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uppP uppP Smed_1135 Smed_1135 mraY mraY Smed_3535 Smed_3535 Smed_3533 Smed_3533 queG queG queA queA tgt tgt rsmA rsmA glmU glmU pheT pheT
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query proteins and first shell of interactors
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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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experimentally determined
Predicted Interactions
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textmining
co-expression
protein homology
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uppPPutative undecaprenol kinase; Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin; Belongs to the UppP family. (268 aa)    
Predicted Functional Partners:
Smed_1135
Undecaprenyl diphosphate synthase; Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
     
 0.934
mraY
phospho-N-acetylmuramoyl-pentapeptide- transferase; First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan; Belongs to the glycosyltransferase 4 family. MraY subfamily.
    
 0.924
Smed_3535
PFAM: Glutathione S-transferase domain; KEGG: sme:SMc00407 putative glutathione S-transferase protein.
       0.577
Smed_3533
PFAM: NAD-dependent epimerase/dehydratase; 3-beta hydroxysteroid dehydrogenase/isomerase; KEGG: sme:SMc00405 hypothetical protein.
       0.573
queG
Domain of unknown function DUF1730; 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.
       0.573
queA
Queuosine biosynthesis protein; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
 
   
 0.512
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 [...]
 
     0.496
rsmA
Dimethyladenosine transferase; 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.
  
  
 0.445
glmU
Nucleotidyl transferase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belongs to the transferase hexapeptide repeat family.
     
 0.444
pheT
TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: sme:SMc00366 probable phenylalanyl-tRNA synthetase beta chain protein; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
     
 0.429
Your Current Organism:
Sinorhizobium medicae
NCBI taxonomy Id: 366394
Other names: Ensifer medicae WSM419, S. medicae WSM419, Sinorhizobium medicae WSM419
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