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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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queDConserved hypothetical protein; Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde. (163 aa)    
Predicted Functional Partners:
queE
Coenzyme PQQ synthesis protein III isolog (Haemophilus influenzae}; 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.
 
 
 0.998
queC
ExsB; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). Belongs to the QueC family.
 
  
 0.989
bpsA
Conserved hypothetical protein; Involved in the biosynthesis of branched-chain polyamines, which support the growth of thermophiles under high-temperature conditions. Catalyzes the sequential condensation of spermidine with the aminopropyl groups of decarboxylated S-adenosylmethionines to produce N(4)-bis(aminopropyl)spermidine via N(4)-aminopropylspermidine.
       0.956
hacB
3-isopropylmalate dehydratase (leuD); Hydro-lyase with broad substrate specificity for cis- unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4- tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4- tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1- hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)- aconitate, and even the non-physiological cis-homo(4)-aconitate with similar efficiency. These reactions are pa [...]
     
 0.793
mptA
Conserved hypothetical protein; Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate, the first intermediate in the biosynthesis of coenzyme methanopterin. It is also able to utilize a variety of GTP analogs as substrates, including GDP, beta,gamma-methylene-GTP and GTP-[gamma- thio]; Belongs to the GTP cyclohydrolase IV family.
    
 0.752
MJ_0092
Heterodisulfide reductase, subunit D (hdrD); Similar to GP:1890198 percent identity: 31.87; identified by sequence similarity; putative; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
  
    0.737
MJ_0805
Conserved hypothetical protein; Similar to PID:1419841 percent identity: 27.98; identified by sequence similarity; putative.
 
     0.736
MJ_1388
Adenosylhomocysteinase (ahcY); Catalyzes the hydrolysis of S-inosyl-L-homocysteine (SIH) to L-homocysteine (Hcy) and inosine. Likely functions in a S-adenosyl-L- methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. Can also catalyze the reverse reaction in vitro, i.e. the synthesis of SIH from Hcy and inosine. Is specific for SIH and inosine as it is unable to either hydrolyze SAH or synthesize SAH from adenosine and Hcy. Belongs to the adenosylhomocysteinase family.
   
 
 0.677
MJ_1371
Methlytransferase; Similar to GP:2437836 percent identity: 39.09; identified by sequence similarity; putative; Belongs to the MtxX family.
       0.667
tgtA
Queuine tRNA-ribosyltransferase (tgtA); Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs. Can also utilize guanine as substrate.
 
 
 
 0.662
Your Current Organism:
Methanocaldococcus jannaschii
NCBI taxonomy Id: 243232
Other names: M. jannaschii DSM 2661, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii str. DSM 2661, Methanococcus jannaschii DSM 2661
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