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Q0VTE1 (DEF_ALCBS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. 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:ABO_0131
OrganismAlcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]
Taxonomic identifier393595 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesAlcanivoracaceaeAlcanivorax

Protein attributes

Sequence length168 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 – 168168Peptide deformylase HAMAP-Rule MF_00163
PRO_0000301000

Sites

Active site1351 By similarity
Metal binding921Iron By similarity
Metal binding1341Iron By similarity
Metal binding1381Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0VTE1 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: E8218549ECA87A58

FASTA16819,284
        10         20         30         40         50         60 
MAKLEILEFP DPRLRTVAKP VEKVDDELRK LIDDMFETMY AAPGIGLAAT QVDVHIQLIV 

        70         80         90        100        110        120 
MDLSEDHNKP MVFINPQITP LTEEQAPYEE GCLSVPGFYE KVTRPARVRI NALDRDGNAF 

       130        140        150        160 
EVEADELLAT CIQHEMDHLD GKLFVDYVSR LKRDRIKKKL EKIHRQQG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286690 Genomic DNA. Translation: CAL15579.1.
RefSeqYP_691851.1. NC_008260.1.

3D structure databases

ProteinModelPortalQ0VTE1.
SMRQ0VTE1. Positions 1-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393595.ABO_0131.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL15579; CAL15579; ABO_0131.
GeneID4212211.
KEGGabo:ABO_0131.
PATRIC20837843. VBIAlcBor124741_0139.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243509.
KOK01462.
OMAELLAICI.
OrthoDBEOG664CMF.

Enzyme and pathway databases

BioCycABOR393595:GHRI-131-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_ALCBS
AccessionPrimary (citable) accession number: Q0VTE1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 5, 2006
Last modified: May 14, 2014
This is version 55 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