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Q6G1G6 (DEF_BARQU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:BQ00690
OrganismBartonella quintana (strain Toulouse) (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier283165 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length176 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 – 176176Peptide deformylase HAMAP-Rule MF_00163
PRO_0000301008

Sites

Active site1371 By similarity
Metal binding941Iron By similarity
Metal binding1361Iron By similarity
Metal binding1401Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6G1G6 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 3702AEE7D95E08AC

FASTA17620,345
        10         20         30         40         50         60 
MPIKPLIILP DPILREVSKP VEHVDSTIQK LADDMLETMY DAQGVGLAAI QIGIPLRMLV 

        70         80         90        100        110        120 
IDVSRNETQK NPLVIINPEI LWLSDERNIC KEGCLSIPEY YTEIERPKRL CVRYQDREGK 

       130        140        150        160        170 
QTEIEADHLL ATCLQHEIDH LNGRLFIDHI SKIKRDMVIR KFKKRAKEKN AQEAIL 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897700 Genomic DNA. Translation: CAF25576.1.
RefSeqYP_031794.1. NC_005955.1.

3D structure databases

ProteinModelPortalQ6G1G6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283165.BQ00690.

Proteomic databases

PRIDEQ6G1G6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF25576; CAF25576; BQ00690.
GeneID2866415.
KEGGbqu:BQ00690.
PATRIC31951267. VBIBarQui58630_0077.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243509.
KOK01462.
OMAEETGEEW.
OrthoDBEOG664CMF.

Enzyme and pathway databases

BioCycBQUI283165:GHZA-69-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_BARQU
AccessionPrimary (citable) accession number: Q6G1G6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 19, 2004
Last modified: May 14, 2014
This is version 58 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