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Protein

Peptide deformylase

Gene

def

Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide.

Cofactori

Fe2+By similarityNote: Binds 1 Fe2+ ion.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi88IronBy similarity1
Metal bindingi130IronBy similarity1
Active sitei131By similarity1
Metal bindingi134IronBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide deformylase (EC:3.5.1.88)
Short name:
PDF
Alternative name(s):
Polypeptide deformylase
Gene namesi
Name:def
Ordered Locus Names:BB_0065
OrganismiBorrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Taxonomic identifieri224326 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesBorreliaceaeBorreliella
Proteomesi
  • UP000001807 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000827461 – 165Peptide deformylaseAdd BLAST165

Proteomic databases

PRIDEiO51092.

Interactioni

Protein-protein interaction databases

STRINGi224326.BB_0065.

Structurei

3D structure databases

ProteinModelPortaliO51092.
SMRiO51092.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.Curated

Phylogenomic databases

eggNOGiENOG4108Z02. Bacteria.
COG0242. LUCA.
KOiK01462.

Family and domain databases

CDDicd00487. Pep_deformylase. 1 hit.
Gene3Di3.90.45.10. 1 hit.
HAMAPiMF_00163. Pep_deformylase. 1 hit.
InterProiIPR023635. Peptide_deformylase.
[Graphical view]
PANTHERiPTHR10458. PTHR10458. 1 hit.
PfamiPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFiPIRSF004749. Pep_def. 1 hit.
PRINTSiPR01576. PDEFORMYLASE.
SUPFAMiSSF56420. SSF56420. 1 hit.
TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.

Sequencei

Sequence statusi: Complete.

O51092-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMVFYPNDL LRVKTKQIEN IDDKIRDYAK KMIELMDISG GVGLAAPQVG
60 70 80 90 100
LDLALFVVRE NKMARPLVFI NPSIIETSYE FSSYKEGCLS IPGVYYDLMR
110 120 130 140 150
PKAVVINFHD ENGKSFTIEN SDFLARIIQH EMDHLNGVLF IDYYEEKLKN
160
KLLKPYMRER GLKAK
Length:165
Mass (Da):19,116
Last modified:April 18, 2012 - v2
Checksum:i33959C6775C1AC32
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000783 Genomic DNA. Translation: AAC66445.2.
PIRiA70108.
RefSeqiNP_212199.2. NC_001318.1.
WP_002662034.1. NC_001318.1.

Genome annotation databases

EnsemblBacteriaiAAC66445; AAC66445; BB_0065.
GeneIDi1194901.
KEGGibbu:BB_0065.
PATRICi20556735. VBIBorBur75917_0463.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000783 Genomic DNA. Translation: AAC66445.2.
PIRiA70108.
RefSeqiNP_212199.2. NC_001318.1.
WP_002662034.1. NC_001318.1.

3D structure databases

ProteinModelPortaliO51092.
SMRiO51092.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224326.BB_0065.

Proteomic databases

PRIDEiO51092.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC66445; AAC66445; BB_0065.
GeneIDi1194901.
KEGGibbu:BB_0065.
PATRICi20556735. VBIBorBur75917_0463.

Phylogenomic databases

eggNOGiENOG4108Z02. Bacteria.
COG0242. LUCA.
KOiK01462.

Family and domain databases

CDDicd00487. Pep_deformylase. 1 hit.
Gene3Di3.90.45.10. 1 hit.
HAMAPiMF_00163. Pep_deformylase. 1 hit.
InterProiIPR023635. Peptide_deformylase.
[Graphical view]
PANTHERiPTHR10458. PTHR10458. 1 hit.
PfamiPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFiPIRSF004749. Pep_def. 1 hit.
PRINTSiPR01576. PDEFORMYLASE.
SUPFAMiSSF56420. SSF56420. 1 hit.
TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDEF_BORBU
AccessioniPrimary (citable) accession number: O51092
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: April 18, 2012
Last modified: November 2, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.