ID DEF_ACIBS Reviewed; 176 AA. AC B0VNL8; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 91. 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=ABSDF0185; OS Acinetobacter baumannii (strain SDF). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=509170; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDF; RX PubMed=18350144; DOI=10.1371/journal.pone.0001805; RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., RA Weissenbach J., Cruveiller S.; RT "Comparative analysis of Acinetobacters: three genomes for three RT lifestyles."; RL PLoS ONE 3:E1805-E1805(2008). 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; CU468230; CAO99588.1; -; Genomic_DNA. DR PDB; 6JER; X-ray; 2.40 A; A/B=3-172. DR PDB; 6JET; X-ray; 2.60 A; A/B=2-172. DR PDB; 6JEU; X-ray; 2.10 A; A/B=2-171. DR PDB; 6JEV; X-ray; 1.90 A; A/B=3-173. DR PDB; 6JEW; X-ray; 2.00 A; A/B=3-173. DR PDB; 6JEX; X-ray; 2.11 A; A/B=2-173. DR PDBsum; 6JER; -. DR PDBsum; 6JET; -. DR PDBsum; 6JEU; -. DR PDBsum; 6JEV; -. DR PDBsum; 6JEW; -. DR PDBsum; 6JEX; -. DR AlphaFoldDB; B0VNL8; -. DR SMR; B0VNL8; -. DR KEGG; abm:ABSDF0185; -. DR HOGENOM; CLU_061901_2_0_6; -. DR Proteomes; UP000001741; 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:SF21; 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. FT CHAIN 1..176 FT /note="Peptide deformylase" FT /id="PRO_1000097291" FT ACT_SITE 135 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00163" FT BINDING 92 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" FT BINDING 138 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:6JEV" FT HELIX 26..41 FT /evidence="ECO:0007829|PDB:6JEV" FT STRAND 45..48 FT /evidence="ECO:0007829|PDB:6JEV" FT HELIX 49..52 FT /evidence="ECO:0007829|PDB:6JEV" FT STRAND 56..61 FT /evidence="ECO:0007829|PDB:6JEV" FT STRAND 64..67 FT /evidence="ECO:0007829|PDB:6JER" FT STRAND 71..81 FT /evidence="ECO:0007829|PDB:6JEV" FT STRAND 85..90 FT /evidence="ECO:0007829|PDB:6JEV" FT STRAND 100..113 FT /evidence="ECO:0007829|PDB:6JEV" FT STRAND 119..125 FT /evidence="ECO:0007829|PDB:6JEV" FT HELIX 126..139 FT /evidence="ECO:0007829|PDB:6JEV" FT HELIX 144..147 FT /evidence="ECO:0007829|PDB:6JEV" FT HELIX 150..172 FT /evidence="ECO:0007829|PDB:6JEV" SQ SEQUENCE 176 AA; 20095 MW; CBDCA96B5FDA36D0 CRC64; MALLPILSFP DPRLRTIAKP VEEVTDEIRQ LAADMFETMY AAPGIGLAAS QVDRHIQLIV MDLSESKDEP MVFINPKVTP LTEETQPYEE GCLSVPQIYD KVDRPSRVKI EAINLEGQAF EIEADGLLAV CIQHEMDHLN GKLFVDYLSP LKRQRVREKV EKIVRQRERE KVAVKR //