STRINGSTRING
rlmN rlmN rsmB rsmB ACS40887.1 ACS40887.1 miaB miaB yggW yggW moaA moaA queE queE bioB bioB ACS40670.1 ACS40670.1 aroB aroB pqqE pqqE
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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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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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rlmNPutative Fe-S containing enzyme (yfgB); Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. (425 aa)    
Predicted Functional Partners:
rsmB
16S rRNA m5C967 methyltransferase, S-adenosyl-L-methionine-dependent; Function of strongly homologous gene; enzyme; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
  
  
 0.791
ACS40887.1
Putative SUN-family protein, RNA methyltransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
  
  
 0.791
miaB
tRNA modification enzyme MiaB, putative isopentenyl-adenosine A37 tRNA methylthiolase; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
 
  
 0.777
yggW
Putative oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family.
 
   
 0.757
moaA
Molybdenum biosynthetic protein A; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate.
     
 0.749
queE
Conserved hypothetical protein; 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.
      
 0.745
bioB
Biotin synthetase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.
      
 0.737
ACS40670.1
MiaB-like tRNA modifying enzyme, putative 2-methylthioadenine synthetase; Function of strongly homologous gene; enzyme.
 
  
 0.723
aroB
Bifunctional shikimate kinase (N-terminal) / dehydroquinate synthase (C-terminal) enzyme; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ); Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
 
     0.717
pqqE
Pyrroloquinoline quinone (PQQ) biosynthesis protein E; Catalyzes the cross-linking of a glutamate residue and a tyrosine residue in the PqqA protein as part of the biosynthesis of pyrroloquinoline quinone (PQQ).
      
 0.696
Your Current Organism:
Methylorubrum extorquens
NCBI taxonomy Id: 272630
Other names: M. extorquens AM1, Methylobacterium extorquens AM1, Methylorubrum extorquens AM1, Pseudomonas sp. AM1
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