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A0LEJ7 (DEF_SYNFM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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:Sfum_0147
OrganismSyntrophobacter fumaroxidans (strain DSM 10017 / MPOB) [Complete proteome] [HAMAP]
Taxonomic identifier335543 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophobacteraceaeSyntrophobacter

Protein attributes

Sequence length170 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 – 170170Peptide deformylase HAMAP-Rule MF_00163
PRO_0000301118

Sites

Active site1361 By similarity
Metal binding931Iron By similarity
Metal binding1351Iron By similarity
Metal binding1391Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
A0LEJ7 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: E2FA2CB48CDED105

FASTA17019,048
        10         20         30         40         50         60 
MAILDICTYP DPILRQKAAS VENIDEALIK LIDDMTETMY EAPGIGLAAN QVGRSLSLIV 

        70         80         90        100        110        120 
VDLQRQDEEH GLIVLINPQI VATQGEITWE EGCLSVPEYF SAVKRHAEVV VRGYGRDGKE 

       130        140        150        160        170 
MEIQAGGLLA VALQHEIDHL EGRLFIDRLN PITRDIFKRK WKKKLKEATA 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000478 Genomic DNA. Translation: ABK15849.1.
RefSeqYP_844284.1. NC_008554.1.

3D structure databases

ProteinModelPortalA0LEJ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335543.Sfum_0147.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK15849; ABK15849; Sfum_0147.
GeneID4461514.
KEGGsfu:Sfum_0147.
PATRIC23845143. VBISynFum78438_0172.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243509.
KOK01462.
OMALETMYQA.
OrthoDBEOG664CMF.
ProtClustDBPRK00150.

Enzyme and pathway databases

BioCycSFUM335543:GH6P-152-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_SYNFM
AccessionPrimary (citable) accession number: A0LEJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: December 12, 2006
Last modified: February 19, 2014
This is version 49 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