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Q9RRQ4 (DEF_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. 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:DR_2434
OrganismDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]
Taxonomic identifier243230 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length232 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 – 232232Peptide deformylase HAMAP-Rule MF_00163
PRO_0000082778

Sites

Active site1791 By similarity
Metal binding1351Iron By similarity
Metal binding1781Iron By similarity
Metal binding1821Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RRQ4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 94A31686AE872ED8

FASTA23226,369
        10         20         30         40         50         60 
MTAPDSSSAP APLAFGGKPR VYPMRLYGDP ILRRKARNLT AADTLHVPGF EPQTVREVAD 

        70         80         90        100        110        120 
TMLETMFEER GVGLAAPQIG LPVRMFVAVE YADDEEENEG QETPLRSRVL REYVMLNPVV 

       130        140        150        160        170        180 
KVINKKKDKS YQEGCLSIPG IYEDGVPRAR QVRVDYTDLD GQPRSIEAED YLARVFQHET 

       190        200        210        220        230 
DHLDGKLFLD HLPADITEDH RKDLLRIQQA SKNFLAQLSE WDKAQRHLKE NL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000513 Genomic DNA. Translation: AAF11975.1.
PIRH75274.
RefSeqNP_296154.1. NC_001263.1.

3D structure databases

ProteinModelPortalQ9RRQ4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243230.DR_2434.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF11975; AAF11975; DR_2434.
GeneID1797596.
KEGGdra:DR_2434.
PATRIC21632586. VBIDeiRad64572_2669.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243509.
KOK01462.
OMAMFVAVEY.
OrthoDBEOG664CMF.
ProtClustDBPRK14596.

Enzyme and pathway databases

BioCycDRAD243230:GH46-2483-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_DEIRA
AccessionPrimary (citable) accession number: Q9RRQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 81 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