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A5EWL8 (DEF_DICNV) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:DNO_0156
OrganismDichelobacter nodosus (strain VCS1703A) [Complete proteome] [HAMAP]
Taxonomic identifier246195 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCardiobacterialesCardiobacteriaceaeDichelobacter

Protein attributes

Sequence length181 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 – 181181Peptide deformylase HAMAP-Rule MF_00163
PRO_0000301027

Sites

Active site1461 By similarity
Metal binding1031Iron By similarity
Metal binding1451Iron By similarity
Metal binding1491Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
A5EWL8 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 5B462AF9E02A7A4A

FASTA18120,521
        10         20         30         40         50         60 
MAIYSILIHP DPRLRLPAQP VTHFDDALAE IVQNMYETMY HFHGIGLAAP QVNIQQRLIV 

        70         80         90        100        110        120 
MDVPQRSAEE GEKAEQIPSD KLVLVNPEIV QRSEECQDYE EGCLSLPNQY ALVTRPANIT 

       130        140        150        160        170        180 
VRYQDITGAT QERAAQGLLS VCIQHEIDHL NGGLFIDHLS RLKRERLEKK LAKSLKNTKK 


S 

« Hide

References

[1]"Genome sequence and identification of candidate vaccine antigens from the animal pathogen Dichelobacter nodosus."
Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q., Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D., McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T., Fedorova N. expand/collapse author list , Khouri H., Bottomley S.P., Whittington R.J., Adler B., Songer J.G., Rood J.I., Paulsen I.T.
Nat. Biotechnol. 25:569-575(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VCS1703A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000513 Genomic DNA. Translation: ABQ13795.1.
RefSeqYP_001209086.1. NC_009446.1.

3D structure databases

ProteinModelPortalA5EWL8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246195.DNO_0156.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ13795; ABQ13795; DNO_0156.
GeneID5123335.
KEGGdno:DNO_0156.
PATRIC21784608. VBIDicNod48475_0156.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243509.
KOK01462.
OMAMAETMYE.
OrthoDBEOG664CMF.

Enzyme and pathway databases

BioCycDNOD246195:GHHS-156-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_DICNV
AccessionPrimary (citable) accession number: A5EWL8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 45 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