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UniProt functional annotation for P0A6K3 | ||
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| UniProt code: P0A6K3. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
Removes the formyl group from the N-terminal Met of newly synthesized proteins (PubMed:7896716). Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. {ECO:0000269|PubMed:7896716, ECO:0000269|PubMed:9610360, ECO:0000305|PubMed:8244948}. |
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| Catalytic activity: | |
Reaction=H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N- terminal L-methionyl-[peptide]; Xref=Rhea:RHEA:24420, Rhea:RHEA- COMP:10639, Rhea:RHEA-COMP:10640, ChEBI:CHEBI:15377, ChEBI:CHEBI:15740, ChEBI:CHEBI:49298, ChEBI:CHEBI:64731; EC=3.5.1.88; |
| Cofactor: | |
Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:9610360}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:8244948, ECO:0000305|PubMed:7896716}; Note=Upon overproduction is isolated with 1 Fe(2+) ion per monomer, a Ni(2+)-bound form is as active while a Zn(2+)-bound form is inactive (PubMed:9610360). {ECO:0000269|PubMed:9610360}; |
| Activity regulation: | |
Inhibited by 1,10-phenanthroline. {ECO:0000269|PubMed:7896716}. |
| Subunit: | |
Monomer. |
| Mass spectrometry: | |
Mass=19175; Mass_error=50; Method=MALDI; Evidence={ECO:0000269|PubMed:8244948}; |
| Similarity: | |
Belongs to the polypeptide deformylase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.