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Q3JXE2 (Q3JXE2_BURP1) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 40. 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:def1 HAMAP MF_00163
Ordered Locus Names:BURPS1710b_0346
OrganismBurkholderia pseudomallei (strain 1710b) [Complete proteome] [HAMAP] EMBL ABA48414.1
Taxonomic identifier320372 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length201 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 site1691 By similarity HAMAP MF_00163
Metal binding1261Iron By similarity HAMAP MF_00163
Metal binding1681Iron By similarity HAMAP MF_00163
Metal binding1721Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
Q3JXE2 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: DA14B2C2FDF16A05

FASTA20122,745
        10         20         30         40         50         60 
MARVVESILR PARASRQSAE RPMRAGRSSP DTEIMALLNI LHYPDKRLHK VAKPVAKVDD 

        70         80         90        100        110        120 
RIRKLVADMA ETMYAAPGIG LAATQVDVHE RVIVIDVSED KNELRVFINP EIVWTGDGKQ 

       130        140        150        160        170        180 
VYEEGCLSVP GVYDEVERPD RVRVRALDGQ GEPFELDCEG LLAVCIQHEM DHLMGRVFVQ 

       190        200 
YLSPLKQTRI KTKMKKLERA M

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References

[1]Woods D.E., Nierman W.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 1710b EMBL ABA48414.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000124 Genomic DNA. Translation: ABA48414.1.
RefSeqYP_331761.2. NC_007434.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ3JXE2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3689602.
GenomeReviewsGene locus BURPS1710b_0346 in contig CP000124_GR.
KEGGbpm:BURPS1710b_0346.
PATRIC19232912. VBIBurPse115837_0348.
TIGRBURPS1710b_0346.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMAPEQSHEI.
PhylomeDBQ3JXE2.
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 nameQ3JXE2_BURP1
AccessionPrimary (citable) accession number: Q3JXE2
Entry history
Integrated into UniProtKB/TrEMBL: November 8, 2005
Last sequence update: November 8, 2005
Last modified: December 14, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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