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P94601 (DEF_MICDP) 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
OrganismMicrochaete diplosiphon (Fremyella diplosiphon)
Taxonomic identifier1197 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesMicrochaetaceaeMicrochaete

Protein attributes

Sequence length187 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
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 – 187187Peptide deformylase HAMAP-Rule MF_00163
PRO_0000082783

Sites

Active site1501 By similarity
Metal binding1071Iron By similarity
Metal binding1491Iron By similarity
Metal binding1531Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
P94601 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: B58EC9BAA0EBF299

FASTA18720,938
        10         20         30         40         50         60 
MPSEIAVEKK KLKNPPLQLH YLGDRVLRQP AKRIAKVDDE LRQLIRDMLQ TMYSKDGIGL 

        70         80         90        100        110        120 
AAPQVGIHKQ LIVIDLEPDN PANPPLVLIN PTIKQVSKEI CVAQEGCLSI PNVYMDVKRP 

       130        140        150        160        170        180 
EVVEIAYKDE NGRPKTLKAT DLLARCIQHE MDHLNGVVFV DRVDNSLTLA QELSKNGFSY 


QAVKPVA 

« Hide

References

[1]"A survey of polypeptide deformylase function throughout the eubacterial lineage."
Mazel D., Coic E., Blanchard S., Saurin W., Marliere P.
J. Mol. Biol. 266:939-949(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y10305 Genomic DNA. Translation: CAA71353.1.

3D structure databases

ProteinModelPortalP94601.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_MICDP
AccessionPrimary (citable) accession number: P94601
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
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