Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A1KRE5 (DEF_NEIMF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:NMC0102
OrganismNeisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18) [Complete proteome] [HAMAP]
Taxonomic identifier272831 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length167 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
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 – 167167Peptide deformylase HAMAP-Rule MF_00163
PRO_0000301067

Sites

Active site1341 By similarity
Metal binding911Iron By similarity
Metal binding1331Iron By similarity
Metal binding1371Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
A1KRE5 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: F579BEAFD6AFA4B5

FASTA16719,115
        10         20         30         40         50         60 
MALLNILQYP DERLHTVAKP VEQVDERIRK LIADMFETMY ESRGIGLAAT QVDVHERVVV 

        70         80         90        100        110        120 
MDLTEDRSEP RVFINPVIVE KDGETTYEEG CLSVPGIYDT VTRAERVKVE ALNEKGEKFT 

       130        140        150        160 
LEADGLLAIC VQHELDHLMG IVFVERLSQL KQGRIKTKLK KRQKHTI 

« Hide

References

[1]"Meningococcal genetic variation mechanisms viewed through comparative analysis of serogroup C strain FAM18."
Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S., Quail M.A., Achtman M. expand/collapse author list , Barrell B.G., Saunders N.J., Parkhill J.
PLoS Genet. 3:230-240(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700532 / DSM 15464 / FAM18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM421808 Genomic DNA. Translation: CAM09421.1.
RefSeqYP_974233.1. NC_008767.1.

3D structure databases

ProteinModelPortalA1KRE5.
SMRA1KRE5. Positions 2-165.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272831.NMC0102.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM09421; CAM09421; NMC0102.
GeneID4675035.
KEGGnmc:NMC0102.
PATRIC20349695. VBINeiMen17609_0116.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243509.
KOK01462.
OMAELLAICI.
OrthoDBEOG664CMF.

Enzyme and pathway databases

BioCycNMEN272831:GJDX-100-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_NEIMF
AccessionPrimary (citable) accession number: A1KRE5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 51 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