STRINGSTRING
leuB leuB leuC leuC leuD leuD Dde_0398 Dde_0398 Dde_2168 Dde_2168 Dde_2167 Dde_2167 Dde_3130 Dde_3130 Dde_0399 Dde_0399 leuA leuA sucD sucD ilvD ilvD
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
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. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily. (358 aa)    
Predicted Functional Partners:
leuC
Homoaconitate hydratase family protein; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 0.999
leuD
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 2 subfamily.
 
 0.999
Dde_0398
TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: dvl:Dvul_2624 acetolactate synthase catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP binding region; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, central region.
 
 0.980
Dde_2168
TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: dvm:DvMF_0153 acetolactate synthase, large subunit, biosynthetic type; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP binding region; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, central region.
 
 0.980
Dde_2167
KEGG: dvm:DvMF_0154 acetolactate synthase 3 regulatory subunit; TIGRFAM: Acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT.
 
 0.975
Dde_3130
KEGG: dvm:DvMF_2624 acetolactate synthase, small subunit; TIGRFAM: Acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT.
 
 0.974
Dde_0399
PFAM: Amino acid-binding ACT; KEGG: dvu:DVU0361 acetolactate synthase 1 regulatory subunit.
  
 0.969
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.
 
 
 0.967
sucD
Succinyl-CoA synthetase, alpha/beta subunit (sucCD); Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
  
 
 0.963
ilvD
TIGRFAM: Dihydroxy-acid dehydratase; KEGG: dvu:DVU3373 dihydroxy-acid dehydratase; PFAM: Dihydroxy-acid/6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family.
 
  
 0.960
Your Current Organism:
Desulfovibrio alaskensis
NCBI taxonomy Id: 207559
Other names: D. alaskensis G20, Desulfovibrio alaskensis G20, Desulfovibrio alaskensis str. G20, Desulfovibrio alaskensis strain G20, Desulfovibrio desulfuricans subsp. desulfuricans str. G20
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.