ID   DEF_THETH               Reviewed;         192 AA.
AC   P43522;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Peptide deformylase;
DE            Short=PDF;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase;
GN   Name=def;
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VK1;
RX   PubMed=7961514; DOI=10.1128/jb.176.23.7387-7390.1994;
RA   Meinnel T., Blanquet S.;
RT   "Characterization of the Thermus thermophilus locus encoding peptide
RT   deformylase and methionyl-tRNA(fMet) formyltransferase.";
RL   J. Bacteriol. 176:7387-7390(1994).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=9126850; DOI=10.1006/jmbi.1997.0904;
RA   Meinnel T., Lazennec C., Villoing S., Blanquet S.;
RT   "Structure-function relationships within the peptide deformylase family.
RT   Evidence for a conserved architecture of the active site involving three
RT   conserved motifs and a metal ion.";
RL   J. Mol. Biol. 267:749-761(1997).
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 (By
CC       similarity). {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(2+) ion. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the polypeptide deformylase family.
CC       {ECO:0000305}.
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DR   EMBL; X79087; CAA55695.1; -; Genomic_DNA.
DR   RefSeq; WP_011174028.1; NZ_CP053287.1.
DR   PDB; 1V3Y; X-ray; 1.81 A; A/B=1-192.
DR   PDBsum; 1V3Y; -.
DR   AlphaFoldDB; P43522; -.
DR   SMR; P43522; -.
DR   DrugBank; DB03661; L-cysteic acid.
DR   GeneID; 3169711; -.
DR   EvolutionaryTrace; P43522; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042586; F:peptide deformylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00487; Pep_deformylase; 1.
DR   Gene3D; 3.90.45.10; -; 1.
DR   HAMAP; MF_00163; Pep_deformylase; 1.
DR   InterPro; IPR023635; Peptide_deformylase.
DR   InterPro; IPR036821; Peptide_deformylase_sf.
DR   PANTHER; PTHR10458; PTHR10458; 1.
DR   Pfam; PF01327; Pep_deformylase; 1.
DR   PIRSF; PIRSF004749; Pep_def; 1.
DR   PRINTS; PR01576; PDEFORMYLASE.
DR   SUPFAM; SSF56420; SSF56420; 1.
DR   TIGRFAMs; TIGR00079; pept_deformyl; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Iron; Metal-binding; Protein biosynthesis.
FT   CHAIN           1..192
FT                   /note="Peptide deformylase"
FT                   /id="PRO_0000082867"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   HELIX           11..14
FT                   /evidence="ECO:0007829|PDB:1V3Y"
FT   HELIX           26..39
FT                   /evidence="ECO:0007829|PDB:1V3Y"
FT   STRAND          43..46
FT                   /evidence="ECO:0007829|PDB:1V3Y"
FT   HELIX           47..50
FT                   /evidence="ECO:0007829|PDB:1V3Y"
FT   STRAND          54..60
FT                   /evidence="ECO:0007829|PDB:1V3Y"
FT   TURN            75..77
FT                   /evidence="ECO:0007829|PDB:1V3Y"
FT   STRAND          81..93
FT                   /evidence="ECO:0007829|PDB:1V3Y"
FT   STRAND          96..100
FT                   /evidence="ECO:0007829|PDB:1V3Y"
FT   STRAND          110..115
FT                   /evidence="ECO:0007829|PDB:1V3Y"
FT   STRAND          117..124
FT                   /evidence="ECO:0007829|PDB:1V3Y"
FT   STRAND          130..136
FT                   /evidence="ECO:0007829|PDB:1V3Y"
FT   HELIX           137..150
FT                   /evidence="ECO:0007829|PDB:1V3Y"
FT   HELIX           155..158
FT                   /evidence="ECO:0007829|PDB:1V3Y"
FT   HELIX           161..170
FT                   /evidence="ECO:0007829|PDB:1V3Y"
FT   HELIX           172..181
FT                   /evidence="ECO:0007829|PDB:1V3Y"
SQ   SEQUENCE   192 AA;  22092 MW;  665945183A251361 CRC64;
     MVYPIRLYGD PVLRRKARPV EDFSGIKRLA EDMLETMFEA KGVGLAAPQI GLSQRLFVAV
     EYADEPEGEE ERPLRELVRR VYVVANPVIT YREGLVEGTE GCLSLPGLYS EEVPRAERIR
     VEYQDEEGRG RVLELEGYMA RVFQHEIDHL DGILFFERLP KPKREAFLEA NRAELVRFQK
     EARALLKELS QG