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A1V798 (A1V798_BURMS) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 30. 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-1 EMBL ABM52027.1
Synonyms:def2 HAMAP MF_00163
Ordered Locus Names:BMASAVP1_A2806
OrganismBurkholderia mallei (strain SAVP1) [Complete proteome] [HAMAP]
Taxonomic identifier320388 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length167 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 site1351 By similarity HAMAP MF_00163
Metal binding921Iron By similarity HAMAP MF_00163
Metal binding1341Iron By similarity HAMAP MF_00163
Metal binding1381Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
A1V798 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: F1D525AB88D989A7

FASTA16718,971
        10         20         30         40         50         60 
MALLNILHYP DKRLHKVAKP VAKVDDRIRK LVADMAETMY AAPGIGLAAT QVDVHERVIV 

        70         80         90        100        110        120 
IDVSEDKNEL RVFINPEIVW TGDGKQVYEE GCLSVPGVYD EVERPDRVRV RALDGQGESF 

       130        140        150        160 
ELDCEGLLAV CIQHEMDHLM GRVFVQYLSP LKQTRIKTKM KKLERAM

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000526 Genomic DNA. Translation: ABM52027.1.
RefSeqYP_994101.1. NC_008785.1.

3D structure databases

ProteinModelPortalA1V798.
SMRA1V798. Positions 1-165.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1V798.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4679555.
GenomeReviewsGene locus BMASAVP1_A2806 in contig CP000526_GR.
KEGGbmv:BMASAVP1_A2806.
PATRIC19158325. VBIBurMal134057_4395.
TIGRBMASAVP1_A2806.

Phylogenomic databases

HOGENOMHBG665227.
OMAGVLFVDY.
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 nameA1V798_BURMS
AccessionPrimary (citable) accession number: A1V798
Entry history
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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