ID DEF_THEMA Reviewed; 164 AA. AC P96113; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 27-MAR-2024, entry version 151. DE RecName: Full=Peptide deformylase; DE Short=PDF; DE EC=3.5.1.88; DE AltName: Full=Polypeptide deformylase; GN Name=def; OrderedLocusNames=TM_1661; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9086272; DOI=10.1006/jmbi.1996.0835; RA Mazel D., Coic E., Blanchard S., Saurin W., Marliere P.; RT "A survey of polypeptide deformylase function throughout the eubacterial RT lineage."; RL J. Mol. Biol. 266:939-949(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). 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 (By CC similarity). {ECO:0000250}. 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 -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; CC Note=Binds 1 Fe(2+) ion. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the polypeptide deformylase family. CC {ECO:0000305}. 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; Y10306; CAA71356.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36728.1; -; Genomic_DNA. DR PIR; C72224; C72224. DR RefSeq; NP_229461.1; NC_000853.1. DR RefSeq; WP_004082176.1; NZ_CP011107.1. DR PDB; 1LME; X-ray; 2.20 A; A/B=1-164. DR PDBsum; 1LME; -. DR AlphaFoldDB; P96113; -. DR SMR; P96113; -. DR STRING; 243274.TM_1661; -. DR DrugBank; DB03661; L-cysteic acid. DR PaxDb; 243274-THEMA_05940; -. DR EnsemblBacteria; AAD36728; AAD36728; TM_1661. DR KEGG; tma:TM1661; -. DR eggNOG; COG0242; Bacteria. DR InParanoid; P96113; -. DR OrthoDB; 9784988at2; -. DR BRENDA; 3.5.1.88; 6331. DR EvolutionaryTrace; P96113; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042586; F:peptide deformylase activity; IBA:GO_Central. DR GO; GO:0043686; P:co-translational protein modification; IBA:GO_Central. 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: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. PE 1: Evidence at protein level; KW 3D-structure; Hydrolase; Iron; Metal-binding; Protein biosynthesis; KW Reference proteome. FT CHAIN 1..164 FT /note="Peptide deformylase" FT /id="PRO_0000082866" FT ACT_SITE 130 FT /evidence="ECO:0000250" FT BINDING 87 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 129 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 133 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT HELIX 10..12 FT /evidence="ECO:0007829|PDB:1LME" FT HELIX 24..39 FT /evidence="ECO:0007829|PDB:1LME" FT STRAND 43..46 FT /evidence="ECO:0007829|PDB:1LME" FT HELIX 47..50 FT /evidence="ECO:0007829|PDB:1LME" FT STRAND 54..59 FT /evidence="ECO:0007829|PDB:1LME" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:1LME" FT STRAND 66..76 FT /evidence="ECO:0007829|PDB:1LME" FT STRAND 80..85 FT /evidence="ECO:0007829|PDB:1LME" FT STRAND 95..108 FT /evidence="ECO:0007829|PDB:1LME" FT STRAND 114..120 FT /evidence="ECO:0007829|PDB:1LME" FT HELIX 121..134 FT /evidence="ECO:0007829|PDB:1LME" FT HELIX 139..142 FT /evidence="ECO:0007829|PDB:1LME" SQ SEQUENCE 164 AA; 19024 MW; 9FE94A206DE50842 CRC64; MYRIRVFGDP VLRKRAKPVT KFDENLKKTI ERMIETMYHY DGVGLAAPQV GISQRFFVMD VGNGPVAVIN PEILEIDPET EVAEEGCLSF PEIFVEIERS KRIKVKYQNT RGEYVEEELE GYAARVFQHE FDHLNGVLII DRISPAKRLL LRKKLMDIAR TVKR //