STRINGSTRING
umpG umpG pcm pcm yfbR yfbR truD truD yjjG yjjG ushA ushA yrfG yrfG pyrH pyrH udk udk guaA guaA cmk cmk
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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
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a 3D structure is known or predicted
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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[Homology]
Score
umpGBroad specificity 5'(3')-nucleotidase and polyphosphatase; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. Also plays [...] (253 aa)    
Predicted Functional Partners:
pcm
L-isoaspartate protein carboxylmethyltransferase type II; Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. This enzyme does not act on D-aspartyl residues; Belongs to the methyltransferase superfamily. L- isoaspartyl/D-aspartyl protein methyltransferase family.
 
  
 0.995
yfbR
5'-nucleotidase; Essential component of the deoxycytidine triphosphate (dCTP) pathway for de novo synthesis of thymidylate. Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates (dAMP, dGMP, dTMP, dUMP, dIMP and dCMP) and does not dephosphorylate 5'-ribonucleotides or ribonucleoside 3'-monophosphates.
     
 0.989
truD
tRNA(Glu) pseudouridine(13) synthase; Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
 
  
 0.979
yjjG
dUMP phosphatase; Nucleotidase that shows high phosphatase activity toward non- canonical pyrimidine nucleotides and three canonical nucleoside 5'- monophosphates (UMP, dUMP, and dTMP), and very low activity against TDP, IMP, UDP, GMP, dGMP, AMP, dAMP, and 6-phosphogluconate. Appears to function as a house-cleaning nucleotidase in vivo, since the general nucleotidase activity of YjjG allows it to protect cells against non- canonical pyrimidine derivatives such as 5-fluoro-2'-deoxyuridine, 5- fluorouridine, 5-fluoroorotate, 5-fluorouracil, and 5-aza-2'- deoxycytidine, and prevents the i [...]
   
 
 0.979
ushA
Bifunctional UDP-sugar hydrolase/5'-nucleotidase; Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell.
     
 0.967
yrfG
GMP/IMP nucleotidase; Catalyzes the dephosphorylation of different purine nucleotides (GMP and IMP). Also hydrolyzes flavin mononucleotide (FMN). Belongs to the HAD-like hydrolase superfamily.
     
 0.962
pyrH
Uridylate kinase; Catalyzes the reversible phosphorylation of UMP to UDP, with ATP as the most efficient phosphate donor.
  
 
 0.961
udk
Uridine/cytidine kinase; Protein involved in nucleobase, nucleoside and nucleotide interconversion; Belongs to the uridine kinase family.
   
 
 0.961
guaA
GMP synthetase (glutamine aminotransferase); Catalyzes the synthesis of GMP from XMP.
  
 
 0.955
cmk
Cytidylate kinase; ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors. Belongs to the cytidylate kinase family. Type 1 subfamily.
  
 
 0.954
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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