ID   DEF_AMOA5               Reviewed;         188 AA.
AC   B3ETT4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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}; OrderedLocusNames=Aasi_1326;
OS   Amoebophilus asiaticus (strain 5a2).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Amoebophilaceae;
OC   Candidatus Amoebophilus.
OX   NCBI_TaxID=452471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5a2;
RX   PubMed=20023027; DOI=10.1128/jb.01379-09;
RA   Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA   Rattei T., Horn M.;
RT   "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT   reveals common mechanisms for host cell interaction among amoeba-associated
RT   bacteria.";
RL   J. Bacteriol. 192:1045-1057(2010).
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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; CP001102; ACE06636.1; -; Genomic_DNA.
DR   RefSeq; WP_012473380.1; NC_010830.1.
DR   AlphaFoldDB; B3ETT4; -.
DR   SMR; B3ETT4; -.
DR   STRING; 452471.Aasi_1326; -.
DR   EnsemblBacteria; ACE06636; ACE06636; Aasi_1326.
DR   KEGG; aas:Aasi_1326; -.
DR   eggNOG; COG0242; Bacteria.
DR   HOGENOM; CLU_061901_2_0_10; -.
DR   OMA; VCIQHEI; -.
DR   OrthoDB; 1649129at2; -.
DR   Proteomes; UP000001227; 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..188
FT                   /note="Peptide deformylase"
FT                   /id="PRO_1000097295"
FT   ACT_SITE        142
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00163"
FT   BINDING         99
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00163"
FT   BINDING         141
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00163"
FT   BINDING         145
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00163"
SQ   SEQUENCE   188 AA;  21562 MW;  DDEBC08B0679DA3F CRC64;
     MIYPIVPYGE SILRQTAAPI ELGTDLETLI ESMFITMNAA KGLGLAAPQI GKSIQLFVVD
     VSPFVGDGMV QPDKHRKVYI NPVLEIYQPN TITHYEEGCL SIPGIYVDVP RNKRVRIKFF
     DRNWQAQEED LVDMPARVVQ HEYDHLYGKL HIDYLRADRR LRLKSKLENI KQGRVEVAYK
     MSFTGNKV