ID DEF1_BACCR Reviewed; 156 AA. AC Q819U0; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 124. DE RecName: Full=Peptide deformylase 1 {ECO:0000255|HAMAP-Rule:MF_00163}; DE Short=PDF 1 {ECO:0000255|HAMAP-Rule:MF_00163}; DE EC=3.5.1.88 {ECO:0000255|HAMAP-Rule:MF_00163}; DE AltName: Full=Polypeptide deformylase 1 {ECO:0000255|HAMAP-Rule:MF_00163}; GN Name=def1 {ECO:0000255|HAMAP-Rule:MF_00163}; GN OrderedLocusNames=BC_3865; OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=226900; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB RC 9373 / NCTC 2599 / NRRL B-3711; RX PubMed=12721630; DOI=10.1038/nature01582; RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G., RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.; RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus RT anthracis."; RL Nature 423:87-91(2003). 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; AE016877; AAP10787.1; -; Genomic_DNA. DR RefSeq; NP_833586.1; NC_004722.1. DR RefSeq; WP_000279455.1; NZ_CP034551.1. DR PDB; 1WS0; X-ray; 1.70 A; A=1-156. DR PDB; 1WS1; X-ray; 2.00 A; A=1-156. DR PDBsum; 1WS0; -. DR PDBsum; 1WS1; -. DR AlphaFoldDB; Q819U0; -. DR SMR; Q819U0; -. DR STRING; 226900.BC_3865; -. DR DrugBank; DB04310; 2-[(Formyl-Hydroxy-Amino)-Methyl]-Heptanoic Acid [1-(2-Hydroxymethyl-Pyrrolidine-1-Carbonyl)-2-Methyl-Propyl]-Amide. DR GeneID; 72450547; -. DR KEGG; bce:BC3865; -. DR PATRIC; fig|226900.8.peg.3984; -. DR HOGENOM; CLU_061901_4_2_9; -. DR OrthoDB; 9784988at2; -. DR EvolutionaryTrace; Q819U0; -. DR Proteomes; UP000001417; 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..156 FT /note="Peptide deformylase 1" FT /id="PRO_0000082735" FT ACT_SITE 133 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00163" FT BINDING 90 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00163" FT BINDING 132 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00163" FT BINDING 136 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00163" FT HELIX 12..15 FT /evidence="ECO:0007829|PDB:1WS0" FT HELIX 26..41 FT /evidence="ECO:0007829|PDB:1WS0" FT STRAND 45..48 FT /evidence="ECO:0007829|PDB:1WS0" FT HELIX 49..52 FT /evidence="ECO:0007829|PDB:1WS0" FT STRAND 56..62 FT /evidence="ECO:0007829|PDB:1WS0" FT TURN 65..67 FT /evidence="ECO:0007829|PDB:1WS0" FT STRAND 69..88 FT /evidence="ECO:0007829|PDB:1WS0" FT STRAND 98..111 FT /evidence="ECO:0007829|PDB:1WS0" FT STRAND 117..123 FT /evidence="ECO:0007829|PDB:1WS0" FT HELIX 124..137 FT /evidence="ECO:0007829|PDB:1WS0" FT HELIX 142..144 FT /evidence="ECO:0007829|PDB:1WS0" FT STRAND 146..149 FT /evidence="ECO:0007829|PDB:1WS0" SQ SEQUENCE 156 AA; 17480 MW; 0B68AB39485C4D8A CRC64; MAVLEIIKHP NEVLETPCER VINFDKKLVK LLKDMHETML IADGVGLAAP QVGVSLQVAV VDVDDDTGKI ELINPSILEK RGEQVGPEGC LSFPGLYGEV ERADYIKVRA QNRRGKVFLL EAEGFLARAI QHEIDHLHGV LFTSKVTRYY EENELE //