ID   DEF_AERS4               Reviewed;         170 AA.
AC   A4ST57;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 13.
DE   RecName: Full=Peptide deformylase;
DE            Short=PDF;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase;
GN   Name=def; OrderedLocusNames=ASA_4140;
OS   Aeromonas salmonicida (strain A449).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=382245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Reith M.E., Singh R.K., Curtis B., Boyd J., Bouevitch A., Kimball J.,
RA   Munholland J., Murphy C., Sarty D., Williams J., Nash J., Johnson S.,
RA   Brown L.;
RT   "The genome sequence of Aeromonas salmonicida subsp. salmonicida
RT   A449.";
RL   Submitted (MAR-2007) 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; CP000644; ABO92079.1; -; Genomic_DNA.
DR   RefSeq; YP_001143827.1; -.
DR   GeneID; 4997273; -.
DR   GenomeReviews; CP000644_GR; ASA_4140.
DR   KEGG; asa:ASA_4140; -.
DR   OMA; A4ST57; IGVPRRM.
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.
DR   TIGRFAMs; TIGR00079; pept_deformyl; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Iron; Metal-binding;
KW   Protein biosynthesis.
FT   CHAIN         1    170       Peptide deformylase.
FT                                /FTId=PRO_0000300999.
FT   ACT_SITE    134    134       By similarity.
FT   METAL        91     91       Iron (By similarity).
FT   METAL       133    133       Iron (By similarity).
FT   METAL       137    137       Iron (By similarity).
SQ   SEQUENCE   170 AA;  19432 MW;  A324FB6DECD4B29B CRC64;
     MAILDVLRFP DERLRTVAAP VETFTPELQH IVDDMFETMY AEEGIGLAAT QVDIHQRIIV
     IDVSENREDP LVLINPEILE QAGSTGIEEG CLSVPDHRAL VPRAEWVKVR ALDRNGQPFE
     LEADDLLAIC IQHEMDHLIG KLFVDYLSPL KRQRIRQKLE KMAREDRKAL
//