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A0Q456 (A0Q456_FRATN) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 32. 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:FTN_0110
OrganismFrancisella tularensis subsp. novicida (strain U112) [Complete proteome] [HAMAP]
Taxonomic identifier401614 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length174 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 site1391 By similarity HAMAP MF_00163
Metal binding961Iron By similarity HAMAP MF_00163
Metal binding1381Iron By similarity HAMAP MF_00163
Metal binding1421Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
A0Q456 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 74C7E633F5AF7D74

FASTA17419,798
        10         20         30         40         50         60 
MNMSLEILKY PHPVLKEVAK EVTKDEINDD LRATIAEMHE LMLEANGVGL AAIQVGIKKR 

        70         80         90        100        110        120 
FFIMYDNLEE QNPKIITIIN PEIIEQSGKI IDEEGCLSFP GVSAKVNRAT TVKIKALNEF 

       130        140        150        160        170 
GDEIEIEKDG FLARCIQHEI DHLNGITFFD HLGSLKRKMI EKKYKKLMQE NAKS 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000439 Genomic DNA. Translation: ABK89021.1.
RefSeqYP_897775.1. NC_008601.1.

3D structure databases

ProteinModelPortalA0Q456.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0Q456.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4547768.
GenomeReviewsGene locus FTN_0110 in contig CP000439_GR.
KEGGftn:FTN_0110.
PATRIC17933261. VBIFraNov128299_0114.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMAEMTELMI.
ProtClustDBCLSK935135.

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 nameA0Q456_FRATN
AccessionPrimary (citable) accession number: A0Q456
Entry history
Integrated into UniProtKB/TrEMBL: January 9, 2007
Last sequence update: January 9, 2007
Last modified: December 14, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)