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Protein

Peptide deformylase

Gene

def

Organism
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide.UniRule annotation

Cofactori

Fe2+UniRule annotationNote: Binds 1 Fe2+ ion.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi87 – 871IronUniRule annotation
Metal bindingi129 – 1291IronUniRule annotation
Active sitei130 – 1301UniRule annotation
Metal bindingi133 – 1331IronUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciTPET390874:GHJI-1165-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide deformylaseUniRule annotation (EC:3.5.1.88UniRule annotation)
Short name:
PDFUniRule annotation
Alternative name(s):
Polypeptide deformylaseUniRule annotation
Gene namesi
Name:defUniRule annotation
Ordered Locus Names:Tpet_1130
OrganismiThermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Taxonomic identifieri390874 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000006558 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164Peptide deformylasePRO_1000023137Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi390874.Tpet_1130.

Structurei

3D structure databases

ProteinModelPortaliA5ILS1.
SMRiA5ILS1. Positions 1-145.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243509.
OMAiSFDSKLH.
OrthoDBiEOG664CMF.

Family and domain databases

Gene3Di3.90.45.10. 1 hit.
HAMAPiMF_00163. Pep_deformylase.
InterProiIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERiPTHR10458. PTHR10458. 1 hit.
PfamiPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFiPIRSF004749. Pep_def. 1 hit.
PRINTSiPR01576. PDEFORMYLASE.
SUPFAMiSSF56420. SSF56420. 1 hit.
TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.

Sequencei

Sequence statusi: Complete.

A5ILS1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRIRVFGDP VLRKRAKPVT KFDDNLEKTI ERMIETMYHY DGVGLAAPQV
60 70 80 90 100
GISQRFFVMD VGNGPVAVIN PEILEIDPET EVAEEGCLSF PEIFVEIERS
110 120 130 140 150
KRIKVRYQNT KGEYVEEVLE GYAARVFQHE FDHLNGVLII DRISPAKRLL
160
LRKKLMDIAR TVKR
Length:164
Mass (Da):18,981
Last modified:June 26, 2007 - v1
Checksum:i1D24744FAB71EB5B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000702 Genomic DNA. Translation: ABQ47144.1.

Genome annotation databases

EnsemblBacteriaiABQ47144; ABQ47144; Tpet_1130.
PATRICi23945078. VBIThePet65348_1147.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000702 Genomic DNA. Translation: ABQ47144.1.

3D structure databases

ProteinModelPortaliA5ILS1.
SMRiA5ILS1. Positions 1-145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi390874.Tpet_1130.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ47144; ABQ47144; Tpet_1130.
PATRICi23945078. VBIThePet65348_1147.

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243509.
OMAiSFDSKLH.
OrthoDBiEOG664CMF.

Enzyme and pathway databases

BioCyciTPET390874:GHJI-1165-MONOMER.

Family and domain databases

Gene3Di3.90.45.10. 1 hit.
HAMAPiMF_00163. Pep_deformylase.
InterProiIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERiPTHR10458. PTHR10458. 1 hit.
PfamiPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFiPIRSF004749. Pep_def. 1 hit.
PRINTSiPR01576. PDEFORMYLASE.
SUPFAMiSSF56420. SSF56420. 1 hit.
TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RKU-1 / ATCC BAA-488 / DSM 13995.

Entry informationi

Entry nameiDEF_THEP1
AccessioniPrimary (citable) accession number: A5ILS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 26, 2007
Last modified: July 22, 2015
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.