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pqqE protein (Methylobacter tundripaludum) - STRING interaction network
"pqqE" - Pyrroloquinoline quinone biosynthesis protein E 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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 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
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
pqqEPyrroloquinoline quinone biosynthesis protein E (375 aa)    
Predicted Functional Partners:
pqqC
Pyrroloquinoline quinone biosynthesis protein C ; Ring cyclization and eight-electron oxidation of 3a-(2- amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline- 7,9-dicarboxylic-acid to PQQ (242 aa)
 
   
  0.997
pqqB
Pyrroloquinoline quinone biosynthesis protein B ; May be involved in the transport of PQQ or its precursor to the periplasm (303 aa)
 
   
  0.996
Mettu_3232
Coenzyme PQQ biosynthesis protein PqqD (90 aa)
 
   
  0.992
Mettu_3246
Putative transcriptional regulator, AsnC family (147 aa)
 
 
  0.901
Mettu_3247
Putative transcriptional regulator, AsnC family (184 aa)
 
 
  0.884
Mettu_3244
AsnC family transcriptional regulator (152 aa)
 
 
  0.859
Mettu_3245
Putative transcriptional regulator, AsnC family (165 aa)
 
 
  0.856
Mettu_0419
PQQ-dependent dehydrogenase, methanol/ethanol family (618 aa)
 
     
  0.836
Mettu_3041
PQQ-dependent dehydrogenase, methanol/ethanol family (604 aa)
 
     
  0.740
cysG
Siroheme synthase ; Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD- dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme (464 aa)
   
   
  0.728
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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