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
Your Input:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
ADR21626.1COGs: COG0440 Acetolactate synthase small (regulatory) subunit; InterPro IPR002912: IPR019455: IPR004789; KEGG: fps:FP0447 acetolactate synthase small subunit; PFAM: amino acid-binding ACT domain protein; Acetolactate synthase, small subunit-like; SPTR: Acetohydroxyacid synthase small subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: ACT domain; Small subunit of acetolactate synthase; TIGRFAM: acetolactate synthase, small subunit. (177 aa)    
Predicted Functional Partners:
ADR21627.1
Acetolactate synthase, large subunit, biosynthetic type; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterProIPR012001: IPR012000: IPR011766: IPR000399: IPR 012846; KEGG: zpr:ZPR_2802 acetolactate synthase large subunit; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; SPTR: Acetolactate synthase; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate [...]
 0.999
ADR21625.1
COGs: COG0059 Ketol-acid reductoisomerase; InterPro IPR013116: IPR000506: IPR013023; KEGG: dfe:Dfer_3679 ketol-acid reductoisomerase; PFAM: Acetohydroxy acid isomeroreductase catalytic domain-containing protein; acetohydroxy acid isomeroreductase; SPTR: Ketol-acid reductoisomerase; TIGRFAM: ketol-acid reductoisomerase; PFAM: Acetohydroxy acid isomeroreductase, catalytic domain; TIGRFAM: ketol-acid reductoisomerase.
 
 
 0.997
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.
 
 0.988
ilvA
Threonine dehydratase; 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.
 
 
 0.968
ilvD
COGs: COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; InterPro IPR000581: IPR020558: IPR004404; KEGG: rbi:RB2501_14414 dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; PRIAM: Dihydroxy-acid dehydratase; SPTR: Dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.
 
 
 0.968
ADR21634.1
Pyruvate carboxyltransferase; COGs: COG0119 Isopropylmalate/homocitrate/citramalate synthase; InterPro IPR000891: IPR002034; KEGG: rbi:RB2501_15799 2-isopropylmalate synthase; PFAM: pyruvate carboxyltransferase; SPTR: Putative 2-isopropylmalate synthase 1; PFAM: HMGL-like; Belongs to the alpha-IPM synthase/homocitrate synthase family.
 
 
 0.960
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.
 
  
 0.898
leuC
3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 
  
 0.891
ADR23309.1
COGs: COG0281 Malic enzyme; InterPro IPR012301: IPR012302: IPR002505: IPR012188; KEGG: chu:CHU_0027 malic enzyme; PFAM: malic protein NAD-binding; malic protein domain protein; phosphate acetyl/butaryl transferase; SPTR: NADP-dependent malate dehydrogenase; PFAM: Phosphate acetyl/butaryl transferase; Malic enzyme, NAD binding domain; Malic enzyme, N-terminal domain; TIGRFAM: phosphate acetyltransferase.
  
 0.864
ADR20886.1
Transketolase central region; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
   
 
  0.835
Your Current Organism:
Marivirga tractuosa
NCBI taxonomy Id: 643867
Other names: Flexibacter tractuosus DSM 4126, Flexibacter tractuosus IFO 15989, M. tractuosa DSM 4126, Marivirga tractuosa DSM 4126, Marivirga tractuosa IFO 15989, Marivirga tractuosa str. DSM 4126, Marivirga tractuosa strain DSM 4126
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