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A6L7J9 (DEF_BACV8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:BVU_4061
OrganismBacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154) [Complete proteome] [HAMAP]
Taxonomic identifier435590 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length184 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 – 184184Peptide deformylase HAMAP-Rule MF_00163
PRO_0000301005

Sites

Active site1411 By similarity
Metal binding981Iron By similarity
Metal binding1401Iron By similarity
Metal binding1441Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
A6L7J9 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: B9E1607904FC722B

FASTA18421,019
        10         20         30         40         50         60 
MILPIYVYGQ PVLRKEAEDI TPDYPNLKEL IANMFETMNR ADGVGLAAPQ IGLPIRVVTI 

        70         80         90        100        110        120 
DLDVMSDDLP EFKDFRRAYI NPHILEVGGE EVSMEEGCLS LPGIHEAVKR PDRIHVTYLD 

       130        140        150        160        170        180 
EELKEHDEWV EGYLARVMQH EFDHLDGKMF IDHLSALRKQ MIKGKLGAML KGKARCSYKV 


KTIK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000139 Genomic DNA. Translation: ABR41663.1.
RefSeqYP_001301285.1. NC_009614.1.

3D structure databases

ProteinModelPortalA6L7J9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING435590.BVU_4061.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR41663; ABR41663; BVU_4061.
GeneID5305020.
KEGGbvu:BVU_4061.
PATRIC21073220. VBIBacVul85104_4171.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243509.
KOK01462.
OMAEETGEEW.
OrthoDBEOG664CMF.

Enzyme and pathway databases

BioCycBVUL435590:GH96-4051-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_BACV8
AccessionPrimary (citable) accession number: A6L7J9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 24, 2007
Last modified: May 14, 2014
This is version 47 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