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B2SEJ9 (B2SEJ9_FRATM) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 24. 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 HAMAP MF_00163
Short name=PDF HAMAP MF_00163
EC=3.5.1.88 HAMAP MF_00163
Alternative name(s):
Polypeptide deformylase HAMAP MF_00163
Gene names
Name:def HAMAP MF_00163
Ordered Locus Names:FTM_0045
OrganismFrancisella tularensis subsp. mediasiatica (strain FSC147) [Complete proteome] [HAMAP]
Taxonomic identifier441952 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Francisellaceae › Francisella

Protein attributes

Sequence length172 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 site1371 By similarity HAMAP MF_00163
Metal binding941Iron By similarity HAMAP MF_00163
Metal binding1361Iron By similarity HAMAP MF_00163
Metal binding1401Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
B2SEJ9 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 8DB640B5F4A76FF1

FASTA17219,579
        10         20         30         40         50         60 
MSLEILKYPH PVLKEVAKEV TKDEINDDLR ATIAEMHELM LEANGVGLAA IQVGIKKRFF 

        70         80         90        100        110        120 
IMYDNLEEQN PEIITIINPE IIEQNGKIID EEGCLSFPGV SAKVNRATVV KIKALNEFGE 

       130        140        150        160        170 
EIEVEKDGFL ARCIQHEIDH LNGITFFDHL GSLKRKMIEK KYKKLMQENA KS

« Hide

References

[1]"Molecular evolutionary consequences of niche restriction in Francisella tularensis, a facultative intracellular pathogen."
Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T., Keim P., Johansson A.
PLoS Pathog. 5:E1000472-E1000472(2009) [PubMed: 19521508] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000915 Genomic DNA. Translation: ACD30158.1.
RefSeqYP_001890936.1. NC_010677.1.

3D structure databases

ProteinModelPortalB2SEJ9.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2SEJ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6290350.
GenomeReviewsGene locus FTM_0045 in contig CP000915_GR.
KEGGftm:FTM_0045.
PATRIC17954247. VBIFraTul67519_0058.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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 nameB2SEJ9_FRATM
AccessionPrimary (citable) accession number: B2SEJ9
Entry history
Integrated into UniProtKB/TrEMBL: July 1, 2008
Last sequence update: July 1, 2008
Last modified: December 14, 2011
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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