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Q5M6B0 (DEF_STRT2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:stu0151
OrganismStreptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) [Complete proteome] [HAMAP]
Taxonomic identifier264199 [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_0000301111

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q5M6B0 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 0E3CA97B1C7E7ADA

FASTA20422,777
        10         20         30         40         50         60 
MDAQTKIIRA SHMIDMNDII REGNPTLRAV AEDVTLPLSD EDIILGEKMM QFLRNSQDPV 

        70         80         90        100        110        120 
IAEKMGLRGG VGLAAPQLDI SKRIIAVLVP NPEDAKGNPP KEAYSLQEIM YNPKVVAHSV 

       130        140        150        160        170        180 
QEAALGNGEG CLSVDRDVPG YVVRHARVTI EYFNKEGEKK RIKLRGYDSI VVQHEIDHTN 

       190        200 
GIMFYDRINK DNPFTIKDGL LIIE 

« Hide

References

[1]"Complete sequence and comparative genome analysis of the dairy bacterium Streptococcus thermophilus."
Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D., Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D., Hancy F. expand/collapse author list , Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.
Nat. Biotechnol. 22:1554-1558(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-250 / LMG 18311.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000023 Genomic DNA. Translation: AAV59876.1.
RefSeqYP_138691.1. NC_006448.1.

3D structure databases

ProteinModelPortalQ5M6B0.
SMRQ5M6B0. Positions 3-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264199.stu0151.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV59876; AAV59876; stu0151.
GeneID3163998.
KEGGstl:stu0151.
PATRIC19801870. VBIStrThe97850_0157.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSTHE264199:GI6K-202-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_STRT2
AccessionPrimary (citable) accession number: Q5M6B0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 1, 2005
Last modified: February 19, 2014
This is version 57 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