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Q8Y3B0 (DEF1_RALSO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. 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:RSc0070
ORF Names:RS02248
OrganismRalstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum) [Complete proteome] [HAMAP]
Taxonomic identifier267608 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia

Protein attributes

Sequence length169 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 – 169169Peptide deformylase 1 HAMAP-Rule MF_00163
PRO_0000082824

Sites

Active site1351 By similarity
Metal binding921Iron By similarity
Metal binding1341Iron By similarity
Metal binding1381Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8Y3B0 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: A72DFF47E1015E29

FASTA16919,425
        10         20         30         40         50         60 
MALLNILQYP DPRLHKVAKP VAVVDDRIRK LVADMAETMY DAPGIGLAAT QVDVHERVIT 

        70         80         90        100        110        120 
IDVSESRDEL RVFINPEIVW ASEARKVWDE GCLSVPDIYD KVERPDRVRV RALNEKGESF 

       130        140        150        160 
ELETDGLLAV CIQHEMDHLM GKVFVEYLSP LKQNRIKIKL KKHQLERAR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL646052 Genomic DNA. Translation: CAD13598.1.
RefSeqNP_518191.1. NC_003295.1.

3D structure databases

ProteinModelPortalQ8Y3B0.
SMRQ8Y3B0. Positions 2-169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267608.RSc0070.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD13598; CAD13598; RSc0070.
GeneID1218872.
KEGGrso:RSc0070.
PATRIC20258681. VBIRalSol70888_0076.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243509.
KOK01462.
OMAMAETMYE.
OrthoDBEOG664CMF.
ProtClustDBPRK00150.

Enzyme and pathway databases

BioCycRSOL267608:GCVU-70-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 nameDEF1_RALSO
AccessionPrimary (citable) accession number: Q8Y3B0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 70 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