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A5M878 (A5M878_STRPN) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 20. 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
ORF Names:CGSSp14BS69_03923 EMBL EDK66139.1
OrganismStreptococcus pneumoniae SP14-BS69 EMBL EDK66139.1
Taxonomic identifier406560 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length203 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 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
A5M878 [UniParc].

Last modified July 10, 2007. 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]Ehrlich G.D.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: SP14-BS69 EMBL EDK66139.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
ABAD01000006 Genomic DNA. Translation: EDK66139.1.

3D structure databases

ProteinModelPortalA5M878.
SMRA5M878. Positions 2-203.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC28648417. VBIStrPne72417_1263.

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 nameA5M878_STRPN
AccessionPrimary (citable) accession number: A5M878
Entry history
Integrated into UniProtKB/TrEMBL: July 10, 2007
Last sequence update: July 10, 2007
Last modified: December 14, 2011
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)