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Protein

Peptide deformylase 1A, chloroplastic

Gene

PDF1A

Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Removes the formyl group from the N-terminal Met of newly synthesized proteins.By similarity

Catalytic activityi

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide.

Cofactori

Zn2+By similarityNote: Binds 1 Zn2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi196 – 1961ZincBy similarity
Metal bindingi238 – 2381ZincBy similarity
Active sitei239 – 2391By similarity
Metal bindingi242 – 2421ZincBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RKQ9FUZ0.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide deformylase 1A, chloroplastic (EC:3.5.1.88)
Short name:
PDF 1A
Alternative name(s):
Polypeptide deformylase
Gene namesi
Name:PDF1A
OrganismiSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifieri4081 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon
ProteomesiUP000004994 Componenti: Chromosome 7

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 277Peptide deformylase 1A, chloroplasticPRO_0000006731
Transit peptidei1 – ?ChloroplastSequence Analysis

Interactioni

Protein-protein interaction databases

STRINGi4081.Solyc07g015860.2.1.

Structurei

3D structure databases

ProteinModelPortaliQ9FUZ0.
SMRiQ9FUZ0. Positions 88-275.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiQ9FUZ0.
KOiK01462.
OMAiTFTNIHW.

Family and domain databases

Gene3Di3.90.45.10. 1 hit.
HAMAPiMF_00163. Pep_deformylase.
InterProiIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERiPTHR10458. PTHR10458. 1 hit.
PfamiPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PRINTSiPR01576. PDEFORMYLASE.
SUPFAMiSSF56420. SSF56420. 1 hit.
TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9FUZ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMERFPRLAQ RVLSVPFTPK YLKSCKKTNP LTSHLMQLRG SQRPIFIQWN
60 70 80 90 100
LQGRPSVCTD LISKKNYSSA TARAGWFLGL GEKKKQAMPD IVKAGDPVLH
110 120 130 140 150
EPSQDIPLEE IGSERIQKII EEMVKVMRNA PGVGLAAPQI GIPLKIIVLE
160 170 180 190 200
DTNEYISYAP KDETKAQDRR PFGLLVIINP KLKKKGNKTA LFFEGCLSVD
210 220 230 240 250
GFRAVVERHL EVEVTGLDRN GKAIKVDASG WQARILQHEY DHLDGTLYVD
260 270
KMAPRTFRTV ENLDLPLAAG CPKLGVC
Length:277
Mass (Da):30,986
Last modified:March 1, 2001 - v1
Checksum:i5E8DB2C695AEBE52
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF271258 mRNA. Translation: AAG33981.1.
RefSeqiNP_001234703.1. NM_001247774.1.
XP_010323165.1. XM_010324863.1.
XP_010323166.1. XM_010324864.1.
XP_010323167.1. XM_010324865.1.
UniGeneiLes.2897.

Genome annotation databases

EnsemblPlantsiSolyc07g015860.2.1; Solyc07g015860.2.1; Solyc07g015860.2.
GeneIDi544225.
KEGGisly:544225.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF271258 mRNA. Translation: AAG33981.1.
RefSeqiNP_001234703.1. NM_001247774.1.
XP_010323165.1. XM_010324863.1.
XP_010323166.1. XM_010324864.1.
XP_010323167.1. XM_010324865.1.
UniGeneiLes.2897.

3D structure databases

ProteinModelPortaliQ9FUZ0.
SMRiQ9FUZ0. Positions 88-275.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4081.Solyc07g015860.2.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiSolyc07g015860.2.1; Solyc07g015860.2.1; Solyc07g015860.2.
GeneIDi544225.
KEGGisly:544225.

Phylogenomic databases

InParanoidiQ9FUZ0.
KOiK01462.
OMAiTFTNIHW.

Enzyme and pathway databases

SABIO-RKQ9FUZ0.

Family and domain databases

Gene3Di3.90.45.10. 1 hit.
HAMAPiMF_00163. Pep_deformylase.
InterProiIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERiPTHR10458. PTHR10458. 1 hit.
PfamiPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PRINTSiPR01576. PDEFORMYLASE.
SUPFAMiSSF56420. SSF56420. 1 hit.
TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms."
    Giglione C., Serero A., Pierre M., Boisson B., Meinnel T.
    EMBO J. 19:5916-5929(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiDEF1A_SOLLC
AccessioniPrimary (citable) accession number: Q9FUZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: March 1, 2001
Last modified: June 24, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.