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O51092 (DEF_BORBU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:BB_0065
OrganismBorrelia burgdorferi (Lyme disease spirochete)
Taxonomic identifier139 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length172 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 MF_00163

Catalytic activity

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP MF_00163

Cofactor

Binds 1 Fe2+ ion By similarity. HAMAP MF_00163

Sequence similarities

Belongs to the polypeptide deformylase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandIron
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processtranslation

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioniron ion binding

Inferred from electronic annotation. Source: InterPro

peptide deformylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 172172Peptide deformylase HAMAP MF_00163
PRO_0000082746

Sites

Active site1381 By similarity
Metal binding951Iron By similarity
Metal binding1371Iron By similarity
Metal binding1411Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
O51092 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 26C211EA57F25DA6

FASTA17219,922
        10         20         30         40         50         60 
MKGGWVFMEM VFYPNDLLRV KTKQIENIDD KIRDYAKKMI ELMDISGGVG LAAPQVGLDL 

        70         80         90        100        110        120 
ALFVVRENKM ARPLVFINPS IIETSYEFSS YKEGCLSIPG VYYDLMRPKA VVINFHDENG 

       130        140        150        160        170 
KSFTIENSDF LARIIQHEMD HLNGVLFIDY YEEKLKNKLL KPYMRERGLK AK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000783 Genomic DNA. Translation: AAC66445.1.
PIRA70108.
RefSeqNP_212199.1. NC_001318.1.

3D structure databases

ProteinModelPortalO51092.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBORT00000008621; EBBORP00000007951; EBBORG00000008620.
GeneID1194901.
GenomeReviewsGene locus BB_0065 in contig AE000783_GR.
KEGGbbu:BB0065.
NMPDRfig|224326.1.peg.449.
PATRIC20556735. VBIBorBur75917_0463.
TIGRBB_0065.

Phylogenomic databases

GeneTreeEBGT00050000007440.
HOGENOMHBG665227.
OMAALANDMM.
PhylomeDBO51092.
ProtClustDBPRK00150.

Enzyme and pathway databases

BioCycBBUR224326:BB_0065-MONOMER.

Family and domain databases

HAMAPMF_00163. Pep_deformylase.
[Tree]
InterProIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
Gene3DG3DSA:3.90.45.10. Fmet_deformylase. 1 hit.
KOK01462.
PANTHERPTHR10458. Fmet_deformylase. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFPIRSF004749. Pep_def. 1 hit.
PRINTSPR01576. PDEFORMYLASE.
SUPFAMSSF56420. Fmet_deformylase. 1 hit.
TIGRFAMsTIGR00079. Pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDEF_BORBU
AccessionPrimary (citable) accession number: O51092
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: January 25, 2012
This is version 78 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

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