aa)
AFZ02570.13-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. (194 aa)
AFZ02727.1Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterPro IPR012001:IPR012000:IPR011766; KEGG: ava:Ava_3533 acetolactate synthase; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; PRIAM: Acetolactate synthase; SPTR: Acetolactate synthase. (547 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)
AFZ02758.1PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; ACT domain; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; TIGRFAM: L-serine dehydratase, iron-sulfur-dependent, beta subunit; D-3-phosphoglycerate dehydrogenase; COGs: COG0111 Phosphoglycerate dehydrogenase and related dehydrogenase; InterPro IPR006236:IPR006139:IPR006140:IPR002912; KEGG: ana:alr1890 D-3-phosphoglycerate dehydrogenase; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; Amino acid-binding ACT; PRIAM: [...] (526 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)
AFZ03077.1D-lactate dehydrogenase; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; COGs: COG1052 Lactate dehydrogenase and related dehydrogenase; InterPro IPR006139:IPR006140; KEGG: ana:alr0058 D-lactate dehydrogenase; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; PRIAM: D-lactate dehydrogenase; SPTR: D-lactate dehydrogenase. (341 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. (534 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. (364 aa)
pdxA4-hydroxythreonine-4-phosphate dehydrogenase; Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L- threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP). (352 aa)
AFZ04053.1Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP(+)); PFAM: Malic enzyme, NAD binding domain; Malic enzyme, N-terminal domain; ACT domain; COGs: COG0281 Malic enzyme; InterPro IPR012302:IPR002912:IPR012301; KEGG: npu:Npun_F1023 malic enzyme, NAD-binding; PFAM: Malic enzyme, NAD-binding; Malic enzyme, N-terminal; Amino acid-binding ACT; PRIAM: Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP(+)); SMART: Malic enzyme, NAD-binding; SPTR: Malic enzyme, NAD-binding. (463 aa)
ilvEBranched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (304 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 2 subfamily. (556 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
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.