ID DEF_STRMU Reviewed; 204 AA. AC Q8DWC2; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 115. DE RecName: Full=Peptide deformylase {ECO:0000255|HAMAP-Rule:MF_00163}; DE Short=PDF {ECO:0000255|HAMAP-Rule:MF_00163}; DE EC=3.5.1.88 {ECO:0000255|HAMAP-Rule:MF_00163}; DE AltName: Full=Polypeptide deformylase {ECO:0000255|HAMAP-Rule:MF_00163}; GN Name=def {ECO:0000255|HAMAP-Rule:MF_00163}; GN OrderedLocusNames=SMU_143c; OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=210007; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700610 / UA159; RX PubMed=12397186; DOI=10.1073/pnas.172501299; RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.; RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental RT pathogen."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002). 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:0000255|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:0000255|HAMAP-Rule:MF_00163}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00163}; CC Note=Binds 1 Fe(2+) ion. {ECO:0000255|HAMAP-Rule:MF_00163}; CC -!- SIMILARITY: Belongs to the polypeptide deformylase family. CC {ECO:0000255|HAMAP-Rule:MF_00163}. 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; AE014133; AAN57921.1; -; Genomic_DNA. DR RefSeq; NP_720615.1; NC_004350.2. DR RefSeq; WP_002263599.1; NC_004350.2. DR PDB; 3L87; X-ray; 2.00 A; A=1-204. DR PDBsum; 3L87; -. DR AlphaFoldDB; Q8DWC2; -. DR SMR; Q8DWC2; -. DR STRING; 210007.SMU_143c; -. DR GeneID; 66818368; -. DR KEGG; smu:SMU_143c; -. DR PATRIC; fig|210007.7.peg.122; -. DR eggNOG; COG0242; Bacteria. DR HOGENOM; CLU_061901_4_0_9; -. DR OrthoDB; 9784988at2; -. DR PhylomeDB; Q8DWC2; -. DR Proteomes; UP000002512; Chromosome. 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 NCBIfam; TIGR00079; pept_deformyl; 1. DR PANTHER; PTHR10458; PEPTIDE DEFORMYLASE; 1. DR PANTHER; PTHR10458:SF8; 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. PE 1: Evidence at protein level; KW 3D-structure; Hydrolase; Iron; Metal-binding; Protein biosynthesis; KW Reference proteome. FT CHAIN 1..204 FT /note="Peptide deformylase" FT /id="PRO_0000082856" FT ACT_SITE 175 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00163" FT BINDING 131 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00163" FT BINDING 174 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00163" FT BINDING 178 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00163" FT HELIX 3..7 FT /evidence="ECO:0007829|PDB:3L87" FT HELIX 25..27 FT /evidence="ECO:0007829|PDB:3L87" FT HELIX 40..57 FT /evidence="ECO:0007829|PDB:3L87" FT HELIX 59..65 FT /evidence="ECO:0007829|PDB:3L87" FT STRAND 71..74 FT /evidence="ECO:0007829|PDB:3L87" FT HELIX 75..78 FT /evidence="ECO:0007829|PDB:3L87" FT STRAND 82..90 FT /evidence="ECO:0007829|PDB:3L87" FT STRAND 101..118 FT /evidence="ECO:0007829|PDB:3L87" FT STRAND 120..125 FT /evidence="ECO:0007829|PDB:3L87" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:3L87" FT STRAND 148..153 FT /evidence="ECO:0007829|PDB:3L87" FT STRAND 159..164 FT /evidence="ECO:0007829|PDB:3L87" FT HELIX 166..179 FT /evidence="ECO:0007829|PDB:3L87" FT HELIX 184..187 FT /evidence="ECO:0007829|PDB:3L87" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:3L87" SQ SEQUENCE 204 AA; 22919 MW; CC8FB580FDFCB8A3 CRC64; MSAIKTITKA SHLIDMNDII REGHPTLRAV AQDVTFPLNE DDIILGEKML QFLKNSQDPV TAEKMELRGG VGLAAPQLDI SKRIIAVLIP NPEDKDGNPP KEAYALKEVM YNPRIIAHSV QDAALADGEG CLSVDRVVEG YVIRHSRVTI EYYDKNSDKK KLKLKGYQSI VVQHEIDHTN GIMFFDRINE KNPFEIKEGL LLIE //