ID   DEF_BIFAA               Reviewed;         218 AA.
AC   A1A2Z1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 16.
DE   RecName: Full=Peptide deformylase;
DE            Short=PDF;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase;
GN   Name=def; OrderedLocusNames=BAD_1293;
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083).
OC   Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=367928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S.,
RA   Hirai S., Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Removes the formyl group from the N-terminal Met of
CC       newly synthesized proteins. Requires at least a dipeptide for an
CC       efficient rate of reaction. N-terminal L-methionine is a
CC       prerequisite for activity but the enzyme has broad specificity at
CC       other positions (By similarity).
CC   -!- CATALYTIC ACTIVITY: Formyl-L-methionyl peptide + H(2)O = formate +
CC       methionyl peptide.
CC   -!- COFACTOR: Binds 1 Fe(2+) ion (By similarity).
CC   -!- SIMILARITY: Belongs to the polypeptide deformylase family.
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DR   EMBL; AP009256; BAF40074.1; -; Genomic_DNA.
DR   RefSeq; YP_910156.1; -.
DR   GeneID; 4556246; -.
DR   GenomeReviews; AP009256_GR; BAD_1293.
DR   KEGG; bad:BAD_1293; -.
DR   NMPDR; fig|1680.3.peg.923; -.
DR   OMA; A1A2Z1; GWPARIL.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042586; F:peptide deformylase activity; IEA:HAMAP.
DR   GO; GO:0006412; P:translation; IEA:HAMAP.
DR   HAMAP; MF_00163; -; 1.
DR   InterPro; IPR000181; Fmet_deformylase.
DR   Gene3D; G3DSA:3.90.45.10; Fmet_deformylase; 1.
DR   PANTHER; PTHR10458; Fmet_deformylase; 1.
DR   Pfam; PF01327; Pep_deformylase; 1.
DR   PIRSF; PIRSF004749; Pep_def; 1.
DR   PRINTS; PR01576; PDEFORMYLASE.
DR   ProDom; PD003844; Fmet_deformylase; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Iron; Metal-binding;
KW   Protein biosynthesis.
FT   CHAIN         1    218       Peptide deformylase.
FT                                /FTId=PRO_0000301010.
FT   ACT_SITE    173    173       By similarity.
FT   METAL       130    130       Iron (By similarity).
FT   METAL       172    172       Iron (By similarity).
FT   METAL       176    176       Iron (By similarity).
SQ   SEQUENCE   218 AA;  24536 MW;  4CE4C976E83FFDCE CRC64;
     MFGHNSKVDL ELNREVEKLI KTGGKEKIMP IVQAGEPVLR QQTIAYDGQL SRKTLDKLID
     TMRTTMLEAP GVGLAATQIG LGLALAVVED HVCEGDDGDP REAAEFPFHA IINPSYEPIG
     TETRSFYEGC LSFDGYQAVR KRWLDITARW QDEDGNKHEE HLHGWPARIF QHETDHLSGE
     LYIDQAEIRS LTTNENLEDF WCEDPVPTEA AAELGFEL
//