ID   DEF3_SHEON              Reviewed;         163 AA.
AC   Q8EE60;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 39.
DE   RecName: Full=Peptide deformylase 3;
DE            Short=PDF 3;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase 3;
GN   Name=def3; OrderedLocusNames=SO_2530;
OS   Shewanella oneidensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=70863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   MEDLINE=22297686; PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A.,
RA   Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S.,
RA   Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A.,
RA   White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M.,
RA   Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J.,
RA   Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O.,
RA   Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(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; AE014299; AAN55560.1; -; Genomic_DNA.
DR   RefSeq; NP_718116.1; -.
DR   HSSP; P27251; 1DEF.
DR   GeneID; 1170239; -.
DR   GenomeReviews; AE014299_GR; SO_2530.
DR   KEGG; son:SO_2530; -.
DR   NMPDR; fig|211586.1.peg.2293; -.
DR   TIGR; SO_2530; -.
DR   HOGENOM; Q8EE60; -.
DR   OMA; Q8EE60; RIMVIDI.
DR   BioCyc; SONE211586:SO_2530-MON; -.
DR   BRENDA; 3.5.1.88; 257422.
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    163       Peptide deformylase 3.
FT                                /FTId=PRO_0000082836.
FT   ACT_SITE    134    134       By similarity.
FT   METAL        91     91       Iron (By similarity).
FT   METAL       133    133       Iron (By similarity).
FT   METAL       137    137       Iron (By similarity).
SQ   SEQUENCE   163 AA;  18221 MW;  A4A06C2952DB92EE CRC64;
     MAVLDILTIP DERLKRKAQP VKDIEAIQGF IDDLIETMYH TDDGIGLAST QVGSTDAVIV
     IDLSETRDQP LVLVNPEIVE KSGEYVGEEG CLSIPGYRAK VTRFEKVKVT ALDRQGKAIE
     IETDDFLAIV LQHEIDHLHG KVFIEHLSTL KQQIALKKVR KYA
//