ID   DEF_ACIC1               Reviewed;         180 AA.
AC   A0LUE1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JUN-2009, entry version 15.
DE   RecName: Full=Peptide deformylase;
DE            Short=PDF;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase;
GN   Name=def; OrderedLocusNames=Acel_1279;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / 11B).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Frankineae; Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Berry A.M., Adney W.S., Normand P.,
RA   Leu D., Pujic P., Richardson P.;
RT   "Complete sequence of Acidothermus cellulolyticus 11B.";
RL   Submitted (OCT-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; CP000481; ABK53051.1; -; Genomic_DNA.
DR   RefSeq; YP_873037.1; -.
DR   GeneID; 4486350; -.
DR   GenomeReviews; CP000481_GR; Acel_1279.
DR   KEGG; ace:Acel_1279; -.
DR   OMA; A0LUE1; MAIRRIC.
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   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    180       Peptide deformylase.
FT                                /FTId=PRO_0000300998.
FT   ACT_SITE    131    131       By similarity.
FT   METAL        88     88       Iron (By similarity).
FT   METAL       130    130       Iron (By similarity).
FT   METAL       134    134       Iron (By similarity).
SQ   SEQUENCE   180 AA;  19801 MW;  D0E27432502105D1 CRC64;
     MAVRPIRLFG DPVLRTPAEP VTDFDKELRV LIKDLIETMQ DAPGVGLAAP QIGVSLRVFV
     YDVDGVVGHL VNPSLDLSEE QQDGDEGCLS LPGLSYPLKR AKRAVAKGFN EFGEPVILEG
     SDLLARCVQH ETDHLDGVLF IDRLDPEQRK LAMRAIREAE WAGQTVRVKT SPHPTRGKAL
//