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Q9KVU3 (DEF1_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. 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 1
Short name=PDF 1
EC=3.5.1.88
Alternative name(s):
Polypeptide deformylase 1
Gene names
Name:def1
Ordered Locus Names:VC_0046
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio ›

Protein attributes

Sequence length169 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 – 169169Peptide deformylase 1 HAMAP-Rule MF_00163
PRO_0000082873

Sites

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

Secondary structure

1 .......................... 169
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9KVU3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 16DB00B08CA40FC7

FASTA16919,147
        10         20         30         40         50         60 
MSVLQVLTFP DDRLRTVAKP VEQVTPEIQQ IVDDMLETMY AEEGIGLAAT QVDIHQRIVV 

        70         80         90        100        110        120 
IDISETRDQP MVLINPEIIE KRGEDGIEEG CLSVPGARAL VPRAAEVTVK ALDRNGQEYQ 

       130        140        150        160 
FDADDLLAIC VQHELDHLAG KLFVDYLSPL KRNRIKEKLE KIKRFNEKK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE003852 Genomic DNA. Translation: AAF93224.1.
PIRA82373.
RefSeqNP_229705.1. NC_002505.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FWXX-ray2.00A/B1-169[»]
ProteinModelPortalQ9KVU3.
SMRQ9KVU3. Positions 2-168.
ModBaseSearch...

Protein-protein interaction databases

STRING243277.VC0046.

Protocols and materials databases

DNASU2614445.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF93224; AAF93224; VC_0046.
GeneID2614445.
KEGGvch:VC0046.
PATRIC20079140. VBIVibCho83274_0045.

Phylogenomic databases

eggNOGCOG0242.
KOK01462.
OMAEMDQYQE.
ProtClustDBPRK00150.

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

EvolutionaryTraceQ9KVU3.

Entry information

Entry nameDEF1_VIBCH
AccessionPrimary (citable) accession number: Q9KVU3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: October 1, 2000
Last modified: May 1, 2013
This is version 78 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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