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UniProt functional annotation for P69925 | ||
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| UniProt code: P69925. |
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| Organism: | |
Escherichia coli O157:H7. |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2 contains the tyrosyl radical required for catalysis. |
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| Catalytic activity: | |
Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'- diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'- diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA- COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10014}; |
| Cofactor: | |
Name=Fe cation; Xref=ChEBI:CHEBI:24875; Note=Binds 2 iron ions per subunit.; |
| Pathway: | |
Genetic information processing; DNA replication. |
| Subunit: | |
Tetramer of two alpha (R1) and two beta (R2) subunits. The B1 protein is a dimer of alpha subunits. A radical transfer pathway occurs between Tyr-123 of R2 and R1 (By similarity). {ECO:0000250}. |
| Miscellaneous: | |
E.coli produces two separate class I enzymes. This one is the functional enzyme during growth. |
| Miscellaneous: | |
A substrate-binding catalytic site, located on R1, is formed only in the presence of the second subunit R2. {ECO:0000250}. |
| Similarity: | |
Belongs to the ribonucleoside diphosphate reductase small chain family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.