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Q3JR24 (Q3JR24_BURP1) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 41. 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 EMBL ABA47944.1
Synonyms:def2 HAMAP MF_00163
Ordered Locus Names:BURPS1710b_2587
OrganismBurkholderia pseudomallei (strain 1710b) [Complete proteome] [HAMAP] EMBL ABA47944.1
Taxonomic identifier320372 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei 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

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
Q3JR24 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 7FAC1DBE77F1D60F

FASTA17719,697
        10         20         30         40         50         60 
MIREILKMGD PRLLEVARPV EAFNTPELHA LVADMFETMH HANGAGLAAP QIGVGLQVII 

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

       130        140        150        160        170 
DQYGAKLERI AEGFHARVVQ HEYDHLIGKL YPMRITDFSK FGFADVLFPG LDAQADD 

« Hide

References

[1]Woods D.E., Nierman W.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 1710b EMBL ABA47944.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000124 Genomic DNA. Translation: ABA47944.1.
RefSeqYP_333979.1. NC_007434.1.

3D structure databases

ProteinModelPortalQ3JR24.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3JR24.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3690263.
GenomeReviewsGene locus BURPS1710b_2587 in contig CP000124_GR.
KEGGbpm:BURPS1710b_2587.
PATRIC19237686. VBIBurPse115837_2713.
TIGRBURPS1710b_2587.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMAPRFKHIC.
PhylomeDBQ3JR24.
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 nameQ3JR24_BURP1
AccessionPrimary (citable) accession number: Q3JR24
Entry history
Integrated into UniProtKB/TrEMBL: November 8, 2005
Last sequence update: November 8, 2005
Last modified: December 14, 2011
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)