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Q823U4 (DEF_CHLCV) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. 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:CCA_00311
OrganismChlamydophila caviae (strain GPIC) [Complete proteome] [HAMAP]
Taxonomic identifier227941 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length186 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 – 186186Peptide deformylase HAMAP-Rule MF_00163
PRO_0000082760

Sites

Active site1421 By similarity
Metal binding991Iron By similarity
Metal binding1411Iron By similarity
Metal binding1451Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q823U4 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 0E12811C80B8F806

FASTA18621,149
        10         20         30         40         50         60 
MIRELEYYGS HILRRKADII PEITDATRQL VQDMYETMVA HKGVGLAAPQ VGESLSLFVM 

        70         80         90        100        110        120 
CVEGETEEGD LIFCDFPKVY INPVLSNPSE DLVIGREGCL SIPGLRADVY RPQSITVTAV 

       130        140        150        160        170        180 
NLDGQEFTEH LEGFPARIIM HENDHLHGVL YIDKMEEPKD IKKFKASLEK IRRRYHAHVK 


PEDRAS 

« Hide

References

[1]"Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae."
Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G. expand/collapse author list , Rank R.G., Bavoil P.M., Fraser C.M.
Nucleic Acids Res. 31:2134-2147(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GPIC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015925 Genomic DNA. Translation: AAP05060.1.
RefSeqNP_829182.1. NC_003361.3.

3D structure databases

ProteinModelPortalQ823U4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227941.CCA00311.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP05060; AAP05060; CCA_00311.
GeneID1217996.
KEGGcca:CCA00311.
PATRIC20269676. VBIChlCav107360_0336.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
KOK01462.
OMAMFVAVEY.
OrthoDBEOG664CMF.
ProtClustDBPRK00150.

Enzyme and pathway databases

BioCycCCAV227941:GH8L-326-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_CHLCV
AccessionPrimary (citable) accession number: Q823U4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 67 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