DEF1A_SOLLC
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 03-AUG-2022, entry version 114.
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.Solyc07g015860.2.1; -.
DR PaxDb; Q9FUZ0; -.
DR PRIDE; Q9FUZ0; -.
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; CRSIRFP; -.
DR OrthoDB; 1532656at2759; -.
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:0031365; P:N-terminal protein amino acid modification; IBA:GO_Central.
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; 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
