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Q147A5 (Q147A5_BURXL) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptide deformylase 1 HAMAP MF_00163

Short name=PDF 1 HAMAP MF_00163
EC=3.5.1.88 HAMAP MF_00163
Alternative name(s):
Polypeptide deformylase 1 HAMAP MF_00163
Gene names
Name:def1 HAMAP MF_00163
Ordered Locus Names:Bxeno_A0046
ORF Names:Bxe_A4416 EMBL ABE28584.1
OrganismBurkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP]
Taxonomic identifier266265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length167 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 MF_00163

Catalytic activity

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP MF_00163 SAAS SAAS000181

Cofactor

Binds 1 Fe2+ ion By similarity. HAMAP MF_00163

Sequence similarities

Belongs to the polypeptide deformylase family. HAMAP MF_00163 RuleBase RU003335

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1351 By similarity HAMAP MF_00163
Metal binding921Iron By similarity HAMAP MF_00163
Metal binding1341Iron By similarity HAMAP MF_00163
Metal binding1381Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
Q147A5 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 9D35727DAD3ACEF1

FASTA16719,017
        10         20         30         40         50         60 
MALLNIINYP DKRLHKIAKP VEAVNDRIRR LVKDMAETMY AAPGVGLAAT QVDVHERVIV 

        70         80         90        100        110        120 
IDVSDDHNEL LTFINPEIIW SSDERKLSEE GCLSVPGIYD NVERAEKVRV RALNEKGETF 

       130        140        150        160 
EMDCEGLLAV CIQHEMDHLM GRVFVEYLSS LKQTRIKSKM KKLAHAM 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000270 Genomic DNA. Translation: ABE28584.1.
RefSeqYP_556636.1. NC_007951.1.

3D structure databases

ProteinModelPortalQ147A5.
SMRQ147A5. Positions 2-164.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ147A5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4002024.
GenomeReviewsGene locus Bxeno_A0046 in contig CP000270_GR.
KEGGbxe:Bxe_A4416.
PATRIC19325409. VBIBurXen52548_0048.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG665227.
OMAGVLFVDY.
PhylomeDBQ147A5.
ProtClustDBPRK00150.

Family and domain databases

HAMAPMF_00163. Pep_deformylase.
[Tree]
InterProIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
Gene3DG3DSA:3.90.45.10. Fmet_deformylase. 1 hit.
KOK01462.
PANTHERPTHR10458. Fmet_deformylase. 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...

Entry information

Entry nameQ147A5_BURXL
AccessionPrimary (citable) accession number: Q147A5
Entry history
Integrated into UniProtKB/TrEMBL: August 22, 2006
Last sequence update: August 22, 2006
Last modified: December 14, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)