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Q5LEQ9 (DEF_BACFN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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

Short name=PDF
EC=3.5.1.88
Alternative name(s):
Polypeptide deformylase
Gene names
Name:def
Ordered Locus Names:BF1691
OrganismBacteroides fragilis (strain ATCC 25285 / NCTC 9343) [Complete proteome] [HAMAP]
Taxonomic identifier272559 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions 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

Sequence similarities

Belongs to the polypeptide deformylase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandIron
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functioniron ion binding

Inferred from electronic annotation. Source: InterPro

peptide deformylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 184184Peptide deformylase HAMAP-Rule MF_00163
PRO_0000301004

Sites

Active site1411 By similarity
Metal binding981Iron By similarity
Metal binding1401Iron By similarity
Metal binding1441Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5LEQ9 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: 1191336370789D37

FASTA18421,101
        10         20         30         40         50         60 
MILPIYVYGQ PVLRQVAEDI TVDYPNLKEL IENMFETMDH ADGVGLAAPQ IGLPIRVVVI 

        70         80         90        100        110        120 
NLDVLSEDYP EYKDFRKAYI NAHIDVVEGE EVSMEEGCLS LPGIHESVKR GSKIHVRYMD 

       130        140        150        160        170        180 
ENFVEHNEVV EGFLARVMQH EFDHLDGKMF IDHISPLRKQ MIKGKLNTML KGKARSSYKM 


KQVK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR626927 Genomic DNA. Translation: CAH07391.1.
RefSeqYP_211329.1. NC_003228.3.

3D structure databases

ProteinModelPortalQ5LEQ9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272559.BF1691.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH07391; CAH07391; BF9343_1610.
GeneID3285455.
KEGGbfs:BF1691.
PATRIC21039805. VBIBacFra29119_1650.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243509.
KOK01462.
OMAFSEGCLS.
OrthoDBEOG664CMF.
ProtClustDBPRK00150.

Enzyme and pathway databases

BioCycBFRA272559:GKF0-1625-MONOMER.

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]
PIRSFPIRSF004749. Pep_def. 1 hit.
PRINTSPR01576. PDEFORMYLASE.
SUPFAMSSF56420. SSF56420. 1 hit.
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDEF_BACFN
AccessionPrimary (citable) accession number: Q5LEQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 21, 2005
Last modified: February 19, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families