DEF_MYCPN
ID DEF_MYCPN Reviewed; 216 AA.
AC P75527;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Peptide deformylase;
DE Short=PDF;
DE EC=3.5.1.88;
DE AltName: Full=Polypeptide deformylase;
GN Name=def; OrderedLocusNames=MPN_245; ORFNames=MP587;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96235.1; -; Genomic_DNA.
DR PIR; S73913; S73913.
DR RefSeq; NP_109933.1; NC_000912.1.
DR RefSeq; WP_010874602.1; NC_000912.1.
DR AlphaFoldDB; P75527; -.
DR SMR; P75527; -.
DR IntAct; P75527; 1.
DR STRING; 272634.MPN_245; -.
DR PRIDE; P75527; -.
DR EnsemblBacteria; AAB96235; AAB96235; MPN_245.
DR KEGG; mpn:MPN_245; -.
DR PATRIC; fig|272634.6.peg.264; -.
DR HOGENOM; CLU_061901_4_0_14; -.
DR OMA; DMMEYLV; -.
DR BioCyc; MPNE272634:G1GJ3-388-MON; -.
DR Proteomes; UP000000808; Chromosome.
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 3: Inferred from homology;
KW Hydrolase; Iron; Metal-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..216
FT /note="Peptide deformylase"
FT /id="PRO_0000082803"
FT ACT_SITE 179
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 216 AA; 24592 MW; 361F434048B505DF CRC64;
MTKILPVSTI SIFRIILILP QINMELLPTK AWLVLDDVKE INEPTKPVQF PLDQASLDCI
AKMMAYVDAS YNGDAEKYGI IPGIGIAANQ IGYWKQMFYI HLMDGGVEHK CLLINPKIIN
LSANKSFLKS GEGCLSVPKM HQGYVIRHEW ITITGFDWLQ QKEITITATG LFGMCLQHEF
DHLQGRFYYH RINPLNPLFT NKEWKVINPA LPSDSE
