ID   DEF1_COREF              Reviewed;         169 AA.
AC   Q8FT51;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Peptide deformylase 1;
DE            Short=PDF 1;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase 1;
GN   Name=def1; OrderedLocusNames=CE1720;
OS   Corynebacterium efficiens.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=152794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   MEDLINE=22723752; PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E.,
RA   Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K.,
RA   Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BA000035; BAC18530.1; -; Genomic_DNA.
DR   RefSeq; NP_738330.1; -.
DR   HSSP; P27251; 2DEF.
DR   GeneID; 1034213; -.
DR   GenomeReviews; BA000035_GR; CE1720.
DR   KEGG; cef:CE1720; -.
DR   NMPDR; fig|196164.1.peg.1720; -.
DR   HOGENOM; Q8FT51; -.
DR   OMA; Q8FT51; MAIRRIC.
DR   BioCyc; CEFF196164:CE1720-MON; -.
DR   BRENDA; 3.5.1.88; 277326.
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 1.
FT                                /FTId=PRO_0000082772.
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;  18445 MW;  1C6EC9BDFDE25B05 CRC64;
     MTVRDVRIFG DPVLTSRADE VVDFDESLAT LIDDMFDTME DAGGVGLAAN QVGVLRRVFV
     FDCSHVDGGL RGHVVNPVWE PIGEETQTGK EGCLSIPDVS AETTRYETVK LSGQDRDGNP
     IGLVASGLLS RCIQHETDHL DGVLFLKRLD PAERKAAMGV IRASDWFNK
//