ID   DEF_BARHE               Reviewed;         176 AA.
AC   Q6G5F0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Peptide deformylase;
DE            Short=PDF;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase;
GN   Name=def; OrderedLocusNames=BH00760;
OS   Bartonella henselae (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=38323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF26892.1; -; Genomic_DNA.
DR   RefSeq; YP_032939.1; -.
DR   GeneID; 2864510; -.
DR   GenomeReviews; BX897699_GR; BH00760.
DR   KEGG; bhe:BH00760; -.
DR   NMPDR; fig|283166.1.peg.67; -.
DR   HOGENOM; Q6G5F0; -.
DR   OMA; Q6G5F0; RIMVIDI.
DR   BioCyc; BHEN283166:BH00760-MON; -.
DR   BRENDA; 3.5.1.88; 277357.
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    176       Peptide deformylase.
FT                                /FTId=PRO_0000301007.
FT   ACT_SITE    137    137       By similarity.
FT   METAL        94     94       Iron (By similarity).
FT   METAL       136    136       Iron (By similarity).
FT   METAL       140    140       Iron (By similarity).
SQ   SEQUENCE   176 AA;  20414 MW;  20600678F4C16145 CRC64;
     MPMRPLVIVP DPILREISKP VEYIDSAVQK LADDMLETMY HAQGVGLAAI QIGIPLRMLV
     LDVSRNDEQK NPLVIINPEV LWLSDERNIY KEGCLSIPEY FAEVERPKRL CVRYQNREGK
     QTEIEADDLL ATCLQHEIDH LNGRLFIDYL SKIKRDMVIR KFKKRAKEKN TQEAVL
//