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Q8EHZ2 (DEF2_SHEON) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 71. 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:SO_1062
OrganismShewanella oneidensis (strain MR-1) [Reference proteome] [HAMAP]
Taxonomic identifier211586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length181 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 – 181181Peptide deformylase 2 HAMAP-Rule MF_00163
PRO_0000082835

Sites

Active site1521 By similarity
Metal binding1091Iron By similarity
Metal binding1511Iron By similarity
Metal binding1551Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8EHZ2 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: BF5C27BADEA587C2

FASTA18120,325
        10         20         30         40         50         60 
MFKDEMRQTP NKPLPIAVVG EAILKQQAIE VRDFDDTLSQ LASQMAASMV EAKGVGIAAP 

        70         80         90        100        110        120 
QVHSPLALFI MASRPNERYP DAPLMEPLVV VNPQIVLRSL QLEKGEEGCL SVPGQRFTIW 

       130        140        150        160        170        180 
RPQTIVVRYQ NLAGQWQHSE LTGFIARIFQ HEFDHLQGIT LLERSQMPEQ KLMAQEGKPQ 


A 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014299 Genomic DNA. Translation: AAN54134.1.
RefSeqNP_716689.1. NC_004347.2.

3D structure databases

ProteinModelPortalQ8EHZ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING211586.SO_1062.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN54134; AAN54134; SO_1062.
GeneID1168899.
KEGGson:SO_1062.
PATRIC23521771. VBISheOne101494_1019.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243508.
KOK01462.
OMAERSQMPE.
OrthoDBEOG664CMF.
PhylomeDBQ8EHZ2.

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_SHEON
AccessionPrimary (citable) accession number: Q8EHZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 71 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