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Q9RD27 (DEF1_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. 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 1

Short name=PDF 1
EC=3.5.1.88
Alternative name(s):
Polypeptide deformylase 1
Gene names
Name:def1
Ordered Locus Names:SCO0883
ORF Names:SCM1.16
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group

Protein attributes

Sequence length218 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 – 218218Peptide deformylase 1 HAMAP-Rule MF_00163
PRO_0000082852

Sites

Active site1691 By similarity
Metal binding1261Iron By similarity
Metal binding1681Iron By similarity
Metal binding1721Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RD27 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 7F45248A0797288D

FASTA21823,198
        10         20         30         40         50         60 
MGTPSDRVPL AERVEELLAV GGPLPIVAAG DPVLRRAAEP YDGQVAPALF ERFVEALRLT 

        70         80         90        100        110        120 
MHAAPGVGLA APQVGVGLRV AVIEDPAPVP DEVRVARGRV PQPFRVLVNP SYEPAGAGRA 

       130        140        150        160        170        180 
AFFEGCLSVP GWQAVVARHA EVRLRAHDEH GRAVDEVFAG WPARIVQHET DHLDGTLYLD 

       190        200        210 
RAELRSLASN AAMAELWSQP TPRRAASALG FELPGPAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939107 Genomic DNA. Translation: CAB62674.1.
RefSeqNP_625182.1. NC_003888.3.

3D structure databases

ProteinModelPortalQ9RD27.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO0883.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB62674; CAB62674; CAB62674.
GeneID1096306.
KEGGsco:SCO0883.
PATRIC23731304. VBIStrCoe124346_0874.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243508.
KOK01462.
OMAGWQARIV.
OrthoDBEOG664CMF.
PhylomeDBQ9RD27.

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.
ProtoNetSearch...

Entry information

Entry nameDEF1_STRCO
AccessionPrimary (citable) accession number: Q9RD27
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 75 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