xthA protein (Escherichia coli K12 DH10B) - STRING interaction network
"xthA" - Exonuclease III in Escherichia coli K12 DH10B
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Predicted Interactions
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Gene Fusion
xthAExonuclease III; Major apurinic-apyrimidinic endonuclease of E.coli. It removes the damaged DNA at cytosines and guanines by cleaving on the 3’-side of the AP site by a beta-elimination reaction. It exhibits 3’-5’-exonuclease, 3’-phosphomonoesterase, 3’-repair diesterase and ribonuclease H activities (268 aa)    
Predicted Functional Partners:
Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N- glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3’ to the AP site by a beta-elimination, leaving a 3’-terminal unsaturated sugar and a product with a terminal 5’-phosphate (211 aa)
DNA polymerase III subunit beta; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3’ to 5’ exonuclease activity. The beta chain is required for initiation of replication; once it is clamped onto DNA it slides freely (bidirectional and ATP- independent) along duplex DNA. Coordinates protein traffic at the replication fork, where it interacts with multiple DNA polymerases (366 aa)
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3’ to 5’ and 5’ to 3’ exonuclease activity. It is able to utilize nicked circular duplex DNA as a template and can unwind the parental DNA strand from its template (928 aa)
Adenine DNA glycosylase; Adenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past GO lesions which are due to the oxidatively damaged form of guanine- 7,8-dihydro-8- oxoguanine (8-oxo-dGTP) (350 aa)
Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5’-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin (285 aa)
Ribonucleotide-diphosphate reductase subunit alpha; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1 contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. It also provides redox- active cysteines (761 aa)
Imidazole glycerol-phosphate dehydratase/histidinol phosphatase (355 aa)
3-methyladenine DNA glycosylase; Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, 3-methylguanine, 7-methylguanine, O2- methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions (282 aa)
uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine (229 aa)
Anaerobic class I fumarate hydratase; Catalyzes the reversible hydration of fumarate to (S)- malate. Functions in the generation of fumarate for use as an anaerobic electron acceptor. To a lesser extent, also displays D- tartrate dehydratase activity, but is not able to convert (R)- malate, L-tartrate or meso-tartrate. Is required for anaerobic growth on D-tartrate (548 aa)
Your Current Organism:
Escherichia coli K12 DH10B
NCBI taxonomy Id: 316385
Other names: E. coli str. K-12 substr. DH10B, Escherichia coli DH10B, Escherichia coli K12 DH10B, Escherichia coli str. K-12 substr. DH10B, Escherichia coli str. K12 substr. DH10B, Escherichia coli strain K12 substrain DH10B
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