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Q9KN16 (DEF2_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:VC_A0150
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length168 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. HAMAP-Rule MF_00163

Sequence similarities

Belongs to the polypeptide deformylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 168168Peptide deformylase 2 HAMAP-Rule MF_00163
PRO_0000082874

Sites

Active site1341 By similarity
Metal binding911Iron By similarity
Metal binding1331Iron By similarity
Metal binding1371Iron By similarity

Secondary structure

.......................... 168
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9KN16 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: F51EDDE3B6C14C59

FASTA16818,671
        10         20         30         40         50         60 
MAVLEILTAP DPRLRVQSKQ VTDVASVQTL IDDLLDTLYA TDNGIGLAAP QVGREEAIVV 

        70         80         90        100        110        120 
IDLSDNRDQP LVLINPKVVS GSNKEMGQEG CLSVPDYYAD VERYTSVVVE ALDREGKPLR 

       130        140        150        160 
IETSDFLAIV MQHEIDHLSG NLFIDYLSPL KQQMAMKKVK KHVKNRAR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003853 Genomic DNA. Translation: AAF96063.1.
PIRC82494.
RefSeqNP_232550.1. NC_002506.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QU1X-ray1.80A/B1-168[»]
ProteinModelPortalQ9KN16.
SMRQ9KN16. Positions 2-168.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VCA0150.

Protocols and materials databases

DNASU2612555.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF96063; AAF96063; VC_A0150.
GeneID2612555.
KEGGvch:VCA0150.
PATRIC20084873. VBIVibCho83274_2788.

Phylogenomic databases

eggNOGCOG0242.
KOK01462.
OMARIMVIDI.
OrthoDBEOG664CMF.
ProtClustDBPRK12846.

Enzyme and pathway databases

BioCycVCHO:VCA0150-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...

Other

EvolutionaryTraceQ9KN16.

Entry information

Entry nameDEF2_VIBCH
AccessionPrimary (citable) accession number: Q9KN16
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 76 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references