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
Lbys_3207KEGG: bth:BT_0768 hypothetical protein; SPTR: Para-aminobenzoate synthase component I; PFAM: Aminotransferase class IV. (206 aa)    
Predicted Functional Partners:
Lbys_3208
Chorismate binding protein; COGs: COG0147 Anthranilate/para-aminobenzoate synthase component I; InterPro IPR015890; KEGG: bth:BT_0767 para-aminobenzoate synthase component I; PFAM: Chorismate binding-like; SPTR: Putative para-aminobenzoate synthase component I; PFAM: chorismate binding enzyme.
 
 
 0.995
Lbys_1609
COGs: COG0294 Dihydropteroate synthase; InterPro IPR000489:IPR006390; KEGG: fjo:Fjoh_3497 dihydropteroate synthase; PFAM: dihydropteroate synthase DHPS; PRIAM: Dihydropteroate synthase; SPTR: Putative dihydropteroate synthase; TIGRFAM: dihydropteroate synthase; PFAM: Pterin binding enzyme; TIGRFAM: dihydropteroate synthase.
  
 
 0.922
gcvP
Glycine dehydrogenase (decarboxylating) beta subunit; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
  
  
 0.842
Lbys_0631
COGs: COG0527 Aspartokinase; InterProIPR018042:IPR019811:IPR011147:IPR001048:IPR 002912:IPR005106:IPR001342:IPR001341; KEGG: sli:Slin_4514 aspartate kinase; PFAM: homoserine dehydrogenase; aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; homoserine dehydrogenase NAD-binding; PRIAM: Aspartate kinase., Homoserine dehydrogenase; SPTR: Aspartate kinase; TIGRFAM: aspartate kinase; PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain; Amino acid kinase family; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase.
  
  
 0.640
ilvD
COGs: COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; InterPro IPR020558:IPR004404:IPR000581; KEGG: dfe:Dfer_3684 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.
  
 
 0.625
Lbys_3304
COGs: COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; InterPro IPR000581; KEGG: dfe:Dfer_4563 dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; PRIAM: Dihydroxy-acid dehydratase; SPTR: Dihydroxy-acid dehydratase; PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.
  
 
 0.625
Lbys_2274
Acetolactate synthase, large subunit, biosynthetic type; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterProIPR000399:IPR001917:IPR012846:IPR012001:IPR 012000:IPR011766; KEGG: dfe:Dfer_3681 acetolactate synthase, large subunit, biosynthetic type; 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 doma [...]
  
 
 0.560
Lbys_3210
Peptidase M28; COGs: COG2234 aminopeptidase; InterPro IPR018247:IPR007484; KEGG: dfe:Dfer_3397 peptidase M28; PFAM: peptidase M28; SPTR: Peptidase M28; PFAM: PA domain; Peptidase family M28.
       0.541
Lbys_0057
Chorismate mutase; COGs: COG0077 Prephenate dehydratase; InterProIPR018528:IPR010957:IPR020822:IPR001086:IPR 008242:IPR002701; KEGG: sli:Slin_2566 chorismate mutase; PFAM: prephenate dehydratase; Chorismate mutase, type II; SPTR: Chorismate mutase; TIGRFAM: chorismate mutase; PFAM: Prephenate dehydratase; Chorismate mutase type II; TIGRFAM: chorismate mutase domain of proteobacterial P-protein, clade 2.
 
   
 0.536
Lbys_2027
2-isopropylmalate synthase; COGs: COG0119 Isopropylmalate/homocitrate/citramalate synthase; InterPro IPR002034:IPR000891; KEGG: sli:Slin_5897 pyruvate carboxyltransferase; PFAM: pyruvate carboxyltransferase; SPTR: Pyruvate carboxyltransferase; PFAM: HMGL-like; Belongs to the alpha-IPM synthase/homocitrate synthase family.
  
 
 0.528
Your Current Organism:
Leadbetterella byssophila
NCBI taxonomy Id: 649349
Other names: L. byssophila DSM 17132, Leadbetterella byssophila 4M15, Leadbetterella byssophila DSM 17132, Leadbetterella byssophila str. DSM 17132, Leadbetterella byssophila strain DSM 17132
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