ID   DEF_MICDP               Reviewed;         187 AA.
AC   P94601;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   13-SEP-2023, entry version 89.
DE   RecName: Full=Peptide deformylase;
DE            Short=PDF;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase;
GN   Name=def;
OS   Microchaete diplosiphon (Fremyella diplosiphon).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Rivulariaceae;
OC   Microchaete.
OX   NCBI_TaxID=1197;
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).
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}.
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DR   EMBL; Y10305; CAA71353.1; -; Genomic_DNA.
DR   AlphaFoldDB; P94601; -.
DR   SMR; P94601; -.
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..187
FT                   /note="Peptide deformylase"
FT                   /id="PRO_0000082783"
FT   ACT_SITE        150
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   187 AA;  20938 MW;  B58EC9BAA0EBF299 CRC64;
     MPSEIAVEKK KLKNPPLQLH YLGDRVLRQP AKRIAKVDDE LRQLIRDMLQ TMYSKDGIGL
     AAPQVGIHKQ LIVIDLEPDN PANPPLVLIN PTIKQVSKEI CVAQEGCLSI PNVYMDVKRP
     EVVEIAYKDE NGRPKTLKAT DLLARCIQHE MDHLNGVVFV DRVDNSLTLA QELSKNGFSY
     QAVKPVA
//