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Q8Y866 (DEF_LISMO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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:lmo1051
OrganismListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]
Taxonomic identifier169963 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length183 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
Reference 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 – 183183Peptide deformylase HAMAP-Rule MF_00163
PRO_0000082798

Sites

Active site1541 By similarity
Metal binding1101Iron By similarity
Metal binding1531Iron By similarity
Metal binding1571Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8Y866 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 65B2430603CDA4EF

FASTA18320,643
        10         20         30         40         50         60 
MLTMDDIVRE GHPALREVAT EVTFPLSDEE KKLGRDMLEF LINSQDEDLA EKYGLRGGVG 

        70         80         90        100        110        120 
IAAPQLAVTK RFLAIHVHDE KDRLYSYVLY NPKIRSHSVQ QACLSGGEGC LSVDREVPGY 

       130        140        150        160        170        180 
VVRSERVTID AFDENGTPLK LRFKGYPAIV IQHEIDHLNG IMFYDHINKE NPSYLPPDVD 


VFG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL591977 Genomic DNA. Translation: CAC99129.1.
PIRAC1206.
RefSeqNP_464576.1. NC_003210.1.

3D structure databases

ProteinModelPortalQ8Y866.
SMRQ8Y866. Positions 1-178.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING169963.lmo1051.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC99129; CAC99129; CAC99129.
GeneID986625.
KEGGlmo:lmo1051.
PATRIC20311205. VBILisMon69206_1080.

Organism-specific databases

GenoListLMO1051.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243507.
KOK01462.
OMAHIDKENP.
OrthoDBEOG6PZXGQ.
ProtClustDBPRK00150.

Enzyme and pathway databases

BioCycLMON169963:LMO1051-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_LISMO
AccessionPrimary (citable) accession number: Q8Y866
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 69 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