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A2S8G8 (A2S8G8_BURM9) 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:def-1 EMBL ABN03203.1
Synonyms:def1 HAMAP MF_00163
Ordered Locus Names:BMA10229_A2274
OrganismBurkholderia mallei (strain NCTC 10229) [Complete proteome] [HAMAP]
Taxonomic identifier412022 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length216 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 site1841 By similarity HAMAP MF_00163
Metal binding1411Iron By similarity HAMAP MF_00163
Metal binding1831Iron By similarity HAMAP MF_00163
Metal binding1871Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
A2S8G8 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: CBB4E90B22962975

FASTA21624,472
        10         20         30         40         50         60 
MRTGPRRLAD HCDARMARVV ESILRPARAS RQSAERPMRA GRSSPDTEIM ALLNILHYPD 

        70         80         90        100        110        120 
KRLHKVAKPV AKVDDRIRKL VADMAETMYA APGIGLAATQ VDVHERVIVI DVSEDKNELR 

       130        140        150        160        170        180 
VFINPEIVWT GDGKQVYEEG CLSVPGVYDE VERPDRVRVR ALDGQGESFE LDCEGLLAVC 

       190        200        210 
IQHEMDHLMG RVFVQYLSPL KQTRIKTKMK KLERAM

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000546 Genomic DNA. Translation: ABN03203.1.
RefSeqYP_001028237.1. NC_008836.1.

3D structure databases

ProteinModelPortalA2S8G8.
SMRA2S8G8. Positions 50-214.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2S8G8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4793913.
GenomeReviewsGene locus BMA10229_A2274 in contig CP000546_GR.
KEGGbml:BMA10229_A2274.
PATRIC19135526. VBIBurMal46188_4468.
TIGRBMA10229_A2274.

Phylogenomic databases

HOGENOMHBG665227.
OMAPEQSHEI.
PhylomeDBA2S8G8.
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 nameA2S8G8_BURM9
AccessionPrimary (citable) accession number: A2S8G8
Entry history
Integrated into UniProtKB/TrEMBL: March 6, 2007
Last sequence update: March 6, 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)
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