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Q939R9 (Q939R9_STRPN) Unreviewed, UniProtKB/TrEMBL

Last modified October 19, 2011. Version 36. 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 3 HAMAP MF_00163
Short name=PDF 3 HAMAP MF_00163
EC=3.5.1.88 HAMAP MF_00163
Alternative name(s):
Polypeptide deformylase 3 HAMAP MF_00163
Gene names
Name:defB EMBL AAK13238.1
Synonyms:def3 HAMAP MF_00163
OrganismStreptococcus pneumoniae EMBL AAK13238.1
Taxonomic identifier1313 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length203 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 MF_00163

Catalytic activity

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

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 site1741 By similarity HAMAP MF_00163
Metal binding1301Iron By similarity HAMAP MF_00163
Metal binding1731Iron By similarity HAMAP MF_00163
Metal binding1771Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
Q939R9 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: E332956982A67161

FASTA20322,692
        10         20         30         40         50         60 
MSAIERITKA AHLIDMNDII REGNPTLRTV AEEVTFPLSD QEIILGEKMM QFLKHSQDPV 

        70         80         90        100        110        120 
MAEKMGLRGG VGLAAPQLDI SKRIIAVLVP NIVEEGETPQ EAYDLEAIMY NPKIVSHSVQ 

       130        140        150        160        170        180 
DAALGEGEGC LSVDRNVPGY VVRHARVTVD YFDKDGEKHR IKLKGYNSIV VQHEIDHING 

       190        200 
IMFYDRINEK DPFAVKDGLL ILE

« Hide

References

[1]"Resistance of Streptococcus pneumoniae to deformylase inhibitors is due to mutations in defB."
Margolis P., Hackbarth C., Lopez S., Maniar M., Wang W., Yuan Z., White R., Trias J.
Antimicrob. Agents Chemother. 45:2432-2435(2001) [PubMed: 11502510] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: R6x EMBL AAK13238.1.
[2]Margolis P.S., Hackbarth C.J., Lopez S., Maniar M., Wang W., Yuan Z., White R., Trias J.
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: R6x EMBL AAK13238.1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY014509 Genomic DNA. Translation: AAK13238.1.
PIRE98035.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3STRX-ray1.75P1-203[»]
3SVJX-ray1.55P1-203[»]
3SW8X-ray1.70P1-203[»]
ProteinModelPortalQ939R9.
SMRQ939R9. Positions 2-203.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
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 nameQ939R9_STRPN
AccessionPrimary (citable) accession number: Q939R9
Entry history
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: October 19, 2011
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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