ID DEF_CALBD Reviewed; 166 AA. AC B9MR36; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 24-JAN-2024, entry version 71. 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=Athe_1039; OS Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / KCTC 15123 / OS Z-1320) (Anaerocellum thermophilum). OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales; OC Caldicellulosiruptoraceae; Caldicellulosiruptor. OX NCBI_TaxID=521460; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1888 / DSM 6725 / KCTC 15123 / Z-1320; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., RA Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., RA Kataeva I., Adams M.W.W.; RT "Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725."; RL Submitted (JAN-2009) 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: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; CP001393; ACM60140.1; -; Genomic_DNA. DR RefSeq; WP_015907552.1; NC_012034.1. DR AlphaFoldDB; B9MR36; -. DR SMR; B9MR36; -. DR STRING; 521460.Athe_1039; -. DR GeneID; 31772390; -. DR KEGG; ate:Athe_1039; -. DR eggNOG; COG0242; Bacteria. DR HOGENOM; CLU_061901_4_2_9; -. DR OMA; VCIQHEI; -. DR Proteomes; UP000007723; 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: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 3: Inferred from homology; KW Hydrolase; Iron; Metal-binding; Protein biosynthesis. FT CHAIN 1..166 FT /note="Peptide deformylase" FT /id="PRO_1000200715" FT ACT_SITE 131 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00163" FT BINDING 88 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00163" FT BINDING 130 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00163" FT BINDING 134 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00163" SQ SEQUENCE 166 AA; 18794 MW; D235D1BE269B83C0 CRC64; MALRKIRTYE DEILRKKSKV VEKFDQRLCQ LLDDMKDTMY EANGIGLAAP QVGVLKRAVV IDIGEGAIEL VNPEIEQVEG SAVDVEGCLS VPNVWGEVER PQKVVVKAQD RFGNEFRLEA EGLLARAVCH EIDHLDGILF VDKVIRFVSE EEIEQRRSRG DKMDLE //