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P43522

- DEF_THETH

UniProt

P43522 - DEF_THETH

Protein

Peptide deformylase

Gene

def

Organism
Thermus thermophilus
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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

    Binds 1 Fe2+ 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

    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 – 144
    Helixi26 – 3914
    Beta strandi43 – 464
    Helixi47 – 504
    Beta strandi54 – 607
    Turni75 – 773
    Beta strandi81 – 9313
    Beta strandi96 – 1005
    Beta strandi110 – 1156
    Beta strandi117 – 1248
    Beta strandi130 – 1367
    Helixi137 – 15014
    Helixi155 – 1584
    Helixi161 – 17010
    Helixi172 – 18110

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MVYPIRLYGD PVLRRKARPV EDFSGIKRLA EDMLETMFEA KGVGLAAPQI    50
    GLSQRLFVAV EYADEPEGEE ERPLRELVRR VYVVANPVIT YREGLVEGTE 100
    GCLSLPGLYS EEVPRAERIR VEYQDEEGRG RVLELEGYMA RVFQHEIDHL 150
    DGILFFERLP KPKREAFLEA NRAELVRFQK EARALLKELS QG 192
    Length:192
    Mass (Da):22,092
    Last modified:November 1, 1995 - v1
    Checksum:i665945183A251361
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79087 Genomic DNA. Translation: CAA55695.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79087 Genomic DNA. Translation: CAA55695.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 76 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