ID   DEF1_RICCN              Reviewed;         175 AA.
AC   Q92IZ1;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   16-JUN-2009, entry version 45.
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=RC0278;
OS   Rickettsia conorii.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=781;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   MEDLINE=21442074; PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M.,
RA   Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL02816.1; -; Genomic_DNA.
DR   PIR; F97734; F97734.
DR   RefSeq; NP_359915.1; -.
DR   HSSP; P27251; 1DEF.
DR   GeneID; 927899; -.
DR   GenomeReviews; AE006914_GR; RC0278.
DR   KEGG; rco:RC0278; -.
DR   NMPDR; fig|272944.1.peg.278; -.
DR   HOGENOM; Q92IZ1; -.
DR   OMA; Q92IZ1; LETMYNA.
DR   BioCyc; RCON272944:RC0278-MON; -.
DR   BRENDA; 3.5.1.88; 267518.
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    175       Peptide deformylase 1.
FT                                /FTId=PRO_0000082829.
FT   ACT_SITE    142    142       By similarity.
FT   METAL        99     99       Iron (By similarity).
FT   METAL       141    141       Iron (By similarity).
FT   METAL       145    145       Iron (By similarity).
SQ   SEQUENCE   175 AA;  20280 MW;  93B050C6003C5A6D CRC64;
     MSILPIVTAP DERLKQKSQP VLEFTDQTRK FMDDMLKTMY HEDGAGLAAV QVGVLKRILV
     IDIQDHDSVA RPKDFYPLFI VNPEIIEKAE ELVTANEGCI SLPEQRIEVA RPESIKIRYL
     DYHGKSRELK ANDWLARVIQ HEYDHLEGKL MIDYLSNLKR DVVLRKLKKL KNNIV
//