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A8LE21 (DEF_FRASN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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:Franean1_1718
OrganismFrankia sp. (strain EAN1pec) [Complete proteome] [HAMAP]
Taxonomic identifier298653 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeFrankiaceaeFrankia

Protein attributes

Sequence length183 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 – 183183Peptide deformylase HAMAP-Rule MF_00163
PRO_1000097312

Sites

Active site1331 By similarity
Metal binding901Iron By similarity
Metal binding1321Iron By similarity
Metal binding1361Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
A8LE21 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 8F991F00211F4169

FASTA18320,091
        10         20         30         40         50         60 
MSVRDIRLLG DPVLRTVADP VATFDRELRR LVDDLADTMR DAGGVGLAAP QLGVSLRIFT 

        70         80         90        100        110        120 
YLDDSDEVGH LINPVLGPFS EEMMDGEEGC LSLPGLAFDL RRPERVLAVG QNSHGDPVTV 

       130        140        150        160        170        180 
EGSGILSRCL QHETDHLDGI LFIDRLDKET KRAAMKAIRE AEWSNEPKPA VKVSPHPLFG 


RGR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000820 Genomic DNA. Translation: ABW11156.1.
RefSeqYP_001506062.1. NC_009921.1.

3D structure databases

ProteinModelPortalA8LE21.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING298653.Franean1_1718.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW11156; ABW11156; Franean1_1718.
GeneID5670120.
KEGGfre:Franean1_1718.
PATRIC21936300. VBIFraSp51419_1763.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243508.
KOK01462.
OMAMEMVFYP.
OrthoDBEOG664CMF.

Enzyme and pathway databases

BioCycFSP298653:GHPI-1734-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_FRASN
AccessionPrimary (citable) accession number: A8LE21
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 4, 2007
Last modified: May 14, 2014
This is version 43 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