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Q8G487 (DEF2_BIFLO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 63. 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 2

Short name=PDF 2
EC=3.5.1.88
Alternative name(s):
Polypeptide deformylase 2
Gene names
Name:def2
Ordered Locus Names:BL1502
OrganismBifidobacterium longum (strain NCC 2705) [Reference proteome] [HAMAP]
Taxonomic identifier206672 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length162 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
Reference 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 – 162162Peptide deformylase 2 HAMAP-Rule MF_00163
PRO_0000082743

Sites

Active site1311 By similarity
Metal binding881Iron By similarity
Metal binding1301Iron By similarity
Metal binding1341Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8G487 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 932A148E88547D53

FASTA16218,369
        10         20         30         40         50         60 
MAIREIRVVP DPVLRTPCDE IKEITPAVRR LVDDLLETVD DPGRAGLSAN QIGVSLRAFS 

        70         80         90        100        110        120 
YNIDGKVGYV LNPVLEEKSG EQYGDEGCLS VPGLWYKTRR ADYARVRGID LDGNEVVLEG 

       130        140        150        160 
SGLMGRMLQH ECDHLDGHVY LDRLEKEERR EALRYMRNRQ AK 

« Hide

References

[1]"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract."
Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.
Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCC 2705.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014295 Genomic DNA. Translation: AAN25297.1.
RefSeqNP_696661.1. NC_004307.2.

3D structure databases

ProteinModelPortalQ8G487.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING206672.BL1502.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN25297; AAN25297; BL1502.
GeneID1021664.
KEGGblo:BL1502.
PATRIC21117791. VBIBifLon107831_0374.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243508.
KOK01462.
OMAYVINPRI.
OrthoDBEOG664CMF.
PhylomeDBQ8G487.

Enzyme and pathway databases

BioCycBLON206672:GI1E-342-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 nameDEF2_BIFLO
AccessionPrimary (citable) accession number: Q8G487
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 63 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