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Q48661 (DEF_LACLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 99. 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:LL0560
ORF Names:L154885
OrganismLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) [Reference proteome] [HAMAP]
Taxonomic identifier272623 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length196 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.

Sequence caution

The sequence AAC41454.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAK04658.1 differs from that shown. Reason: Erroneous initiation.

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 – 196196Peptide deformylase HAMAP-Rule MF_00163
PRO_0000082792

Sites

Active site1671 By similarity
Metal binding1231Iron By similarity
Metal binding1661Iron By similarity
Metal binding1701Iron By similarity

Experimental info

Sequence conflict861D → E in AAC41454. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q48661 [UniParc].

Last modified April 27, 2001. Version 3.
Checksum: C5914BB3A92BF243

FASTA19622,047
        10         20         30         40         50         60 
MISMDDIIRE GYPTLREVAN DVTLPLSDED IILGEKMLQF LHNSQDPVMA EKMGLRGGVG 

        70         80         90        100        110        120 
LAANQLGLLK KVIAVLIPNE PEVDEDGNEI PPKEAYKMRE IMYNAKVVSH SVQDAAVEGG 

       130        140        150        160        170        180 
EGCLSVDREV PGYVVRHARV TVEYYNKEGE KKKIRLKDFP AICVQHEIDH TNGVMFYDHI 

       190 
NMNDPWEIKD GMIIVK 

« Hide

References

« Hide 'large scale' references
[1]"Lactococcus lactis glyceraldehyde-3-phosphate dehydrogenase gene, gap: further evidence for strongly biased codon usage in glycolytic pathway genes."
Cancilla M.R., Hillier A.J., Davidson B.E.
Microbiology 141:1027-1036(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LM0230.
[2]"The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403."
Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A.
Genome Res. 11:731-753(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IL1403.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L36907 Genomic DNA. Translation: AAC41454.1. Different initiation.
AE005176 Genomic DNA. Translation: AAK04658.1. Different initiation.
PIRH86694.
RefSeqNP_266716.1. NC_002662.1.

3D structure databases

ProteinModelPortalQ48661.
SMRQ48661. Positions 1-195.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272623.L154885.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK04658; AAK04658; L154885.
GeneID1114179.
KEGGlla:L154885.
PATRIC22293378. VBILacLac136773_0598.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243507.
KOK01462.
OMASQDPKIA.
OrthoDBEOG6PZXGQ.

Enzyme and pathway databases

BioCycLLAC272623:GHSH-617-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_LACLA
AccessionPrimary (citable) accession number: Q48661
Secondary accession number(s): Q9CI08
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 27, 2001
Last modified: May 14, 2014
This is version 99 of the entry and version 3 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