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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Score
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. (362 aa)    
Predicted Functional Partners:
leuC
3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 0.999
AFZ48224.1
3-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.
 
 
 0.997
AFZ48469.1
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: cyt:cce_0628 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein; PRIAM: Acetolactate synthase; SPTR: Acetolactate synthase small subunit; TIGRFAM: acetolactate synthase, small subunit.
 
 0.987
AFZ47101.1
Acetolactate 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; InterProIPR012846:IPR000399:IPR012001:IPR012000:IPR 011766; KEGG: cyt:cce_4478 acetolactate synthase 3 catalytic subunit; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; SPTR: A [...]
 
 0.966
AFZ47721.1
Acetolactate 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:IPR000399; KEGG: cyt:cce_4227 acetolactate synthase; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; SPTR: Acetolactate synthase large subunit.
 
 0.953
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.
 
  
 0.943
ilvD
PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; COGs: COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; InterPro IPR002114:IPR020558:IPR004404:IPR000581; KEGG: cyt:cce_4400 dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; PRIAM: Dihydroxy-acid dehydratase; SPTR: Dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.
 
  
 0.920
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.
 
 
 0.910
AFZ46499.1
2-isopropylmalate synthase; PFAM: LeuA allosteric (dimerisation) domain; HMGL-like; TIGRFAM: 2-isopropylmalate synthase/homocitrate synthase family protein; COGs: COG0119 Isopropylmalate/homocitrate/citramalate synthase; InterPro IPR000891:IPR013709:IPR002034:IPR005675; KEGG: cyc:PCC7424_3413 putative alpha-isopropylmalate/homocitrate synthase family transferase; PFAM: LeuA allosteric (dimerisation) domain-containing protein; pyruvate carboxyltransferase; SPTR: 2-isopropylmalate synthase/homocitrate synthase family protein; TIGRFAM: 2-isopropylmalate synthase/homocitrate synthase famil [...]
 
 
 0.839
AFZ46044.1
PFAM: Isocitrate/isopropylmalate dehydrogenase; TIGRFAM: isocitrate dehydrogenase, NADP-dependent, prokaryotic type; COGs: COG0538 Isocitrate dehydrogenase; InterPro IPR019818:IPR001804:IPR004439; KEGG: cyp:PCC8801_3969 isocitrate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase; SPTR: Isocitrate dehydrogenase [NADP]; TIGRFAM: isocitrate dehydrogenase, NADP-dependent.
 
 
0.738
Your Current Organism:
Cyanobacterium stanieri
NCBI taxonomy Id: 292563
Other names: C. stanieri PCC 7202, Cyanobacterium stanieri PCC 7202, Synechococcus cedrorum CCAP 14792a (no longer available), Synechococcus cedrorum CCAP 14792b (no longer available), Synechococcus cedrorum M137/1a, Synechococcus cedrorum SAG 88.79, Synechococcus sp. ATCC 29140, Synechococcus sp. PCC 7202
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