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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Slin_5913TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; Acetolactate synthase, small subunit-like; KEGG: afw:Anae109_1878 acetolactate synthase, small subunit. (177 aa)    
Predicted Functional Partners:
Slin_5912
KEGG: fph:Fphi_1550 ketol-acid reductoisomerase; TIGRFAM: ketol-acid reductoisomerase; PFAM: Acetohydroxy acid isomeroreductase catalytic domain protein; acetohydroxy acid isomeroreductase.
 
 
 0.999
Slin_5914
TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate protein TPP binding domain protein; thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; KEGG: ftn:FTN_1042 acetolactate synthase large subunit.
 0.999
Slin_6370
PFAM: thiamine pyrophosphate protein domain protein TPP-binding; thiamine pyrophosphate protein central region; thiamine pyrophosphate protein TPP binding domain protein; KEGG: sme:SM_b20095 putative pyruvate oxidase protein; Belongs to the TPP enzyme family.
 0.998
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.
 
 
 0.989
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
Slin_5900
PFAM: pyruvate carboxyltransferase; LeuA allosteric (dimerisation) domain; KEGG: mpo:Mpop_2796 2-isopropylmalate synthase; Belongs to the alpha-IPM synthase/homocitrate synthase family.
 
 
 0.974
ilvD
KEGG: pin:Ping_2151 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family.
 
 
 0.965
Slin_5897
PFAM: pyruvate carboxyltransferase; KEGG: pat:Patl_3268 2-isopropylmalate synthase; Belongs to the alpha-IPM synthase/homocitrate synthase family.
 
 
 0.961
Slin_4514
Aspartate kinase; KEGG: hypothetical protein; K00003 homoserine dehydrogenase; TIGRFAM: aspartate kinase; PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase NAD-binding; aspartate/glutamate/uridylate kinase.
  
  
 0.954
Slin_5902
3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 
  
 0.953
Your Current Organism:
Spirosoma linguale
NCBI taxonomy Id: 504472
Other names: S. linguale DSM 74, Spirosoma linguale DSM 74, Spirosoma linguale str. DSM 74, Spirosoma linguale strain DSM 74
Server load: low (26%) [HD]