ID   DEF_THETH               Reviewed;         192 AA.
AC   P43522;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-NOV-2008, entry version 56.
DE   RecName: Full=Peptide deformylase;
DE            Short=PDF;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase;
GN   Name=def;
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VK1;
RX   MEDLINE=95050326; PubMed=7961514;
RA   Meinnel T., Blanquet S.;
RT   "Characterization of the Thermus thermophilus locus encoding peptide
RT   deformylase and methionyl-tRNA(fMet) formyltransferase.";
RL   J. Bacteriol. 176:7387-7390(1994).
RN   [2]
RP   CHARACTERIZATION.
RX   MEDLINE=97272005; PubMed=9126850; DOI=10.1006/jmbi.1997.0904;
RA   Meinnel T., Lazennec C., Villoing S., Blanquet S.;
RT   "Structure-function relationships within the peptide deformylase
RT   family. Evidence for a conserved architecture of the active site
RT   involving three conserved motifs and a metal ion.";
RL   J. Mol. Biol. 267:749-761(1997).
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; X79087; CAA55695.1; -; Genomic_DNA.
DR   PDB; 1V3Y; X-ray; 1.81 A; A/B=1-192.
DR   PDBsum; 1V3Y; -.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Iron; Metal-binding; Protein biosynthesis.
FT   CHAIN         1    192       Peptide deformylase.
FT                                /FTId=PRO_0000082867.
FT   ACT_SITE    146    146       By similarity.
FT   METAL       102    102       Iron (By similarity).
FT   METAL       145    145       Iron (By similarity).
FT   METAL       149    149       Iron (By similarity).
FT   HELIX        11     14
FT   HELIX        26     39
FT   STRAND       43     46
FT   HELIX        47     50
FT   STRAND       54     60
FT   TURN         75     77
FT   STRAND       81     93
FT   STRAND       96    100
FT   STRAND      110    115
FT   STRAND      117    124
FT   STRAND      130    136
FT   HELIX       137    150
FT   HELIX       155    158
FT   HELIX       161    170
FT   HELIX       172    181
SQ   SEQUENCE   192 AA;  22092 MW;  665945183A251361 CRC64;
     MVYPIRLYGD PVLRRKARPV EDFSGIKRLA EDMLETMFEA KGVGLAAPQI GLSQRLFVAV
     EYADEPEGEE ERPLRELVRR VYVVANPVIT YREGLVEGTE GCLSLPGLYS EEVPRAERIR
     VEYQDEEGRG RVLELEGYMA RVFQHEIDHL DGILFFERLP KPKREAFLEA NRAELVRFQK
     EARALLKELS QG
//