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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
ispE4-diphosphocytidyl-2-C-methyl-D- erythritolkinase; Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. (302 aa)    
Predicted Functional Partners:
ispF
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2- C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
 
 
 0.985
AEJ62202.1
PFAM: Uncharacterized protein family UPF0007; TIGRFAM: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; COGs: COG1211 4-diphosphocytidyl-2-methyl-D-erithritol synthase; InterPro IPR001228; KEGG: sta:STHERM_c18980 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; PFAM: 4-diphosphocytidyl-2C-methyl-D-erythritol synthase; SPTR: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.
 
  
 0.983
dxr
1-deoxy-D-xylulose 5-phosphate reductoisomerase; Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- phosphate (MEP); Belongs to the DXR family.
 
   
 0.836
AEJ62044.1
PFAM: LytB protein; TIGRFAM: (E)-4-hydroxy-3-methyl-but-2-enyl pyrophosphate reductase (IPP and DMAPP forming); COGs: COG0761 Penicillin tolerance protein; InterPro IPR003451; KEGG: sta:STHERM_c17130 4-hydroxy-3-methylbut-2-enyl diphosphate reductase; PFAM: LytB protein; SPTR: Hydroxymethylbutenyl pyrophosphate reductase; TIGRFAM: LytB protein.
 
  
 0.827
ispG
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family.
 
  
 0.807
AEJ61336.1
L-aspartate oxidase; Catalyzes the oxidation of L-aspartate to iminoaspartate.
       0.786
AEJ61335.1
Nicotinate-nucleotide pyrophosphorylase; PFAM: Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl transferase, N-terminal domain; TIGRFAM: nicotinate-nucleotide pyrophosphorylase; COGs: COG0157 Nicotinate-nucleotide pyrophosphorylase; InterPro IPR002638:IPR004393; KEGG: sta:STHERM_c10350 hypothetical protein; PFAM: Quinolinate phosphoribosyl transferase; SPTR: Nicotinate-nucleotide pyrophosphorylase; TIGRFAM: Nicotinate-nucleotide pyrophosphorylase; Belongs to the NadC/ModD family.
       0.782
spoVG
Septation protein spoVG; Could be involved in septation.
       0.698
dxs
1-deoxy-D-xylulose-5-phosphate synthase; Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D- xylulose-5-phosphate (DXP); Belongs to the transketolase family. DXPS subfamily.
 
   
 0.679
pcm
Protein-L-isoaspartate O-methyltransferase; Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
   
    0.655
Your Current Organism:
Spirochaeta thermophila
NCBI taxonomy Id: 869211
Other names: S. thermophila DSM 6578, Spirochaeta thermophila DSM 6578, Spirochaeta thermophila str. DSM 6578, Spirochaeta thermophila strain DSM 6578
Server load: low (10%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.