ID   DEF2_PSEPK              Reviewed;         178 AA.
AC   Q88EA7;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 37.
DE   RecName: Full=Peptide deformylase 2;
DE            Short=PDF 2;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase 2;
GN   Name=def2; OrderedLocusNames=PP_4559;
OS   Pseudomonas putida (strain KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22423060; PubMed=12534463;
RX   DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M.,
RA   Hance I., Chris Lee P., Holtzapple E.K., Scanlan D., Tran K.,
RA   Moazzez A., Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D.,
RA   Wedler H., Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S.,
RA   Kiewitz C., Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B.,
RA   Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the
RT   metabolically versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN70132.1; -; Genomic_DNA.
DR   RefSeq; NP_746668.1; -.
DR   HSSP; Q9F2F0; 1LM6.
DR   GeneID; 1046247; -.
DR   GenomeReviews; AE015451_GR; PP_4559.
DR   KEGG; ppu:PP_4559; -.
DR   NMPDR; fig|160488.1.peg.4498; -.
DR   TIGR; PP_4559; -.
DR   HOGENOM; Q88EA7; -.
DR   OMA; Q88EA7; LYPSRIT.
DR   BioCyc; PPUT160488:PP_4559-MON; -.
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    178       Peptide deformylase 2.
FT                                /FTId=PRO_0000082821.
FT   ACT_SITE    144    144       By similarity.
FT   METAL       101    101       Iron (By similarity).
FT   METAL       143    143       Iron (By similarity).
FT   METAL       147    147       Iron (By similarity).
SQ   SEQUENCE   178 AA;  19852 MW;  044749D0EE6738C8 CRC64;
     MIRDILKMGD ERLLRIAPPV PEHMLGSAEL QQLIDDMFET MRHVGGVGLA APQVGIDLQL
     VIFGFERSER YPDAEAVPQT ILLNPVITPT SSEVEDGWEG CLSVPGLRGV VPRFKHICYQ
     GIDPQGSPIN RFADGFHARV VQHECDHLIG RLYPSRIQDF AKFGYTEVLF PGLEVSED
//