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P68771 (DEF_STRP1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:SPy_1958, M5005_Spy1669
OrganismStreptococcus pyogenes serotype M1 [Complete proteome] [HAMAP]
Taxonomic identifier301447 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete 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_0000082859

Sites

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

Secondary structure

............................... 204
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P68771 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 89F8EDE94D94DC05

FASTA20422,862
        10         20         30         40         50         60 
MSAQDKLIKP SHLITMDDII REGNPTLRAV AKEVSLPLCD EDILLGEKMM QFLKHSQDPV 

        70         80         90        100        110        120 
MAEKLGLRAG VGLAAPQIDV SKRIIAVLVP NLPDKEGNPP KEAYSWQEVL YNPKIVSHSV 

       130        140        150        160        170        180 
QDAALSDGEG CLSVDRVVEG YVVRHARVTV DYYDKEGQQH RIKLKGYNAI VVQHEIDHIN 

       190        200 
GVLFYDRINA KNPFETKEEL LILD 

« Hide

References

[1]"Complete genome sequence of an M1 strain of Streptococcus pyogenes."
Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K., Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P., Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L. expand/collapse author list , White J., Yuan X., Clifton S.W., Roe B.A., McLaughlin R.E.
Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700294 / SF370 / Serotype M1.
[2]"Evolutionary origin and emergence of a highly successful clone of serotype M1 group A Streptococcus involved multiple horizontal gene transfer events."
Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K., Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P., Musser J.M.
J. Infect. Dis. 192:771-782(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-947 / MGAS5005 / Serotype M1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004092 Genomic DNA. Translation: AAK34651.1.
CP000017 Genomic DNA. Translation: AAZ52287.1.
RefSeqNP_269930.1. NC_002737.1.
YP_283032.1. NC_007297.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OS3X-ray2.26A2-204[»]
ProteinModelPortalP68771.
SMRP68771. Positions 2-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING160490.SPy_1958.

Proteomic databases

PaxDbP68771.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK34651; AAK34651; SPy_1958.
AAZ52287; AAZ52287; M5005_Spy1669.
GeneID3571223.
901633.
KEGGspy:SPy_1958.
spz:M5005_Spy_1669.
PATRIC19717319. VBIStrPyo79812_1705.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSPYO160490:GJ81-1613-MONOMER.
SPYO293653:GHFC-1748-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...

Other

EvolutionaryTraceP68771.

Entry information

Entry nameDEF_STRP1
AccessionPrimary (citable) accession number: P68771
Secondary accession number(s): P82590, Q48WI8, Q99XY7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: December 21, 2004
Last modified: February 19, 2014
This is version 67 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references