STRINGSTRING
STRING protein interaction network
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
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[Homology]
Score
AFY34715.1Acetolactate 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 [...] (630 aa)    
Predicted Functional Partners:
AFY30781.1
PFAM: ACT domain; Small subunit of acetolactate synthase; TIGRFAM: acetolactate synthase, small subunit; COGs: COG0440 Acetolactate synthase small (regulatory) subunit; InterPro IPR002912:IPR019455:IPR004789; KEGG: naz:Aazo_1096 acetolactate synthase small 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.
 0.999
ilvC
Ketol-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.
 
 
 0.994
leuB
3-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.
 0.983
AFY31054.1
PFAM: Alpha-acetolactate decarboxylase; TIGRFAM: alpha-acetolactate decarboxylase; COGs: COG3527 Alpha-acetolactate decarboxylase; InterPro IPR005128; KEGG: npu:Npun_R6050 alpha-acetolactate decarboxylase; PFAM: Alpha-acetolactate decarboxylase; PRIAM: Acetolactate decarboxylase; SPTR: Alpha-acetolactate decarboxylase; TIGRFAM: Alpha-acetolactate decarboxylase.
  
 
 0.972
ilvD
PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; COGs: COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; HAMAP: Dihydroxy-acid dehydratase; InterPro IPR000581:IPR004404; KEGG: npu:Npun_R3783 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.
  
 0.972
AFY35768.1
Pyruvate ferredoxin/flavodoxin oxidoreductase; Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin.
  
 
 0.951
ilvA
L-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.
  
 0.935
leuA
2-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.
 
 
 0.923
AFY33702.1
Acetolactate 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: 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.
  
  
 
0.919
leuA-2
2-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.
 
 
 0.897
Your Current Organism:
Calothrix sp. PCC7507
NCBI taxonomy Id: 99598
Other names: C. sp. PCC 7507, Calothrix sp. PCC 7507
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