ID DEF_CLOB8 Reviewed; 136 AA. AC O08450; A6LZ54; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 27-MAR-2024, entry version 120. DE RecName: Full=Peptide deformylase; DE Short=PDF; DE EC=3.5.1.88; DE AltName: Full=Polypeptide deformylase; GN Name=def; Synonyms=fms; OrderedLocusNames=Cbei_3511; OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium OS acetobutylicum). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=290402; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9572951; DOI=10.1128/aem.64.5.1780-1785.1998; RA Evans V.J., Liyanage H., Ravagnani A., Young M., Kashket E.R.; RT "Truncation of peptide deformylase reduces the growth rate and stabilizes RT solvent production in Clostridium beijerinckii NCIMB 8052."; RL Appl. Environ. Microbiol. 64:1780-1785(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51743 / NCIMB 8052; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G., RA Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W., RA Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B., RA Blaschek H., Richardson P.; RT "Complete sequence of Clostridium beijerinckii NCIMB 8052."; RL Submitted (JUN-2007) 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 (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; Z96934; CAB09662.1; -; Genomic_DNA. DR EMBL; CP000721; ABR35634.1; -; Genomic_DNA. DR RefSeq; WP_012059684.1; NC_009617.1. DR AlphaFoldDB; O08450; -. DR SMR; O08450; -. DR KEGG; cbe:Cbei_3511; -. DR eggNOG; COG0242; Bacteria. DR HOGENOM; CLU_061901_3_1_9; -. DR Proteomes; UP000000565; 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 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..136 FT /note="Peptide deformylase" FT /id="PRO_0000082768" FT ACT_SITE 127 FT /evidence="ECO:0000250" FT BINDING 85 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 126 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 130 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" SQ SEQUENCE 136 AA; 15623 MW; 7E9CE063FFDE9BE6 CRC64; MIKPIVKDIL FLGQKSEEAT KNDMVVIDDL IDTLRANLEH CVGLAANMIG VKKRILVFTV GNLIVPMINP VILKKEKPYE TEESCLSLIG FRKTKRYETI EVTYLDRNFN KKKQVFNGFT AQIIQHEMDH FEGIII //