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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Score
Ppha_2257PFAM: domain of unknown function DUF1730; KEGG: cch:Cag_0255 iron-sulfur cluster-binding protein. (324 aa)    
Predicted Functional Partners:
Ppha_1115
methylated-DNA/protein-cysteine methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
      0.782
queA
S-adenosylmethionine/tRNA-ribosyltransferase- isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
 
  
 0.704
queA-2
S-adenosylmethionine/tRNA-ribosyltransferase- isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
 
  
 0.700
Ppha_2463
Methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
 
   
 0.567
Ppha_2878
TIGRFAM: HAD-superfamily hydrolase, subfamily IA, variant 3; beta-phosphoglucomutase family hydrolase; PFAM: Haloacid dehalogenase domain protein hydrolase; KEGG: cch:Cag_0071 beta-phosphoglucomutase hydrolase.
      0.560
Ppha_2256
PFAM: amine oxidase; Rieske [2Fe-2S] domain protein; FAD dependent oxidoreductase; KEGG: cph:Cpha266_0659 Rieske (2Fe-2S) domain protein.
       0.543
nnrD
Carbohydrate kinase, YjeF related protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow t [...]
     
 0.530
Ppha_0695
PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; pyruvate ferredoxin/flavodoxin oxidoreductase; pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; KEGG: cph:Cpha266_0571 pyruvate flavodoxin/ferredoxin oxidoreductase domain protein.
     
 0.482
queF
7-cyano-7-deazaguanine reductase; Catalyzes the NADPH-dependent reduction of 7-cyano-7- deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). Belongs to the GTP cyclohydrolase I family. QueF type 1 subfamily.
 
   
 0.459
tgt
Queuine tRNA-ribosyltransferase; 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 to form t [...]
 
  
 0.417
Your Current Organism:
Pelodictyon phaeoclathratiforme
NCBI taxonomy Id: 324925
Other names: P. phaeoclathratiforme BU-1, Pelodictyon phaeoclathratiforme BU-1, Pelodictyon phaeoclathratiforme DSM 5477, Pelodictyon phaeoclathratiforme str. BU-1, Pelodictyon phaeoclathratiforme strain BU-1
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