GCW_03600
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Uniprot: A0A0F6CLC4
Description: peptide deformylase EC number: 3.5.1.88 Annotation score: 2 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: Formyl-L-methionyl peptide + H(2)O = formate + methionyl peptide. {ECO:0000256|HAMAP-Rule:MF_00163, ECO:0000256|SAAS:SAAS00314723}. Cofactor: COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-Rule:MF_00163}; ; Note=Binds 1 Fe(2+) ion. {ECO:0000256|HAMAP-Rule:MF_00163} Enzyme regulation: Function [CC]: FUNCTION: Removes the formyl group from the N-terminal Met of newly synthesized proteins. 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:0000256|HAMAP-Rule:MF_00163}. Pathway: Active site: ACT_SITE 159 159 {ECO:0000256|HAMAP-Rule:MF_00163}. Binding site: Calcium binding: DNA binding: Metal binding: METAL 114 114 Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.; METAL 158 158 Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.; METAL 162 162 Iron. {ECO:0000256|HAMAP-Rule:MF_00163}. Nucleotide binding: Site: Gene names (primary): def Gene names (synonym): Mass: 22,869 Subunit structure [CC]: Gene ontology (GO): iron ion binding [GO:0005506]; peptide deformylase activity [GO:0042586]; translation [GO:0006412] Gene ontology IDs: GO:0005506; GO:0006412; GO:0042586 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the polypeptide deformylase family. {ECO:0000256|HAMAP-Rule:MF_00163, ECO:0000256|SAAS:SAAS00539564}. Protein families: Polypeptide deformylase family Coiled coil: Domain [FT]: Motif: Region: EMBL: CP006916 ProteinModelPortal: MEROPS: EnsemblBacteria KO: AHB99896 UniPathway: K01462 CDD: Gene3D: cd00487 HAMAP: 3.90.45.10 InterPro: MF_00163 PANTHER: IPR023635 PIRSF: PTHR10458 PRINTS: PIRSF004749 PROSITE: PR01576 Pfam: ProDom: PF01327 SMART: SUPFAM: TIGRFAMs: SSF56420 860576-861167(+) >nucleotide sequence CGTGAAGTATGTACTGAGGTAAAATTCCCCTTAAGTCAAGAAGTGCTAGATATCATCGAT AAGATGTTAGCTTATGTAGATGAAAGCTTTGATGACAATGCCGAAAAGTATGATATCCGT CCAGGGATTGGGATAGCTGCTAACCAATTAGGTTTAAATCAAAGATTTTTTTATGTTCAT TTTACTGATTTTTGTCAAAAAGAACATCGATACTTACTGATCAATCCTGAATGGATTGAT AAGAGTCTTAACAAAGCTTACTTAGCTGTTGGTGAGGGTTGTTTATCAGTTCCCAAAGAT AAAGATGGTTATGTAATTCGAAGTGAAACCGTTAAACTTAAAGGGTTCGATTACTTAACA CAAAAAGATGTTGAGATCAGTGCCCATGGATTATTAGCCATGTGCTTACAACATGAGATG GATCATTTAGAAGGTAAGTTTTATTATGATTCAATCAACATGATGAAACCATACTTTAAA AAAGATGAGTGAGTTAGCATTGATCAAAAAGTGTGTGATCAATGTAAATAA >protein sequence PGIGIAANQLGLNQRFFYVHFTDFCQKEHRYLLINPEWIDKSLNKAYLAVGEGCLSVPKD KDGYVIRSETVKLKGFDYLTQKDVEISAHGLLAMCLQHEMDHLEGKFYYDSINMMKPYFK KDEWVSIDQKVCDQCK |
© Fisunov Lab of Proteomics, 2016.