AC   MF_00163;
DC   Protein; auto
TR   HAMAP; MF_00163; -; 1; level=0
XX
Names: Pep_deformylase
XX
ID   DEF
DE   RecName: Full=Peptide deformylase;
DE            Short=PDF;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase;
GN   Name=def;
XX
CC   -!- FUNCTION: Removes the formyl group from the N-terminal Met of newly
CC       synthesized proteins. Requires at least a dipeptide for an efficient
CC       rate of reaction. N-terminal L-methionine is a prerequisite for
CC       activity but the enzyme has broad specificity at other positions.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-
CC         terminal L-methionyl-[peptide]; Xref=Rhea:RHEA:24420, Rhea:RHEA-
CC         COMP:10639, Rhea:RHEA-COMP:10640, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:49298, ChEBI:CHEBI:64731; EC=3.5.1.88;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC       Note=Binds 1 Fe(2+) ion.;
end case
CC   -!- SIMILARITY: Belongs to the polypeptide deformylase family.
XX
DR   Pfam; PF01327; Pep_deformylase; 1; trigger=no
DR   PRINTS; PR01576; PDEFORMYLASE; 1; trigger=no
DR   NCBIfam; TIGR00079; Pept_deformyl; 1; trigger=no
XX
KW   Protein biosynthesis
KW   Hydrolase
case <FTGroup:1>
KW   Iron
KW   Metal-binding
end case
XX
GO   GO:0042586; F:peptide deformylase activity
GO   GO:0006412; P:translation
XX
FT   From: DEF_ECOLI (P0A6K3)
FT   ACT_SITE        134
FT   Condition: E
FT   BINDING         91
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   Group: 1; Condition: C
FT   BINDING         133
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   Group: 1; Condition: H
FT   BINDING         137
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   Group: 1; Condition: H
XX
Size: 136-232;
Related: None;
Template: P0A6K3; O31410; Q93LE9; P68826; Q45495; P43522;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in NOSS1, BACAN, BACCR, BACSU, BIFLO, BORBR, BORPA, BORPE, CLOAB,
 CLOPE, COREF, CORGL, COXBU, GLOVI, NITEU, PROMM, RALN1, RICCN, STRAW, STRCO,
 VIBCH, VIBVY, XANAC, XANCP
Plasmid: None
Comments: Possible wrong start in a number of bacteria.
 Def-like proteins exist a number of bacteria and lack some active site
 and metal-binding residues.
XX
# Revision 1.32 2023/11/28
//