ID   DEF_PSEAE               Reviewed;         168 AA.
AC   Q9I7A8;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Peptide deformylase;
DE            Short=PDF;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase;
GN   Name=def; OrderedLocusNames=PA0019;
OS   Pseudomonas aeruginosa.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
RX   MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
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; AE004091; AAG03409.1; -; Genomic_DNA.
DR   PIR; H83643; H83643.
DR   RefSeq; NP_248709.1; -.
DR   PDB; 1IX1; X-ray; 1.85 A; A/B=1-168.
DR   PDB; 1LRY; X-ray; 2.60 A; A=2-168.
DR   PDB; 1N5N; X-ray; 1.80 A; A/B=1-168.
DR   PDB; 1S17; X-ray; 1.95 A; A/B=1-168.
DR   PDBsum; 1IX1; -.
DR   PDBsum; 1LRY; -.
DR   PDBsum; 1N5N; -.
DR   PDBsum; 1S17; -.
DR   GeneID; 879306; -.
DR   GenomeReviews; AE004091_GR; PA0019.
DR   KEGG; pae:PA0019; -.
DR   PseudoCAP; PA0019; -.
DR   HOGENOM; Q9I7A8; -.
DR   OMA; Q9I7A8; CIQHECD.
DR   BioCyc; PAER208964:PA0019-MON; -.
DR   BRENDA; 3.5.1.88; 354.
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   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Hydrolase; Iron; Metal-binding;
KW   Protein biosynthesis.
FT   CHAIN         1    168       Peptide deformylase.
FT                                /FTId=PRO_0000082819.
FT   ACT_SITE    135    135       By similarity.
FT   METAL        92     92       Iron (By similarity).
FT   METAL       134    134       Iron (By similarity).
FT   METAL       138    138       Iron (By similarity).
FT   HELIX        12     15
FT   HELIX        26     41
FT   STRAND       45     48
FT   HELIX        49     52
FT   STRAND       56     62
FT   STRAND       64     67
FT   STRAND       70     81
FT   STRAND       85     90
FT   STRAND      100    113
FT   STRAND      119    125
FT   HELIX       126    139
FT   HELIX       144    147
FT   HELIX       150    168
SQ   SEQUENCE   168 AA;  19365 MW;  A95F6B921E5F3189 CRC64;
     MAILNILEFP DPRLRTIAKP VEVVDDAVRQ LIDDMFETMY EAPGIGLAAT QVNVHKRIVV
     MDLSEDKSEP RVFINPEFEP LTEDMDQYQE GCLSVPGFYE NVDRPQKVRI KALDRDGNPF
     EEVAEGLLAV CIQHECDHLN GKLFVDYLST LKRDRIRKKL EKQHRQQA
//