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Mettu_1266 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_1266" - KEGG: gur:Gura_4090 radical SAM domain-containing protein in Methylobacter tundripaludum
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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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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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Mettu_1266KEGG- gur-Gura_4090 radical SAM domain-containing protein; PFAM- Radical SAM; Cobalamin (vitamin B12)-binding; SMART- Elongator protein 3/MiaB/NifB (524 aa)    
Predicted Functional Partners:
hemE
Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III (355 aa)
         
  0.976
Mettu_0723
KEGG- gca-Galf_1632 uroporphyrinogen decarboxylase (URO-D) (342 aa)
   
   
  0.966
Mettu_1268
annotation not available (62 aa)
              0.837
Mettu_1267
PFAM- Protein of unknown function DUF115 (341 aa)
              0.837
rlmL
Ribosomal RNA large subunit methyltransferase K/L; Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA; Belongs to the methyltransferase superfamily. RlmKL family (774 aa)
   
   
  0.666
metK
S-adenosylmethionine synthase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme (386 aa)
       
    0.607
Mettu_2540
KEGG- mca-MCA2793 delta-aminolevulinic acid dehydratase; PFAM- Tetrapyrrole biosynthesis, porphobilinogen synthase; Belongs to the ALAD family (334 aa)
         
  0.523
Mettu_2437
PFAM- Tetrapyrrole biosynthesis, uroporphyrinogen III synthase; KEGG- nhl-Nhal_3935 uroporphyrinogen III synthase HEM4 (256 aa)
     
 
    0.508
ubiA
4-hydroxybenzoate octaprenyltransferase; Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3- octaprenyl-4-hydroxybenzoate (289 aa)
       
  0.497
Mettu_0710
TIGRFAM- Hopene cyclase; Squalene cyclase; KEGG- mca-MCA0812 squalene-hopene cyclase; PFAM- Prenyltransferase/squalene oxidase (651 aa)
 
     
  0.459
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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