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Q88VB2 (DEF_LACPL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 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
Synonyms:def1
Ordered Locus Names:lp_2155
OrganismLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) [Reference proteome] [HAMAP]
Taxonomic identifier220668 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

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
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 – 186186Peptide deformylase HAMAP-Rule MF_00163
PRO_0000082793

Sites

Active site1571 By similarity
Metal binding1131Iron By similarity
Metal binding1561Iron By similarity
Metal binding1601Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q88VB2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: E080FF56D7723576

FASTA18620,855
        10         20         30         40         50         60 
MIKMRDIIRE GNHTLRAEAK QVKFPLSEAD QKLANDMMEY LENSQDPELA KKYGLRAGVG 

        70         80         90        100        110        120 
LAAPQVDVSE QMAAVLVPSE NEDDEPVFKD VIINPVIISH SVQPGALTEG EGCLSVDRDI 

       130        140        150        160        170        180 
AGYVIRHDRI TLRYYNMAGE EKKIRLKNYP AIVCQHEIDH LHGILFYDHI NGDNPFAADD 


DLVLIS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL935263 Genomic DNA. Translation: CCC79383.1.
RefSeqYP_004889897.1. NC_004567.2.

3D structure databases

ProteinModelPortalQ88VB2.
SMRQ88VB2. Positions 1-185.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220668.lp_2155.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCC79383; CCC79383; lp_2155.
GeneID1063706.
KEGGlpl:lp_2155.
PATRIC22250367. VBILacPla27411_1824.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243507.
KOK01462.
OMASQDPKIA.

Enzyme and pathway databases

BioCycLPLA220668-WGS:GSPK-1844-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_LACPL
AccessionPrimary (citable) accession number: Q88VB2
Secondary accession number(s): F9UQ94
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: June 1, 2003
Last modified: July 9, 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