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Q9FV54 (DEF1B_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptide deformylase 1B, chloroplastic

Short name=PDF 1B
EC=3.5.1.88
Alternative name(s):
Polypeptide deformylase
Gene names
Name:PDF1B
OrganismSolanum lycopersicum (Tomato) (Lycopersicon esculentum) [Reference proteome]
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon

Protein attributes

Sequence length279 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. HAMAP-Rule MF_00163

Catalytic activity

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP-Rule MF_00163

Cofactor

Binds 1 Fe2+ ion By similarity. HAMAP-Rule MF_00163

Subcellular location

Plastidchloroplast Potential HAMAP-Rule MF_00163.

Sequence similarities

Belongs to the polypeptide deformylase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandIron
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchloroplast

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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Chloroplast Potential
Chain? – 279Peptide deformylase 1B, chloroplastic HAMAP-Rule MF_00163PRO_0000006733

Sites

Active site2201 By similarity
Metal binding1771Iron By similarity
Metal binding2191Iron By similarity
Metal binding2231Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9FV54 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 750F6406FDAC4233

FASTA27931,197
        10         20         30         40         50         60 
MAMAAASWAS SSSFTRFLRP LLSRNSSPSP ISYSLHRYKS ANCLFFSASS NKPPKLAVYA 

        70         80         90        100        110        120 
QARRVLSSKT KGDEIATPAD LSFVVPLKIV EYPDPILRAK NKRIDNFDAN LKKLVDEMFD 

       130        140        150        160        170        180 
IMYKTDGIGL SAPQVGMNVQ LMVFNAAGER GEGEEIVLVN PRVSRYSRRI IPYEEGCLSF 

       190        200        210        220        230        240 
PMIHGDVKRP ESVKVDAQDI NGTRFEISLS ALPARVFQHE FDHLQGVLFF DKMTDEVLDT 

       250        260        270 
IREKLVALEK KYEDRTGLPT PESINTRKIK KAAVGFGKS 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF250958 mRNA. Translation: AAG33972.1.
RefSeqNP_001234441.1. NM_001247512.1.
UniGeneLes.3729.

3D structure databases

ProteinModelPortalQ9FV54.
SMRQ9FV54. Positions 80-262.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsSolyc02g086680.2.1; Solyc02g086680.2.1; Solyc02g086680.2.
GeneID543648.
KEGGsly:543648.

Phylogenomic databases

KOK01462.

Enzyme and pathway databases

SABIO-RKQ9FV54.

Family and domain databases

Gene3D3.90.45.10. 1 hit.
HAMAPMF_00163. Pep_deformylase.
InterProIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERPTHR10458. PTHR10458. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PRINTSPR01576. PDEFORMYLASE.
SUPFAMSSF56420. SSF56420. 1 hit.
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDEF1B_SOLLC
AccessionPrimary (citable) accession number: Q9FV54
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: March 1, 2001
Last modified: March 19, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families