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Q88B43 (DEF1_PSESM) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 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:PSPTO_0177
OrganismPseudomonas syringae pv. tomato (strain DC3000) [Complete proteome] [HAMAP]
Taxonomic identifier223283 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length168 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 – 168168Peptide deformylase 1 HAMAP-Rule MF_00163
PRO_0000082822

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q88B43 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 04BA118A2ABF0B69

FASTA16819,185
        10         20         30         40         50         60 
MAILNILEFP DSRLRTLAKP VAMVDDGIRQ LVDDMFETMY EAPGIGLAAT QVNVHKRVVV 

        70         80         90        100        110        120 
MDLSEDRSAP MVFINPEIEK LTDEMDQYQE GCLSVPGFYE NVDRPQKVRV KALDRDGKPY 

       130        140        150        160 
ELVAEGLLAI CIQHECDHLN GKLFVDYLSN LKRDRIKKKL EKQHKLNA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016853 Genomic DNA. Translation: AAO53731.1.
RefSeqNP_790036.1. NC_004578.1.

3D structure databases

ProteinModelPortalQ88B43.
SMRQ88B43. Positions 1-165.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223283.PSPTO_0177.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO53731; AAO53731; PSPTO_0177.
GeneID1181785.
KEGGpst:PSPTO_0177.
PATRIC19991506. VBIPseSyr93040_0183.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243509.
KOK01462.
OMAELLAICI.
OrthoDBEOG664CMF.
PhylomeDBQ88B43.

Enzyme and pathway databases

BioCycPSYR223283:GJIX-176-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_PSESM
AccessionPrimary (citable) accession number: Q88B43
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: June 1, 2003
Last modified: July 9, 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