ID   DEF_AQUAE               Reviewed;         169 AA.
AC   O66847;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Peptide deformylase;
DE            Short=PDF;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase;
GN   Name=def; OrderedLocusNames=aq_579;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC06802.1; -; Genomic_DNA.
DR   PIR; C70352; C70352.
DR   RefSeq; NP_213407.1; -.
DR   HSSP; P27251; 2DEF.
DR   GeneID; 1193265; -.
DR   GenomeReviews; AE000657_GR; aq_579.
DR   KEGG; aae:aq_579; -.
DR   NMPDR; fig|224324.1.peg.422; -.
DR   HOGENOM; O66847; -.
DR   OMA; O66847; HEEASPN.
DR   BioCyc; AAEO224324:AQ_579-MON; -.
DR   BRENDA; 3.5.1.88; 189781.
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    169       Peptide deformylase.
FT                                /FTId=PRO_0000082732.
FT   ACT_SITE    136    136       By similarity.
FT   METAL        93     93       Iron (By similarity).
FT   METAL       135    135       Iron (By similarity).
FT   METAL       139    139       Iron (By similarity).
SQ   SEQUENCE   169 AA;  19270 MW;  2C20014DFB199B6E CRC64;
     MVRDIVIYPN EILKKPTEKV DVIDKEVKNL IRDMFDTMYE AEGVGLAANQ IGVPLSVMVI
     DTSPKEDAPP LKLVLINPEI KEGEGKIKYK EGCLSFPGLS VEVERFQKVK VNALNEHGEP
     VELTLEGFPA IVFQHELDHL KGITFVDRLK GWRRRMALEK YQKLLKSRK
//