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
Deba_1359COGs: COG0498 Threonine synthase; InterPro IPR001926:IPR000634:IPR004450; KEGG: dal:Dalk_4397 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; PRIAM: Threonine synthase; SPTR: B8FNA7 Threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. (500 aa)    
Predicted Functional Partners:
Deba_1382
COGs: COG0460 Homoserine dehydrogenase; InterProIPR005106:IPR001342:IPR002912:IPR019811:IPR 016204:IPR016040; KEGG: gsu:GSU1693 homoserine dehydrogenase; PFAM: homoserine dehydrogenase; homoserine dehydrogenase NAD-binding; amino acid-binding ACT domain protein; SPTR: Q74CI0 Homoserine dehydrogenase; PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain.
  
 
 0.931
pdxA
4-hydroxythreonine-4-phosphate dehydrogenase; Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L- threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
    
 0.909
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.
  
  
 0.845
Deba_0944
COGs: COG0527 Aspartokinase; InterProIPR001057:IPR001048:IPR002912:IPR018042:IPR 001341:IPR005260; KEGG: pca:Pcar_1006 aspartate kinase; PFAM: aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; SPTR: Q3A5V0 Aspartokinase; TIGRFAM: aspartate kinase; aspartate kinase, monofunctional class; PFAM: ACT domain; Amino acid kinase family; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase; Belongs to the aspartokinase family.
  
 
 0.824
Deba_2156
Hypothetical protein; KEGG: mex:Mext_1994 beta-lactamase domain-containing protein; SPTR: A9W487 Beta-lactamase domain protein.
  
 
 0.801
Deba_1360
Thioesterase superfamily protein; InterPro IPR006683; KEGG: tye:THEYE_A0630 hypothetical protein; PFAM: thioesterase superfamily protein; SPTR: B5YJQ8 Putative uncharacterized protein; PFAM: Thioesterase superfamily; TIGRFAM: uncharacterized domain 1.
       0.789
rlmH
Protein of unknown function DUF163; Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA; Belongs to the RNA methyltransferase RlmH family.
       0.789
Deba_1152
COGs: COG0069 Glutamate synthase domain 2; InterProIPR002489:IPR000583:IPR006982:IPR002932:IPR 013785:IPR017932; KEGG: ttr:Tter_0474 glutamate synthase (ferredoxin); PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein; PRIAM: Glutamate synthase (ferredoxin); SPTR: D1CEN9 Glutamate synthase (Ferredoxin); PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II.
  
  
 0.768
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.
  
  
 0.736
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.
  
  
 0.719
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
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.