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A5ILS1 (DEF_THEP1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptide deformylase

Short name=PDF
EC=3.5.1.88
Alternative name(s):
Polypeptide deformylase
Gene names
Name:def
Ordered Locus Names:Tpet_1130
OrganismThermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995) [Complete proteome] [HAMAP]
Taxonomic identifier390874 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length164 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-Rule MF_00163

Catalytic activity

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP-Rule MF_00163

Cofactor

Binds 1 Fe2+ ion By similarity. HAMAP-Rule MF_00163

Sequence similarities

Belongs to the polypeptide deformylase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandIron
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functioniron ion binding

Inferred from electronic annotation. Source: InterPro

peptide deformylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 164164Peptide deformylase HAMAP-Rule MF_00163
PRO_1000023137

Sites

Active site1301 By similarity
Metal binding871Iron By similarity
Metal binding1291Iron By similarity
Metal binding1331Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
A5ILS1 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 1D24744FAB71EB5B

FASTA16418,981
        10         20         30         40         50         60 
MYRIRVFGDP VLRKRAKPVT KFDDNLEKTI ERMIETMYHY DGVGLAAPQV GISQRFFVMD 

        70         80         90        100        110        120 
VGNGPVAVIN PEILEIDPET EVAEEGCLSF PEIFVEIERS KRIKVRYQNT KGEYVEEVLE 

       130        140        150        160 
GYAARVFQHE FDHLNGVLII DRISPAKRLL LRKKLMDIAR TVKR 

« Hide

References

[1]"Complete sequence of Thermotoga petrophila RKU-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RKU-1 / ATCC BAA-488 / DSM 13995.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000702 Genomic DNA. Translation: ABQ47144.1.
RefSeqYP_001244720.1. NC_009486.1.

3D structure databases

ProteinModelPortalA5ILS1.
SMRA5ILS1. Positions 1-145.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390874.Tpet_1130.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ47144; ABQ47144; Tpet_1130.
GeneID5169986.
KEGGtpt:Tpet_1130.
PATRIC23945078. VBIThePet65348_1147.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243509.
KOK01462.
OMAEETGEEW.
OrthoDBEOG664CMF.

Enzyme and pathway databases

BioCycTPET390874:GHJI-1165-MONOMER.

Family and domain databases

Gene3D3.90.45.10. 1 hit.
HAMAPMF_00163. Pep_deformylase.
InterProIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERPTHR10458. PTHR10458. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFPIRSF004749. Pep_def. 1 hit.
PRINTSPR01576. PDEFORMYLASE.
SUPFAMSSF56420. SSF56420. 1 hit.
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDEF_THEP1
AccessionPrimary (citable) accession number: A5ILS1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 26, 2007
Last modified: May 14, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families