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A6V966 (A6V966_PSEA7) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 29. 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:def1 EMBL ABR80933.1
Synonyms:def2 HAMAP MF_00163
Ordered Locus Names:PSPA7_4247
OrganismPseudomonas aeruginosa (strain PA7) [Complete proteome] [HAMAP]
Taxonomic identifier381754 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

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 site1441 By similarity HAMAP MF_00163
Metal binding1011Iron By similarity HAMAP MF_00163
Metal binding1431Iron By similarity HAMAP MF_00163
Metal binding1471Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
A6V966 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 1984F1A6BADEBBC7

FASTA17920,039
        10         20         30         40         50         60 
MIREILKMGD ERLLRIAPPV PAESFGSQEL QRLIDDMFET MRHVGGVGLA APQIGVDLQL 

        70         80         90        100        110        120 
VIFGFERSER YPDAPAVPPT ILLNPRITAL DDEIEEGWEG CLSVPGLRGM VPRHRRIRYQ 

       130        140        150        160        170 
GVDPQGKPID RSVEGFHARV VQHECDHLIG RLYPSRITDF GKFGFTEVLF PGLDPAADD 

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References

[1]Dodson R.J., Harkins D., Paulsen I.T.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000744 Genomic DNA. Translation: ABR80933.1.
RefSeqYP_001349601.1. NC_009656.1.

3D structure databases

ProteinModelPortalA6V966.
SMRA6V966. Positions 2-169.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6V966.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5357226.
GenomeReviewsGene locus PSPA7_4247 in contig CP000744_GR.
KEGGpap:PSPA7_4247.
PATRIC19830122. VBIPseAer80442_4068.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMAHNERYPD.
PhylomeDBA6V966.
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 nameA6V966_PSEA7
AccessionPrimary (citable) accession number: A6V966
Entry history
Integrated into UniProtKB/TrEMBL: August 21, 2007
Last sequence update: August 21, 2007
Last modified: December 14, 2011
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)