ID A0A200HN15_9ENTE Unreviewed; 163 AA. AC A0A200HN15; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 22-FEB-2023, entry version 12. DE RecName: Full=Peptide deformylase {ECO:0000256|HAMAP-Rule:MF_00163}; DE Short=PDF {ECO:0000256|HAMAP-Rule:MF_00163}; DE EC=3.5.1.88 {ECO:0000256|HAMAP-Rule:MF_00163}; DE AltName: Full=Polypeptide deformylase {ECO:0000256|HAMAP-Rule:MF_00163}; GN Name=def {ECO:0000256|HAMAP-Rule:MF_00163}; GN ORFNames=A5868_003748 {ECO:0000313|EMBL:OUZ13545.1}; OS Enterococcus sp. 12F9_DIV0723. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1834169 {ECO:0000313|EMBL:OUZ13545.1, ECO:0000313|Proteomes:UP000195774}; RN [1] {ECO:0000313|EMBL:OUZ13545.1, ECO:0000313|Proteomes:UP000195774} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12F9_DIV0723 {ECO:0000313|EMBL:OUZ13545.1, RC ECO:0000313|Proteomes:UP000195774}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genomic Center for Infectious Diseases; RA Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P., RA Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Enterococcus sp. 12F9_DIV0723."; RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Removes the formyl group from the N-terminal Met of newly CC synthesized proteins. Requires at least a dipeptide for an efficient CC rate of reaction. N-terminal L-methionine is a prerequisite for CC activity but the enzyme has broad specificity at other positions. CC {ECO:0000256|HAMAP-Rule:MF_00163}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N- CC terminal L-methionyl-[peptide]; Xref=Rhea:RHEA:24420, Rhea:RHEA- CC COMP:10639, Rhea:RHEA-COMP:10640, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15740, ChEBI:CHEBI:49298, ChEBI:CHEBI:64731; EC=3.5.1.88; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00163}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00163}; CC Note=Binds 1 Fe(2+) ion. {ECO:0000256|HAMAP-Rule:MF_00163}; CC -!- SIMILARITY: Belongs to the polypeptide deformylase family. CC {ECO:0000256|ARBA:ARBA00010759, ECO:0000256|HAMAP-Rule:MF_00163}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OUZ13545.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NIBK01000003; OUZ13545.1; -; Genomic_DNA. DR AlphaFoldDB; A0A200HN15; -. DR EnsemblBacteria; OUZ13545; OUZ13545; A5868_003748. DR Proteomes; UP000195774; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042586; F:peptide deformylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule. DR CDD; cd00487; Pep_deformylase; 1. DR Gene3D; 3.90.45.10; Peptide deformylase; 1. DR HAMAP; MF_00163; Pep_deformylase; 1. DR InterPro; IPR023635; Peptide_deformylase. DR InterPro; IPR036821; Peptide_deformylase_sf. DR PANTHER; PTHR10458; PEPTIDE DEFORMYLASE; 1. DR PANTHER; PTHR10458:SF22; PEPTIDE DEFORMYLASE; 1. DR Pfam; PF01327; Pep_deformylase; 1. DR PIRSF; PIRSF004749; Pep_def; 1. DR PRINTS; PR01576; PDEFORMYLASE. DR SUPFAM; SSF56420; Peptide deformylase; 1. DR TIGRFAMs; TIGR00079; pept_deformyl; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00163}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00163}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00163}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00163}. FT ACT_SITE 131 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00163" FT BINDING 88 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00163" FT BINDING 130 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00163" FT BINDING 134 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00163" SQ SEQUENCE 163 AA; 18691 MW; 5D45A582E6677667 CRC64; MRYPIIIHPD DRLLKKAAPI EYITDEIVTL LDDMYETMVA HDGIGLAAPQ IGKNLRIAVV EVDEGDRFDF INPEIIERKG TSIDVEGCLS IPETYGTVAR ADEVTVRYYD REGSEMEVTA YGYLARAFQH EIDHLDGKLF IDQVIEKIEP EDLERYMEEH VDD //