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C0MFA6 (DEF_STRS7) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. 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:SZO_02070
OrganismStreptococcus equi subsp. zooepidemicus (strain H70) [Complete proteome] [HAMAP]
Taxonomic identifier553483 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length204 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 – 204204Peptide deformylase HAMAP-Rule MF_00163
PRO_1000203607

Sites

Active site1751 By similarity
Metal binding1311Iron By similarity
Metal binding1741Iron By similarity
Metal binding1781Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
C0MFA6 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: E0BA0325CD631DEF

FASTA20422,851
        10         20         30         40         50         60 
MSAQDKLIKA QHLIDMNDII REGNPTLRAV AKEVEFPLSD DDIILGEKMM QFLKHSQDPV 

        70         80         90        100        110        120 
MGEKLGLRAG VGLAAPQIDV SKRIIAVLVP NPEDSEGNPP KEAYSMEEVL YNPKIVSHSV 

       130        140        150        160        170        180 
QDAALADGEG CLSVDRVVEG YVVRHARVTV EYYDKHNEKH RIKLKGYNAI VVQHEIDHIN 

       190        200 
GVLFYDRINA KKPFEAKEGM LILE 

« Hide

References

[1]"Genomic evidence for the evolution of Streptococcus equi: host restriction, increased virulence, and genetic exchange with human pathogens."
Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F., Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M., Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A. expand/collapse author list , Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C., Maskell D.J., Parkhill J., Waller A.S.
PLoS Pathog. 5:E1000346-E1000346(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: H70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM204884 Genomic DNA. Translation: CAW97934.1.
RefSeqYP_002743768.1. NC_012470.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING553483.SZO_02070.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAW97934; CAW97934; SZO_02070.
GeneID7695160.
KEGGseq:SZO_02070.
PATRIC19650000. VBIStrEqu35012_0228.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243507.
KOK01462.
OMAHIDKENP.
OrthoDBEOG6PZXGQ.
ProtClustDBPRK00150.

Enzyme and pathway databases

BioCycSEQU40041:GC8B-250-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_STRS7
AccessionPrimary (citable) accession number: C0MFA6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 5, 2009
Last modified: February 19, 2014
This is version 37 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