ID   DEF2_VIBVU              Reviewed;         168 AA.
AC   Q8D5P5;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-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=VV2_0863;
OS   Vibrio vulnificus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H.,
RA   Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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; AE016796; AAO07786.1; -; Genomic_DNA.
DR   RefSeq; NP_762796.1; -.
DR   HSSP; P27251; 1LRU.
DR   GeneID; 1180842; -.
DR   GenomeReviews; AE016796_GR; VV2_0863.
DR   KEGG; vvu:VV2_0863; -.
DR   HOGENOM; Q8D5P5; -.
DR   OMA; Q8D5P5; SENRDEP.
DR   BioCyc; VVUL216895:VV2_0863-MON; -.
DR   BRENDA; 3.5.1.88; 277169.
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    168       Peptide deformylase 2.
FT                                /FTId=PRO_0000082878.
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   168 AA;  18729 MW;  D835D1F2ECFF68DC CRC64;
     MAVLEILTAP DPRLRVQSKE VTDVAAVQTL IDDLLETLYE TDNGVGLAAP QVGREEAIVV
     IDLSENRDEP LVLVNPKVVS GSNKEMGQEG CLSVPDYYAD VERYTSVVVE ALDRDGKPLR
     IETSEFLAIV MQHEIDHLSG NLFIDYLSPL KQQMAMKKVK KHNKLRAR
//