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Reviewed, UniProtKB/Swiss-Prot Q819K2 (DEF2_BACCR)

Last modified November 3, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: BC_3974
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Complete proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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.

Catalytic activity

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP MF_00163

Cofactor

Binds 1 Fe2+ ion By similarity.

Sequence similarities

Belongs to the polypeptide deformylase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandIron
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processtranslation

Inferred from electronic annotation. Source: HAMAP

   Molecular functioniron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptide deformylase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 184184Peptide deformylase 2 HAMAP MF_00163
PRO_0000082736

Sites

Active site1541 By similarity
Metal binding1101Iron By similarity
Metal binding1531Iron By similarity
Metal binding1571Iron By similarity

Secondary structure

........................... 184
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q819K2-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 8B4E1CBE1CACA1F1

FASTA18420,474
        10         20         30         40         50         60 
MLTMKDVIRE GDPILRNVAE EVSLPASEED TTTLKEMIEF VINSQDPEMA EKYSLRPGIG 

        70         80         90        100        110        120 
LAAPQIGVSK KMIAVHVTDA DGTLYSHALF NPKIISHSVE RTYLQGGEGC LSVDREVPGY 

       130        140        150        160        170        180 
VPRYTRITVK ATSINGEEVK LRLKGLPAIV FQHEIDHLNG VMFYDHINKE NPFAAPDDSK 


PLER 

« Hide

Cross-references

Sequence databases

AE016877 Genomic DNA. Translation: AAP10894.1.
RefSeqNP_833693.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2OKLX-ray1.70A/B1-184[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ819K2.

Genome annotation databases

GeneID1206319.
GenomeReviewsGene locus BC_3974 in contig AE016877_GR.
KEGGbce:BC3974.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ819K2.
OMADDSKPLE.

Enzyme and pathway databases

BioCycBCER226900:BC_3974-MON.

Family and domain databases

HAMAPMF_00163.
[Tree]
InterProIPR000181. Fmet_deformylase.
[Graphical view]
Gene3DG3DSA:3.90.45.10. Fmet_deformylase. 1 hit.
PANTHERPTHR10458. Fmet_deformylase. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFPIRSF004749. Pep_def. 1 hit.
PRINTSPR01576. PDEFORMYLASE.
ProDomPD003844. Fmet_deformylase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDEF2_BACCR
AccessionPrimary (citable) accession number: Q819K2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents