Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q6FDC9 (Q6FDC9_ACIAD) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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:def2 HAMAP MF_00163 EMBL CAG67929.1
Ordered Locus Names:ACIAD1039
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP] EMBL CAG67929.1
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length160 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 site1461 By similarity HAMAP MF_00163
Metal binding1031Iron By similarity HAMAP MF_00163
Metal binding1451Iron By similarity HAMAP MF_00163
Metal binding1491Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
Q6FDC9 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: FF9F20442EA84DA1

FASTA16018,156
        10         20         30         40         50         60 
MSTVLTVAKR GEEILKLNAA PVSEQEFDSE WLQQLVKAMQ ATMLERNGVG IAAPQIYVSK 

        70         80         90        100        110        120 
RIMIVASRPN PRYPDAPEMQ PVVMINPEIT HFSFEKELGE EGCLSVPDQR GQVERAQSID 

       130        140        150        160 
VRYFSLQGQL IEQRFHGFPA RIVQHEIDHL NGVLFVDRLI 

« Hide

References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ADP1 EMBL CAG67929.1.
[2]Genoscope
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ADP1 EMBL CAG67929.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR543861 Genomic DNA. Translation: CAG67929.1.
RefSeqYP_045751.1. NC_005966.1.

3D structure databases

ProteinModelPortalQ6FDC9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6FDC9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2881098.
GenomeReviewsGene locus ACIAD1039 in contig CR543861_GR.
KEGGaci:ACIAD1039.
NMPDRfig|62977.3.peg.1136.
PATRIC20739934. VBIAciSp98416_0931.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMAYISKRII.
PhylomeDBQ6FDC9.
ProtClustDBCLSK707175.

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 nameQ6FDC9_ACIAD
AccessionPrimary (citable) accession number: Q6FDC9
Entry history
Integrated into UniProtKB/TrEMBL: July 19, 2004
Last sequence update: July 19, 2004
Last modified: December 14, 2011
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)