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Reviewed, UniProtKB/Swiss-Prot Q9FUZ0 (DEF1A_SOLLC)

Last modified February 9, 2010. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptide deformylase 1A, chloroplastic
      Short name=PDF 1A
    EC=3.5.1.88
Alternative name(s):
    Polypeptide deformylase
Gene names
Name: PDF1A
OrganismSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 Zinc ion per subunit By similarity.

Subcellular location

Plastidchloroplast stroma By similarity.

Sequence similarities

Belongs to the polypeptide deformylase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological processtranslation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast stroma

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioniron ion binding

Inferred from electronic annotation. Source: InterPro

peptide deformylase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Chloroplast Potential
Chain? – 277Peptide deformylase 1A, chloroplasticPRO_0000006731

Sites

Active site2391 By similarity
Metal binding1961Zinc By similarity
Metal binding2381Zinc By similarity
Metal binding2421Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9FUZ0-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 5E8DB2C695AEBE52

FASTA27730,986
        10         20         30         40         50         60 
MMERFPRLAQ RVLSVPFTPK YLKSCKKTNP LTSHLMQLRG SQRPIFIQWN LQGRPSVCTD 

        70         80         90        100        110        120 
LISKKNYSSA TARAGWFLGL GEKKKQAMPD IVKAGDPVLH EPSQDIPLEE IGSERIQKII 

       130        140        150        160        170        180 
EEMVKVMRNA PGVGLAAPQI GIPLKIIVLE DTNEYISYAP KDETKAQDRR PFGLLVIINP 

       190        200        210        220        230        240 
KLKKKGNKTA LFFEGCLSVD GFRAVVERHL EVEVTGLDRN GKAIKVDASG WQARILQHEY 

       250        260        270 
DHLDGTLYVD KMAPRTFRTV ENLDLPLAAG CPKLGVC 

« Hide

References

[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: 11060042] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF271258 mRNA. Translation: AAG33981.1.
UniGeneLes.2897

3D structure databases

SMRQ9FUZ0. Positions 88-275.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.5.1.88. 281054.

Family and domain databases

InterProIPR000181. Fmet_deformylase.
[Graphical view]
Gene3DG3DSA:3.90.45.10. Fmet_deformylase. 1 hit.
PANTHERPTHR10458. Fmet_deformylase. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PRINTSPR01576. PDEFORMYLASE.
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDEF1A_SOLLC
AccessionPrimary (citable) accession number: Q9FUZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: March 1, 2001
Last modified: February 9, 2010
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents