ID   DEF1B_SOLLC             Reviewed;         279 AA.
AC   Q9FV54;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Peptide deformylase 1B, chloroplastic;
DE            Short=PDF 1B;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase;
DE   Flags: Precursor;
GN   Name=PDF1B;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11060042; DOI=10.1093/emboj/19.21.5916;
RA   Giglione C., Serero A., Pierre M., Boisson B., Meinnel T.;
RT   "Identification of eukaryotic peptide deformylases reveals universality of
RT   N-terminal protein processing mechanisms.";
RL   EMBO J. 19:5916-5929(2000).
CC   -!- FUNCTION: Removes the formyl group from the N-terminal Met of newly
CC       synthesized proteins. {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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the polypeptide deformylase family.
CC       {ECO:0000305}.
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DR   EMBL; AF250958; AAG33972.1; -; mRNA.
DR   RefSeq; NP_001234441.1; NM_001247512.2.
DR   AlphaFoldDB; Q9FV54; -.
DR   SMR; Q9FV54; -.
DR   STRING; 4081.Solyc02g086680.2.1; -.
DR   PaxDb; Q9FV54; -.
DR   PRIDE; Q9FV54; -.
DR   GeneID; 543648; -.
DR   KEGG; sly:543648; -.
DR   eggNOG; KOG3137; Eukaryota.
DR   HOGENOM; CLU_061901_0_1_1; -.
DR   InParanoid; Q9FV54; -.
DR   OrthoDB; 1532656at2759; -.
DR   PhylomeDB; Q9FV54; -.
DR   SABIO-RK; Q9FV54; -.
DR   Proteomes; UP000004994; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042586; F:peptide deformylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018206; P:peptidyl-methionine modification; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
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   PRINTS; PR01576; PDEFORMYLASE.
DR   SUPFAM; SSF56420; SSF56420; 1.
DR   TIGRFAMs; TIGR00079; pept_deformyl; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Hydrolase; Iron; Metal-binding; Plastid; Protein biosynthesis;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..279
FT                   /note="Peptide deformylase 1B, chloroplastic"
FT                   /id="PRO_0000006733"
FT   ACT_SITE        220
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   279 AA;  31197 MW;  750F6406FDAC4233 CRC64;
     MAMAAASWAS SSSFTRFLRP LLSRNSSPSP ISYSLHRYKS ANCLFFSASS NKPPKLAVYA
     QARRVLSSKT KGDEIATPAD LSFVVPLKIV EYPDPILRAK NKRIDNFDAN LKKLVDEMFD
     IMYKTDGIGL SAPQVGMNVQ LMVFNAAGER GEGEEIVLVN PRVSRYSRRI IPYEEGCLSF
     PMIHGDVKRP ESVKVDAQDI NGTRFEISLS ALPARVFQHE FDHLQGVLFF DKMTDEVLDT
     IREKLVALEK KYEDRTGLPT PESINTRKIK KAAVGFGKS