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
ipk4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase; Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. (294 aa)    
Predicted Functional Partners:
ispD
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
 
  
 0.984
ispF
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; 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).
 
 
 0.984
rsmA
16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))- dimethyltransferase; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
 
  
 0.870
APC02086.1
Hypothetical protein; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
  
    0.835
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.
 
   
 0.832
ispH
4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. Belongs to the IspH family.
 
   
 0.825
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.
  
   
 0.702
APC02084.1
A/G-specific adenine glycosylase; Adenine glycosylase active on G-A mispairs.
  
    0.657
tadA
tRNA-specific adenosine deaminase; Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2); Belongs to the cytidine and deoxycytidylate deaminase family.
      0.627
mutM
formamidopyrimidine-DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
       0.616
Your Current Organism:
Polynucleobacter asymbioticus
NCBI taxonomy Id: 576611
Other names: Burkholderiaceae bacterium KF022, Burkholderiaceae bacterium KF023, Burkholderiaceae bacterium KF032, Burkholderiaceae bacterium KF040, Burkholderiaceae bacterium KF041, Burkholderiaceae bacterium KF042, Burkholderiaceae bacterium KF043, Burkholderiaceae bacterium KF046, Burkholderiaceae bacterium KF047, Burkholderiaceae bacterium KF069, Burkholderiaceae bacterium KF071, Burkholderiaceae bacterium KF072, CIP 109841, DSM 18221, P. asymbioticus, Polynucleobacter asymbioticus (Hahn et al. 2009) Hahn et al. 2016, Polynucleobacter necessarius subsp. asymbioticus, Polynucleobacter necessarius subsp. asymbioticus Hahn et al. 2009, Polynucleobacter sp. INAWF005, Polynucleobacter sp. INAWF006, Polynucleobacter sp. INAWF008, Polynucleobacter sp. INAWF009, Polynucleobacter sp. INAWF010, Polynucleobacter sp. INAWF011, Polynucleobacter sp. INAWF012, Polynucleobacter sp. INBF001, Polynucleobacter sp. MWH-Creno-4A3, Polynucleobacter sp. MWH-Creno-4D65, Polynucleobacter sp. MWH-Mekk-C4, Polynucleobacter sp. MWH-Mekk-D4, Polynucleobacter sp. MWH-NZ4W7a, Polynucleobacter sp. MWH-P1sevC1, Polynucleobacter sp. P1-KOL8, Polynucleobacter sp. QLW-P1DMWA-2, Polynucleobacter sp. QLW-P1DNSYA-1, Polynucleobacter sp. QLW-P1DNSYA-2, Polynucleobacter sp. QLW-P1FAT50D-2, Polynucleobacter sp. QLW-P1FMW50A-1, Polynucleobacter sp. QLW-P1FNSY20A-6, Polynucleobacter sp. SHIRF001, Polynucleobacter sp. SHIRF002, Polynucleobacter sp. SHIRF003, Polynucleobacter sp. SHIRF004, Polynucleobacter sp. SHIRF005, Polynucleobacter sp. SHIRF006, Polynucleobacter sp. SHIRF007, Polynucleobacter sp. SHIRF008, Polynucleobacter sp. SHIRF009, Polynucleobacter sp. SHIRF010, Polynucleobacter sp. SHIRF011, Polynucleobacter sp. SHIRF012, Polynucleobacter sp. SHIRF013, Polynucleobacter sp. SHIRF014, Polynucleobacter sp. SHIRF015, Polynucleobacter sp. SHIRF016, Polynucleobacter sp. SHIRF017, Polynucleobacter sp. SHIRF018, Polynucleobacter sp. SHIRF019, Polynucleobacter sp. SUWAF015, Polynucleobacter sp. SUWAF016, Polynucleobacter sp. TEGAF008, Polynucleobacter sp. TEGF001, Polynucleobacter sp. UF003, Polynucleobacter sp. UF009, Polynucleobacter sp. USHIF002, Polynucleobacter sp. USHIF003, Polynucleobacter sp. USHIF004, Polynucleobacter sp. USHIF007, Polynucleobacter sp. USHIF009, Polynucleobacter sp. USHIF010, Polynucleobacter sp. USHIF011, Polynucleobacter sp. USHIF012, beta proteobacterium MWH-HuK1, beta proteobacterium MWH-T1W11, strain QLW-P1DMWA-1
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