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Q9F2F0 (DEF_STRPN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 94. 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:SP_1456
OrganismStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) [Complete proteome] [HAMAP]
Taxonomic identifier170187 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length203 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 – 203203Peptide deformylase HAMAP-Rule MF_00163
PRO_0000082857

Sites

Active site1741 By similarity
Metal binding1301Iron By similarity
Metal binding1731Iron By similarity
Metal binding1771Iron By similarity

Secondary structure

................................ 203
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9F2F0 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 192F91B42375F8CD

FASTA20322,676
        10         20         30         40         50         60 
MSAIERITKA AHLIDMNDII REGNPTLRAI AEEVTFPLSD QEIILGEKMM QFLKHSQDPV 

        70         80         90        100        110        120 
MAEKMGLRGG VGLAAPQLDI SKRIIAVLVP NIVEEGETPQ EAYDLEAIMY NPKIVSHSVQ 

       130        140        150        160        170        180 
DAALGEGEGC LSVDRNVPGY VVRHARVTVD YFDKDGEKHR IKLKGYNSIV VQHEIDHING 

       190        200 
IMFYDRINEK DPFAVKDGLL ILE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ278785 Genomic DNA. Translation: CAC15392.1.
AE005672 Genomic DNA. Translation: AAK75550.1.
PIRE95169.
RefSeqNP_345910.1. NC_003028.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LM6X-ray1.75A1-203[»]
ProteinModelPortalQ9F2F0.
SMRQ9F2F0. Positions 2-203.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING170187.SP_1456.

Chemistry

ChEMBLCHEMBL2029196.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK75550; AAK75550; SP_1456.
GeneID931384.
KEGGspn:SP_1456.
PATRIC19707331. VBIStrPne105772_1508.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSPNE170187:GHGN-1462-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

EvolutionaryTraceQ9F2F0.

Entry information

Entry nameDEF_STRPN
AccessionPrimary (citable) accession number: Q9F2F0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: March 1, 2001
Last modified: February 19, 2014
This is version 94 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