ID   DEF1A_SOLLC             Reviewed;         277 AA.
AC   Q9FUZ0;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Peptide deformylase 1A, chloroplastic;
DE            Short=PDF 1A;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase;
DE   Flags: Precursor;
GN   Name=PDF1A;
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=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the polypeptide deformylase family.
CC       {ECO:0000305}.
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DR   EMBL; AF271258; AAG33981.1; -; mRNA.
DR   RefSeq; NP_001234703.1; NM_001247774.2.
DR   RefSeq; NP_001303906.1; NM_001316977.1.
DR   RefSeq; XP_010323166.1; XM_010324864.2.
DR   RefSeq; XP_010323167.1; XM_010324865.2.
DR   AlphaFoldDB; Q9FUZ0; -.
DR   SMR; Q9FUZ0; -.
DR   STRING; 4081.Q9FUZ0; -.
DR   PaxDb; 4081-Solyc07g015860-2-1; -.
DR   EnsemblPlants; Solyc07g015860.3.1; Solyc07g015860.3.1; Solyc07g015860.3.
DR   GeneID; 544225; -.
DR   Gramene; Solyc07g015860.3.1; Solyc07g015860.3.1; Solyc07g015860.3.
DR   KEGG; sly:544225; -.
DR   eggNOG; KOG3137; Eukaryota.
DR   HOGENOM; CLU_061901_5_0_1; -.
DR   InParanoid; Q9FUZ0; -.
DR   OMA; HLYYDHI; -.
DR   OrthoDB; 5472512at2759; -.
DR   PhylomeDB; Q9FUZ0; -.
DR   SABIO-RK; Q9FUZ0; -.
DR   Proteomes; UP000004994; Chromosome 7.
DR   GO; GO:0009570; C:chloroplast stroma; 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; IBA:GO_Central.
DR   GO; GO:0043686; P:co-translational protein 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; Peptide deformylase; 1.
DR   HAMAP; MF_00163; Pep_deformylase; 1.
DR   InterPro; IPR023635; Peptide_deformylase.
DR   InterPro; IPR036821; Peptide_deformylase_sf.
DR   NCBIfam; TIGR00079; pept_deformyl; 1.
DR   PANTHER; PTHR10458; PEPTIDE DEFORMYLASE; 1.
DR   PANTHER; PTHR10458:SF2; PEPTIDE DEFORMYLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01327; Pep_deformylase; 1.
DR   PRINTS; PR01576; PDEFORMYLASE.
DR   SUPFAM; SSF56420; Peptide deformylase; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Hydrolase; Metal-binding; Plastid; Protein biosynthesis;
KW   Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..277
FT                   /note="Peptide deformylase 1A, chloroplastic"
FT                   /id="PRO_0000006731"
FT   ACT_SITE        239
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   277 AA;  30986 MW;  5E8DB2C695AEBE52 CRC64;
     MMERFPRLAQ RVLSVPFTPK YLKSCKKTNP LTSHLMQLRG SQRPIFIQWN LQGRPSVCTD
     LISKKNYSSA TARAGWFLGL GEKKKQAMPD IVKAGDPVLH EPSQDIPLEE IGSERIQKII
     EEMVKVMRNA PGVGLAAPQI GIPLKIIVLE DTNEYISYAP KDETKAQDRR PFGLLVIINP
     KLKKKGNKTA LFFEGCLSVD GFRAVVERHL EVEVTGLDRN GKAIKVDASG WQARILQHEY
     DHLDGTLYVD KMAPRTFRTV ENLDLPLAAG CPKLGVC
//