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Q819K2 (DEF2_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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) [Reference proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group ›

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
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. 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.

Sequence similarities

Belongs to the polypeptide deformylase family.

Ontologies

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

Inferred from electronic annotation. Source: HAMAP

   Molecular_functioniron ion binding

Inferred from electronic annotation. Source: InterPro

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-Rule MF_00163
PRO_0000082736

Sites

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

Secondary structure

1 ........................... 184
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q819K2 [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

EMBL
GenBank
DDBJ		AE016877 Genomic DNA. Translation: AAP10894.1.
RefSeqNP_833693.1. NC_004722.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OKLX-ray1.70A/B1-184[»]
ProteinModelPortalQ819K2.
SMRQ819K2. Positions 1-184.
ModBaseSearch...

Protein-protein interaction databases

STRING226900.BC3974.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP10894; AAP10894; BC_3974.
GeneID1206319.
KEGGbce:BC3974.
PATRIC32603994. VBIBacCer54481_4100.

Phylogenomic databases

eggNOGCOG0242.
KOK01462.
OMALTSGEGC.
ProtClustDBPRK00150.

Enzyme and pathway databases

BioCycBCER226900:GJEU-3970-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. Fmet_deformylase. 1 hit.
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ819K2.

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: May 1, 2013
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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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