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A1V574 (A1V574_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 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-2 EMBL ABM52773.1
Synonyms:def1 HAMAP MF_00163
Ordered Locus Names:BMASAVP1_A2061
OrganismBurkholderia mallei (strain SAVP1) [Complete proteome] [HAMAP]
Taxonomic identifier320388 [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
A1V574 [UniParc].

Last modified February 6, 2007. 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]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: ABM52773.1.
RefSeqYP_993377.1. NC_008785.1.

3D structure databases

ProteinModelPortalA1V574.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1V574.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4680497.
GenomeReviewsGene locus BMASAVP1_A2061 in contig CP000526_GR.
KEGGbmv:BMASAVP1_A2061.
PATRIC19156849. VBIBurMal134057_3672.
TIGRBMASAVP1_A2061.

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 nameA1V574_BURMS
AccessionPrimary (citable) accession number: A1V574
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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