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fpg protein (Pseudomonas oleovorans) - STRING interaction network
"fpg" - Formamidopyrimidine-DNA glycosylase in Pseudomonas oleovorans
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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:
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
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[Homology]
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fpgFormamidopyrimidine-DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3’- and 5’-phosphates (270 aa)    
Predicted Functional Partners:
coaE
Dephospho-CoA kinase; Catalyzes the phosphorylation of the 3’-hydroxyl group of dephosphocoenzyme A to form coenzyme A; Belongs to the CoaE family (202 aa)
 
   
  0.939
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (931 aa)
   
   
  0.905
ybeY
Endoribonuclease YbeY; Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3’ terminus of the 16S rRNA (159 aa)
 
 
  0.887
purL
Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (1281 aa)
 
   
  0.758
coaD
Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4’- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate; Belongs to the bacterial CoaD family (157 aa)
       
  0.753
JNHE01000040_gene88
annotation not available (288 aa)
   
        0.728
JNHE01000003_gene1860
annotation not available (737 aa)
 
     
  0.728
JNHE01000028_gene833
annotation not available (355 aa)
   
 
  0.691
JNHE01000040_gene86
annotation not available (192 aa)
   
        0.687
hslO
33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress (295 aa)
 
   
  0.673
Your Current Organism:
Pseudomonas oleovorans
NCBI taxonomy Id: 301
Other names: ATCC 8062, CCUG 2087, CFBP 5589, CIP 59.11, IFO 13583, JCM 11598, LMG 2229, NBRC 13583, NCIMB 6576, NCTC 10692, NRRL B-778, P. oleovorans, Pseudomonas oleovorans, Pseudomonas sp. MGY01
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