Skip Header

Contribute Send feedback
Read comments (?) or add your own

B5E5U9 (DEF_STRP4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 32. 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
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:SPG_1382
OrganismStreptococcus pneumoniae serotype 19F (strain G54) [Complete proteome] [HAMAP]
Taxonomic identifier512566 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length203 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.

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: HAMAP

   Molecular_functioniron ion binding

Inferred from electronic annotation. Source: InterPro

peptide deformylase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 203203Peptide deformylase HAMAP-Rule MF_00163
PRO_1000097348

Sites

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

Sequences

Sequence LengthMass (Da)Tools
B5E5U9 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: 138F8EC89BDC55B8

FASTA20322,729
        10         20         30         40         50         60 
MSAIERITKA AHLIDMNDII REGNPTLRAI AEKVTFPLSD QEIILGEKMM QFLKHSQDPV 

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

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

       190        200 
IMFYDRINEK DPFAVKDGLL ILE

« Hide

References

[1]"Annotated draft genomic sequence from a Streptococcus pneumoniae type 19F clinical isolate."
Dopazo J., Mendoza A., Herrero J., Caldara F., Humbert Y., Friedli L., Guerrier M., Grand-Schenk E., Gandin C., de Francesco M., Polissi A., Buell G., Feger G., Garcia E., Peitsch M., Garcia-Bustos J.F.
Microb. Drug Resist. 7:99-125(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G54.
[2]"Pneumococcal beta glucoside metabolism investigated by whole genome comparison."
Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G., Davidsen T.M., Tettelin H., Oggioni M.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G54.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001015 Genomic DNA. Translation: ACF55009.1.
RefSeqYP_002038089.1. NC_011072.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING512566.SPG_1382.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF55009; ACF55009; SPG_1382.
GeneID6480157.
KEGGspx:SPG_1382.
PATRIC19688389. VBIStrPne77426_1445.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243507.
KOK01462.
OMALTSGEGC.
ProtClustDBPRK00150.

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. Fmet_deformylase. 1 hit.
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDEF_STRP4
AccessionPrimary (citable) accession number: B5E5U9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 14, 2008
Last modified: May 1, 2013
This is version 32 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents