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Q886I1 (DEF2_PSESM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. 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 2

Short name=PDF 2
EC=3.5.1.88
Alternative name(s):
Polypeptide deformylase 2
Gene names
Name:def2
Ordered Locus Names:PSPTO_1598
OrganismPseudomonas syringae pv. tomato (strain DC3000) [Complete proteome] [HAMAP]
Taxonomic identifier223283 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length179 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 – 179179Peptide deformylase 2 HAMAP-Rule MF_00163
PRO_0000082823

Sites

Active site1441 By similarity
Metal binding1011Iron By similarity
Metal binding1431Iron By similarity
Metal binding1471Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q886I1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 7CD70D0ACA744A98

FASTA17920,051
        10         20         30         40         50         60 
MIRNILKMGD ERLLRIAPPV PAEMFGSSEL ETLIADMFET MHSVGGVGLA APQIGIDLQL 

        70         80         90        100        110        120 
VIFGFERSER YPQAEAVPQT ILLNPLITPL HPGVEEGWEG CLSVPGLRGM VDRYQSIRYE 

       130        140        150        160        170 
GFDPDGQPIE RIAHGFHARV VQHECDHLIG RLYPSRITDF SKFGFMDVMF PDMDPNADE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016853 Genomic DNA. Translation: AAO55118.1.
RefSeqNP_791423.1. NC_004578.1.

3D structure databases

ProteinModelPortalQ886I1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223283.PSPTO_1598.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO55118; AAO55118; PSPTO_1598.
GeneID1183235.
KEGGpst:PSPTO_1598.
PATRIC19994442. VBIPseSyr93040_1622.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243508.
KOK01462.
OMARVCQVGD.
OrthoDBEOG664CMF.
ProtClustDBPRK12846.

Enzyme and pathway databases

BioCycPSYR223283:GJIX-1627-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 nameDEF2_PSESM
AccessionPrimary (citable) accession number: Q886I1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 73 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