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B0SQM2 (DEF_LEPBP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:LEPBI_I1573
OrganismLeptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris) [Complete proteome] [HAMAP]
Taxonomic identifier456481 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length179 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 – 179179Peptide deformylase HAMAP-Rule MF_00163
PRO_1000097322

Sites

Active site1461 By similarity
Metal binding1031Iron By similarity
Metal binding1451Iron By similarity
Metal binding1491Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
B0SQM2 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 50A5293F6C91CCE5

FASTA17920,479
        10         20         30         40         50         60 
MAVRKILKIG NPILRQTSED VSESEIQTKD FKKLIRDMFE TMRHADGVGL AAPQIGVLKK 

        70         80         90        100        110        120 
LVVVGQEDDN ERYPGTPEVP NQIILNPEIT PLSPPRDGFW EGCLSVPGMR GYVERPNKIR 

       130        140        150        160        170 
MKWRDENYVE HDEIIEGYRA IVLQHECDHL FGVLYVDRLK STKLFGYNED IDTAGKLLD 

« Hide

References

[1]"Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis."
Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A. expand/collapse author list , Davies J.K., Medigue C., Adler B.
PLoS ONE 3:E1607-E1607(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Patoc 1 / ATCC 23582 / Paris.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000786 Genomic DNA. Translation: ABZ97680.1.
RefSeqYP_001838956.1. NC_010602.1.

3D structure databases

ProteinModelPortalB0SQM2.
SMRB0SQM2. Positions 2-179.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING456481.LEPBI_I1573.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ97680; ABZ97680; LEPBI_I1573.
GeneID6222392.
KEGGlbi:LEPBI_I1573.
PATRIC22349946. VBILepBif123590_1608.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243508.
KOK01462.
OMALETMYQA.
OrthoDBEOG664CMF.
ProtClustDBPRK12846.

Enzyme and pathway databases

BioCycLBIF456481:GCM0-1556-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_LEPBP
AccessionPrimary (citable) accession number: B0SQM2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 43 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