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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
EKF05098.1Acetolactate synthase, small subunit; KEGG: ava:Ava_2035 9.6e-83 ilvH; acetolactate synthase 3 regulatory subunit K01653. (182 aa)    
Predicted Functional Partners:
EKF05783.1
Acetolactate synthase; KEGG: ana:all3555 9.1e-277 ilvB; acetolactate synthase; K01652 acetolactate synthase I/II/III large subunit; Psort location: Cytoplasmic, score: 9.97; Belongs to the TPP enzyme family.
 0.999
EKF00103.1
KEGG: npu:Npun_R1735 0. acetolactate synthase, large subunit, biosynthetic type K01652; Psort location: Cytoplasmic, score: 9.97.
 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.
 
 
 0.998
EKE97064.1
KEGG: cyc:PCC7424_4704 1.6e-233 thiamine pyrophosphate protein TPP binding domain protein; K01576 benzoylformate decarboxylase; Psort location: Cytoplasmic, score: 9.97; Belongs to the TPP enzyme family.
 
 0.996
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.
 
 0.995
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.
 
 
 0.968
EKF02719.1
KEGG: npu:Npun_F4065 1.5e-265 2-isopropylmalate synthase/homocitrate synthase family protein K01649; Psort location: Cytoplasmic, score: 8.96; Belongs to the alpha-IPM synthase/homocitrate synthase family.
 
 
 0.967
ilvA
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.
 
 0.965
ilvD-2
KEGG: npu:Npun_R3783 3.2e-274 dihydroxy-acid dehydratase K01687; Belongs to the IlvD/Edd family.
 
 
 0.961
ilvD
KEGG: ava:Ava_0023 1.7e-268 dihydroxy-acid dehydratase K01687; Psort location: Cytoplasmic, score: 8.96; Belongs to the IlvD/Edd family.
 
 
 0.960
Your Current Organism:
Tolypothrix sp. PCC7601
NCBI taxonomy Id: 1188
Other names: Calothrix sp. PCC 7601, Fremyella diplosiphon ACMM 396, Fremyella diplosiphon IAM M-100, Fremyella diplosiphon UTEX B 481, Microchaete diplosiphon UTEX B 481, T. sp. PCC 7601, Tolypothrix (Calothrix) sp. PCC 7601, Tolypothrix sp. PCC 7601, Tolypothrix sp. PCC 7601 = UTEX B 481
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