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
EIJ33050.1PFAM: ACT domain; Small subunit of acetolactate synthase; TIGRFAM: acetolactate synthase, small subunit; COGs: COG0440 Acetolactate synthase small (regulatory) subunit; InterPro IPR002912:IPR019455:IPR004789; KEGG: nhl:Nhal_0656 acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT; SPTR: Acetolactate synthase, small subunit; TIGRFAM: Acetolactate synthase, small subunit. (164 aa)    
Predicted Functional Partners:
EIJ33049.1
Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterPro IPR012001:IPR012000:IPR011766:IPR012846; KEGG: tgr:Tgr7_2158 acetolactate synthase, large subunit, biosynthetic type; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP binding region; Thiamine pyrophosphate enzyme, central region; Thiamine pyro [...]
 
 0.999
EIJ33051.1
Ketol-acid reductoisomerase; PFAM: Acetohydroxy acid isomeroreductase, catalytic domain; TIGRFAM: ketol-acid reductoisomerase; COGs: COG0059 Ketol-acid reductoisomerase; HAMAP: Ketol-acid reductoisomerase; InterPro IPR013116:IPR000506:IPR013023; KEGG: hch:HCH_05914 ketol-acid reductoisomerase; PFAM: Acetohydroxy acid isomeroreductase, catalytic; Acetohydroxy acid isomeroreductase C-terminal; SPTR: Ketol-acid reductoisomerase; TIGRFAM: Acetohydroxy acid isomeroreductase.
 
 
 0.999
EIJ36170.1
Thiamine pyrophosphate TPP-binding domain-containing protein; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterPro IPR012001:IPR012000:IPR011766; KEGG: tbd:Tbd_0662 acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP binding region; Thiamine pyrophosphate enzyme, central region; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; SPTR: Acetolactate synthase la [...]
 
 0.999
ilvA
Threonine dehydratase, biosynthetic; 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.
 
 
 0.988
EIJ35222.1
PFAM: domain; Pyruvate ferredoxin/flavodoxin oxidoreductase; Transketolase, C-terminal domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; COGs: COG0674 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductase alpha subunit; InterPro IPR002880:IPR019752:IPR001450:IPR011766; KEGG: alv:Alvin_1172 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate/ketoisovalerate oxidoreductase; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Thiamine pyrophosphate [...]
  
 
 0.983
EIJ36152.1
PFAM: Isocitrate/isopropylmalate dehydrogenase; TIGRFAM: 3-isopropylmalate dehydrogenase; COGs: COG0473 Isocitrate/isopropylmalate dehydrogenase; HAMAP: Isopropylmalate dehydrogenase; InterPro IPR004429:IPR001804; KEGG: tkm:TK90_1341 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase; SPTR: 3-isopropylmalate dehydrogenase; TIGRFAM: Isopropylmalate dehydrogenase.
 
 0.963
EIJ36760.1
PFAM: Isocitrate/isopropylmalate dehydrogenase; TIGRFAM: 3-isopropylmalate dehydrogenase; COGs: COG0473 Isocitrate/isopropylmalate dehydrogenase; HAMAP: Isopropylmalate dehydrogenase; InterPro IPR004429:IPR001804; KEGG: tgr:Tgr7_1247 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase; SPTR: Putative uncharacterized protein; TIGRFAM: Isopropylmalate dehydrogenase.
 
 0.963
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.
 
 
 0.951
EIJ36551.1
PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain; COGs: COG0460 Homoserine dehydrogenase; InterPro IPR005106:IPR001342:IPR002912; KEGG: tgr:Tgr7_1439 homoserine dehydrogenase; PFAM: Homoserine dehydrogenase, catalytic; Aspartate/homoserine dehydrogenase, NAD-binding; Amino acid-binding ACT; SPTR: Homoserine dehydrogenase.
  
 
 0.939
EIJ36151.1
PFAM: Aconitase C-terminal domain; TIGRFAM: 3-isopropylmalate dehydratase, small subunit; COGs: COG0066 3-isopropylmalate dehydratase small subunit; HAMAP: 3-isopropylmalate dehydratase, small subunit region; InterPro IPR004431:IPR000573; KEGG: hna:Hneap_1718 3-isopropylmalate dehydratase, small subunit; PFAM: Aconitase A/isopropylmalate dehydratase small subunit, swivel; SPTR: 3-isopropylmalate dehydratase small subunit; TIGRFAM: 3-isopropylmalate dehydratase, small subunit region.
 
 
 0.934
Your Current Organism:
Thiothrix nivea
NCBI taxonomy Id: 870187
Other names: T. nivea DSM 5205, Thiothrix nivea DSM 5205, Thiothrix nivea JP2, Thiothrix nivea str. DSM 5205, Thiothrix nivea strain DSM 5205
Server load: medium (50%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.