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P43522

- DEF_THETH

UniProt

P43522 - DEF_THETH

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Protein

Peptide deformylase

Gene

def

Organism
Thermus thermophilus
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Fe2+By similarityNote: Binds 1 Fe(2+) ion.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi102 – 1021IronBy similarity
Metal bindingi145 – 1451IronBy similarity
Active sitei146 – 1461By similarity
Metal bindingi149 – 1491IronBy similarity

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. peptide deformylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide deformylase (EC:3.5.1.88)
Short name:
PDF
Alternative name(s):
Polypeptide deformylase
Gene namesi
Name:def
OrganismiThermus thermophilus
Taxonomic identifieri274 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 192192Peptide deformylasePRO_0000082867Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi262724.TTC1662.

Structurei

Secondary structure

1
192
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 144Combined sources
Helixi26 – 3914Combined sources
Beta strandi43 – 464Combined sources
Helixi47 – 504Combined sources
Beta strandi54 – 607Combined sources
Turni75 – 773Combined sources
Beta strandi81 – 9313Combined sources
Beta strandi96 – 1005Combined sources
Beta strandi110 – 1156Combined sources
Beta strandi117 – 1248Combined sources
Beta strandi130 – 1367Combined sources
Helixi137 – 15014Combined sources
Helixi155 – 1584Combined sources
Helixi161 – 17010Combined sources
Helixi172 – 18110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V3YX-ray1.81A/B1-192[»]
ProteinModelPortaliP43522.
SMRiP43522. Positions 1-182.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43522.

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.Curated

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.

P43522-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVYPIRLYGD PVLRRKARPV EDFSGIKRLA EDMLETMFEA KGVGLAAPQI
60 70 80 90 100
GLSQRLFVAV EYADEPEGEE ERPLRELVRR VYVVANPVIT YREGLVEGTE
110 120 130 140 150
GCLSLPGLYS EEVPRAERIR VEYQDEEGRG RVLELEGYMA RVFQHEIDHL
160 170 180 190
DGILFFERLP KPKREAFLEA NRAELVRFQK EARALLKELS QG
Length:192
Mass (Da):22,092
Last modified:November 1, 1995 - v1
Checksum:i665945183A251361
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79087 Genomic DNA. Translation: CAA55695.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79087 Genomic DNA. Translation: CAA55695.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1V3Y X-ray 1.81 A/B 1-192 [» ]
ProteinModelPortali P43522.
SMRi P43522. Positions 1-182.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 262724.TTC1662.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P43522.

Family and domain databases

Gene3Di 3.90.45.10. 1 hit.
HAMAPi MF_00163. Pep_deformylase.
InterProi IPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view ]
PANTHERi PTHR10458. PTHR10458. 1 hit.
Pfami PF01327. Pep_deformylase. 1 hit.
[Graphical view ]
PIRSFi PIRSF004749. Pep_def. 1 hit.
PRINTSi PR01576. PDEFORMYLASE.
SUPFAMi SSF56420. SSF56420. 1 hit.
TIGRFAMsi TIGR00079. pept_deformyl. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Characterization of the Thermus thermophilus locus encoding peptide deformylase and methionyl-tRNA(fMet) formyltransferase."
    Meinnel T., Blanquet S.
    J. Bacteriol. 176:7387-7390(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: VK1.
  2. "Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ion."
    Meinnel T., Lazennec C., Villoing S., Blanquet S.
    J. Mol. Biol. 267:749-761(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiDEF_THETH
AccessioniPrimary (citable) accession number: P43522
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 77 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3