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Q9PK41 (DEF_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 86. 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:TC_0632
OrganismChlamydia muridarum (strain MoPn / Nigg) [Complete proteome] [HAMAP]
Taxonomic identifier243161 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length181 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 – 181181Peptide deformylase HAMAP-Rule MF_00163
PRO_0000082761

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q9PK41 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 5EB21D7C0A3995CA

FASTA18120,535
        10         20         30         40         50         60 
MIRDLEYYDS PILRKVAAPI DEITDELRQL VLDMSETMTF YKGVGLAAPQ VGHSVALFIM 

        70         80         90        100        110        120 
GVEKELDDGE LIFCDFPKVF INPVITQKSE QLVYGNEGCL SIPGLRGEVA RPDKITVTAK 

       130        140        150        160        170        180 
NLDGQPFSMT LEGFLARIVM HETDHLHGVL YIDRMSDKDK TKQFKNNLEK IRRKYSILRG 


L 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002160 Genomic DNA. Translation: AAF39461.1.
PIRC81680.
RefSeqNP_297006.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PK41.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243161.TC0632.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF39461; AAF39461; TC_0632.
GeneID1245992.
KEGGcmu:TC_0632.
PATRIC20372716. VBIChlMur19118_0671.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
KOK01462.
OMAFPARIVM.
OrthoDBEOG664CMF.

Enzyme and pathway databases

BioCycCMUR243161:GHYU-654-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_CHLMU
AccessionPrimary (citable) accession number: Q9PK41
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 86 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