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A3NQ22 (A3NQ22_BURP0) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 34. 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 EMBL ABN90331.1
Synonyms:def1 HAMAP MF_00163
Ordered Locus Names:BURPS1106A_0159
OrganismBurkholderia pseudomallei (strain 1106a) [Complete proteome] [HAMAP]
Taxonomic identifier357348 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length179 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 site1471 By similarity HAMAP MF_00163
Metal binding1041Iron By similarity HAMAP MF_00163
Metal binding1461Iron By similarity HAMAP MF_00163
Metal binding1501Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
A3NQ22 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 868147C8C26F905B

FASTA17920,283
        10         20         30         40         50         60 
MRAGRSSPDT EIMALLNILH YPDKRLHKVA KPVAKVDDRI RKLVADMAET MYAAPGIGLA 

        70         80         90        100        110        120 
ATQVDVHERV IVIDVSEDKN ELRVFINPEI VWTGDGKQVY EEGCLSVPGV YDEVERPDRV 

       130        140        150        160        170 
RVRALDGQGE PFELDCEGLL AVCIQHEMDH LMGRVFVQYL SPLKQTRIKT KMKKLERAM 

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References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000572 Genomic DNA. Translation: ABN90331.1.
RefSeqYP_001064443.1. NC_009076.1.

3D structure databases

ProteinModelPortalA3NQ22.
SMRA3NQ22. Positions 13-177.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3NQ22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4899509.
GenomeReviewsGene locus BURPS1106A_0159 in contig CP000572_GR.
KEGGbpl:BURPS1106A_0159.
PATRIC19218923. VBIBurPse14980_0149.
TIGRBURPS1106A_0159.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMAPEQSHEI.
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 nameA3NQ22_BURP0
AccessionPrimary (citable) accession number: A3NQ22
Entry history
Integrated into UniProtKB/TrEMBL: April 3, 2007
Last sequence update: April 3, 2007
Last modified: December 14, 2011
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)