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A2SB67 (A2SB67_BURM9) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 31. 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 2 HAMAP MF_00163
Short name=PDF 2 HAMAP MF_00163
EC=3.5.1.88 HAMAP MF_00163
Alternative name(s):
Polypeptide deformylase 2 HAMAP MF_00163
Gene names
Name:def-2 EMBL ABN03373.1
Synonyms:def2 HAMAP MF_00163
Ordered Locus Names:BMA10229_A3250
OrganismBurkholderia mallei (strain NCTC 10229) [Complete proteome] [HAMAP]
Taxonomic identifier412022 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length177 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 site1421 By similarity HAMAP MF_00163
Metal binding991Iron By similarity HAMAP MF_00163
Metal binding1411Iron By similarity HAMAP MF_00163
Metal binding1451Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
A2SB67 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: E5CC1DA29903CAE1

FASTA17719,711
        10         20         30         40         50         60 
MIREILKMGD PRLLEVARPV EAFNTPELHA LVADMFETMH HANGAGLAAP QIGVGLQVII 

        70         80         90        100        110        120 
FGFGSSERYP EAPPVPETVL VNPSIEYLPP DLEEGWEGCL SLPGLRGVVS RYRRVRYSGF 

       130        140        150        160        170 
DQYGAKLERI AEGFHARVVQ HEYDHLIGKL YPMRITDFSK FGFADVLFPG LDAQADD

« 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: ABN03373.1.
RefSeqYP_001029186.1. NC_008836.1.

3D structure databases

ProteinModelPortalA2SB67.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2SB67.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4792997.
GenomeReviewsGene locus BMA10229_A3250 in contig CP000546_GR.
KEGGbml:BMA10229_A3250.
PATRIC19137516. VBIBurMal46188_5443.
TIGRBMA10229_A3250.

Phylogenomic databases

HOGENOMHBG665227.
OMAPRFKHIC.
ProtClustDBPRK12846.

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 nameA2SB67_BURM9
AccessionPrimary (citable) accession number: A2SB67
Entry history
Integrated into UniProtKB/TrEMBL: March 6, 2007
Last sequence update: March 6, 2007
Last modified: December 14, 2011
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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