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
EDS75315.1KEGG: lwe:lwe2607 5.7e-42 acetyltransferase, GNAT family K00657; COG: COG0454 Histone acetyltransferase HPA2 and related acetyltransferases; Psort location: Cytoplasmic, score: 8.87. (158 aa)    
Predicted Functional Partners:
nifJ
KEGG: fnu:FN1170 0. pyruvate-flavodoxin oxidoreductase K03737; COG: COG1013 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit; Psort location: Cytoplasmic, score: 8.87.
    
  0.841
rdgB
Non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.
 
 
  
 0.711
glmS
Glutamine-fructose-6-phosphate transaminase (isomerizing); Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
  
 0.487
EDS75316.1
Hypothetical protein; KEGG: cal:orf19.5580 0.0035 TEL1; sim to putative phosphatidylinositol kinase involved in telomere length regulation K00914; Psort location: Cytoplasmic, score: 8.87.
       0.475
EDS75313.1
COG: COG1937 Uncharacterized protein conserved in bacteria; Psort location: Cytoplasmic, score: 8.87.
       0.464
EDS75314.1
Copper-exporting ATPase; KEGG: cpf:CPF_0534 2.0e-185 copper-translocating P-type ATPase K01533; COG: COG2217 Cation transport ATPase; Psort location: CytoplasmicMembrane, score: 10.00.
     
 0.464
EDS75519.1
Protein phosphatase 2C; KEGG: bsu:BG13390 1.1e-43 prpC, yloO; PP2C protein phosphatase K01090; COG: COG0631 Serine/threonine protein phosphatase; Psort location: Cytoplasmic, score: 8.87.
    
   0.447
EDS75394.1
DegT/DnrJ/EryC1/StrS aminotransferase family protein; KEGG: cno:NT01CX_1463 6.9e-101 spsC; spore coat polysaccharide biosynthesis protein SpsC K01726; COG: COG0399 Predicted pyridoxal phosphate-dependent enzyme apparently involved in regulation of cell wall biogenesis; Psort location: Cytoplasmic, score: 8.87; Belongs to the DegT/DnrJ/EryC1 family.
  
 
 0.430
gpsA
KEGG: bce:BC1505 5.7e-74 gpsA; NAD(P)H-dependent glycerol-3-phosphate dehydrogenase K00057; COG: COG0240 Glycerol-3-phosphate dehydrogenase; Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
    
   0.416
nagB
Glucosamine-6-phosphate deaminase; Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
   
 
 0.411
Your Current Organism:
Clostridium spiroforme
NCBI taxonomy Id: 428126
Other names: Clostridium spiroforme ATCC 29900, [. spiroforme DSM 1552, [Clostridium] spiroforme DSM 1552
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.