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HAMAP rule MF_00163

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General rule information [?]

Accession MF_00163
Dates 1-JUN-2001 (Created)
28-NOV-2023 (Last updated, Version 32)
Name Pep_deformylase
Scope(s) Bacteria
Template(s) P0A6K3 (DEF_ECOLI); O31410 (DEF2_GEOSE); Q93LE9 (DEF_LEPIN); P68826 (DEF_STAAU); Q45495 (DEF2_BACSU); P43522 (DEF_THETH); [ Recover all ]
Triggered by HAMAP; MF_00163 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier DEF
Protein name RecName: Full=Peptide deformylase;
AltName: Full=Polypeptide deformylase;
Gene name Name=def;

Comments [?]

FUNCTIONRemoves the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
CATALYTIC ACTIVITY Reaction=H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N- terminal L-methionyl-[peptide]; Xref=Rhea:RHEA:24420, Rhea:RHEA- COMP:10639, Rhea:RHEA-COMP:10640, ChEBI:CHEBI:15377, ChEBI:CHEBI:15740, ChEBI:CHEBI:49298, ChEBI:CHEBI:64731; EC=;
case <FTGroup:1>
COFACTOR Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Note=Binds 1 Fe(2+) ion.;
end case
SIMILARITYBelongs to the polypeptide deformylase family.

Keywords [?]

Protein biosynthesis
case <FTGroup:1>
end case

Gene Ontology [?]

GO:0042586; Molecular function:peptide deformylase activity
GO:0006412; Biological process:translation

Cross-references [?]

Pfam PF01327; Pep_deformylase; 1;
NCBIfam TIGR00079; Pept_deformyl; 1;

Features [?]

From: DEF_ECOLI (P0A6K3)
Key From To Description Tag Condition FTGroup
ACT_SITE 134 134 E
BINDING 91 91 /ligand="Fe cation"
C 1
BINDING 133 133 /ligand="Fe cation"
H 1
BINDING 137 137 /ligand="Fe cation"
H 1

Additional information [?]

Size range 136-232 amino acids
Related rules None
Fusion Nter: None Cter: 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.

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