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
Your Input:
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Co-expression
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[Homology]
Score
Deba_0342COGs: COG0473 Isocitrate/isopropylmalate dehydrogenase; InterPro IPR001804:IPR019818; KEGG: afu:AF0628 multifunctional 3-isopropylmalate dehydrogenase/D-malate dehydrogenase; PFAM: isocitrate/isopropylmalate dehydrogenase; PRIAM: 3-isopropylmalate dehydrogenase; SPTR: O29627 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase; TIGRFAM: isopropylmalate/isohomocitrate dehydrogenases. (330 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.
 0.998
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 1 subfamily.
 
 
 0.998
Deba_0337
COGs: COG0440 Acetolactate synthase small (regulatory) subunit; InterPro IPR002912:IPR019455:IPR004789; KEGG: pth:PTH_0528 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein; SPTR: A5D4Z3 Acetolactate synthase; TIGRFAM: acetolactate synthase, small subunit; PFAM: Small subunit of acetolactate synthase; ACT domain; TIGRFAM: acetolactate synthase, small subunit.
  
 0.992
Deba_0336
Acetolactate synthase, large subunit, biosynthetic type; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterProIPR012001:IPR012000:IPR011766:IPR012846:IPR 000399; KEGG: mtp:Mthe_0110 acetolactate synthase 3 catalytic subunit; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein domain protein TPP-binding; SPTR: A0B5D8 Acetolactate synthase; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, [...]
 
 0.975
Deba_1491
COGs: COG0372 Citrate synthase; InterProIPR002020:IPR019810:IPR016142:IPR010953:IPR 016141; KEGG: dal:Dalk_4974 citrate synthase I; PFAM: Citrate synthase; PRIAM: Citrate (Si)-synthase; SPTR: B8FDL5 Citrate synthase; TIGRFAM: citrate synthase I; PFAM: Citrate synthase; TIGRFAM: citrate synthase I (hexameric type); Belongs to the citrate synthase family.
  
 0.926
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.
 
  
 0.914
Deba_2192
Aconitate hydratase; COGs: COG1048 Aconitase A; InterProIPR001030:IPR015928:IPR015931:IPR015932:IPR 000573:IPR006250; KEGG: glo:Glov_1612 aconitate hydratase; PFAM: aconitate hydratase domain protein; SPTR: Q1NKB5 Putative aconitate hydratase; TIGRFAM: aconitate hydratase; PFAM: Aconitase C-terminal domain; Aconitase family (aconitate hydratase); TIGRFAM: aconitate hydratase, putative, Aquifex type.
 
 0.906
ilvD
COGs: COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; InterPro IPR000581:IPR004404:IPR020558; KEGG: mja:MJ1276 dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; PRIAM: Dihydroxy-acid dehydratase; SPTR: C5U5V1 Dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.
 
 
 0.896
Deba_1275
COGs: COG0538 Isocitrate dehydrogenase; InterPro IPR001804:IPR019818; KEGG: dol:Dole_1908 isocitrate dehydrogenase, NADP-dependent; PFAM: isocitrate/isopropylmalate dehydrogenase; PRIAM: Isocitrate dehydrogenase (NADP(+)); SPTR: A8ZSH5 Isocitrate dehydrogenase [NADP]; PFAM: Isocitrate/isopropylmalate dehydrogenase; TIGRFAM: isocitrate dehydrogenase, NADP-dependent, prokaryotic type.
 
0.892
sucD
succinyl-CoA synthetase, alpha subunit; 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.
  
 
 0.883
Your Current Organism:
Desulfarculus baarsii
NCBI taxonomy Id: 644282
Other names: D. baarsii DSM 2075, Desulfarculus baarsii 2st 14, Desulfarculus baarsii DSM 2075, Desulfarculus baarsii str. DSM 2075, Desulfarculus baarsii strain DSM 2075
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