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
queFNADPH-dependent 7-cyano-7-deazaguanine reductase QueF; Catalyzes the NADPH-dependent reduction of 7-cyano-7- deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). (275 aa)    
Predicted Functional Partners:
queC
7-cyano-7-deazaguanine synthase; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). Belongs to the QueC family.
 
 
 0.986
queE
7-carboxy-7-deazaguanine synthase; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds.
 
  
 0.912
APC01608.1
6-carboxy-5,6,7,8-tetrahydropterin synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.831
APC02069.1
5'-nucleotidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
      0.821
ilvA
PLP-dependent threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
       0.755
APC02331.1
Hypothetical protein; Involved in the import of queuosine (Q) precursors, required for Q precursor salvage; Belongs to the vitamin uptake transporter (VUT/ECF) (TC 2.A.88) family. Q precursor transporter subfamily.
  
  
 0.752
tgt
tRNA guanosine(34) transglycosylase Tgt; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose t [...]
    
 0.745
queA
tRNA preQ1(34) S-adenosylmethionine ribosyltransferase-isomerase QueA; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
 
  
 0.634
queG
Epoxyqueuosine reductase; Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr); Belongs to the QueG family.
 
   
 0.600
ribB
3,4-dihydroxy-2-butanone-4-phosphate synthase; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; Belongs to the DHBP synthase family.
     
 0.599
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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