ID   DEF_MYCLE               Reviewed;         197 AA.
AC   Q9CBI2;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Peptide deformylase;
DE            Short=PDF;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase;
GN   Name=def; OrderedLocusNames=ML1929;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; AL583923; CAC30884.1; -; Genomic_DNA.
DR   PIR; D87150; D87150.
DR   RefSeq; NP_302302.1; NC_002677.1.
DR   RefSeq; WP_010908623.1; NC_002677.1.
DR   AlphaFoldDB; Q9CBI2; -.
DR   SMR; Q9CBI2; -.
DR   STRING; 272631.ML1929; -.
DR   EnsemblBacteria; CAC30884; CAC30884; CAC30884.
DR   KEGG; mle:ML1929; -.
DR   PATRIC; fig|272631.5.peg.3651; -.
DR   Leproma; ML1929; -.
DR   eggNOG; COG0242; Bacteria.
DR   HOGENOM; CLU_061901_1_0_11; -.
DR   OMA; VCIQHEI; -.
DR   Proteomes; UP000000806; 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; -; 1.
DR   HAMAP; MF_00163; Pep_deformylase; 1.
DR   InterPro; IPR023635; Peptide_deformylase.
DR   InterPro; IPR036821; Peptide_deformylase_sf.
DR   PANTHER; PTHR10458; PTHR10458; 1.
DR   Pfam; PF01327; Pep_deformylase; 1.
DR   PIRSF; PIRSF004749; Pep_def; 1.
DR   PRINTS; PR01576; PDEFORMYLASE.
DR   SUPFAM; SSF56420; SSF56420; 1.
DR   TIGRFAMs; TIGR00079; pept_deformyl; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Iron; Metal-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..197
FT                   /note="Peptide deformylase"
FT                   /id="PRO_0000082805"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   197 AA;  21144 MW;  5402C1A35E35CE37 CRC64;
     MAIAPIRIVG DPVLHTPTAP VQVAADGSLP ANLNGLISTM YDTMDAAHGV GLAANQIGYG
     LRVFVYDCAE DCRQTARRRG VVINPILETS EIPETMPDPD TDNEGCLSVP GESFPIGRAQ
     WARVTGLDAD GNPVTTEGTG LFARMLQHET GHLDGFLYLD YLIGRHARSA KRAIKSRHWG
     VPGLSWMPGE VPDPFGP