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C4ZUE1

- DEF_ECOBW

UniProt

C4ZUE1 - DEF_ECOBW

Protein

Peptide deformylase

Gene

def

Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 36 (01 Oct 2014)
      Sequence version 1 (28 Jul 2009)
      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.UniRule annotation

    Catalytic activityi

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

    Cofactori

    Binds 1 Fe2+ ion.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi91 – 911IronUniRule annotation
    Metal bindingi133 – 1331IronUniRule annotation
    Active sitei134 – 1341UniRule annotation
    Metal bindingi137 – 1371IronUniRule annotation

    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

    Enzyme and pathway databases

    BioCyciECOL595496:GI18-3101-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:BWG_2977
    OrganismiEscherichia coli (strain K12 / MC4100 / BW2952)
    Taxonomic identifieri595496 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000001478: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 169169Peptide deformylasePRO_1000203601Add
    BLAST

    Proteomic databases

    PRIDEiC4ZUE1.

    Interactioni

    Protein-protein interaction databases

    STRINGi595496.BWG_2977.

    Structurei

    3D structure databases

    ProteinModelPortaliC4ZUE1.
    SMRiC4ZUE1. Positions 2-168.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polypeptide deformylase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0242.
    HOGENOMiHOG000243509.
    KOiK01462.
    OMAiELLAICI.
    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.

    C4ZUE1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVLQVLHIP DERLRKVAKP VEEVNAEIQR IVDDMFETMY AEEGIGLAAT    50
    QVDIHQRIIV IDVSENRDER LVLINPELLE KSGETGIEEG CLSIPEQRAL 100
    VPRAEKVKIR ALDRDGKPFE LEADGLLAIC IQHEMDHLVG KLFMDYLSPL 150
    KQQRIRQKVE KLDRLKARA 169
    Length:169
    Mass (Da):19,328
    Last modified:July 28, 2009 - v1
    Checksum:iC485EB6C1D2D91B8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001396 Genomic DNA. Translation: ACR63985.1.
    RefSeqiYP_002928173.1. NC_012759.1.

    Genome annotation databases

    EnsemblBacteriaiACR63985; ACR63985; BWG_2977.
    GeneIDi7952911.
    KEGGiebw:BWG_2977.
    PATRICi18275542. VBIEscCol60876_3262.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001396 Genomic DNA. Translation: ACR63985.1 .
    RefSeqi YP_002928173.1. NC_012759.1.

    3D structure databases

    ProteinModelPortali C4ZUE1.
    SMRi C4ZUE1. Positions 2-168.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 595496.BWG_2977.

    Chemistry

    BindingDBi C4ZUE1.

    Proteomic databases

    PRIDEi C4ZUE1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACR63985 ; ACR63985 ; BWG_2977 .
    GeneIDi 7952911.
    KEGGi ebw:BWG_2977.
    PATRICi 18275542. VBIEscCol60876_3262.

    Phylogenomic databases

    eggNOGi COG0242.
    HOGENOMi HOG000243509.
    KOi K01462.
    OMAi ELLAICI.
    OrthoDBi EOG664CMF.

    Enzyme and pathway databases

    BioCyci ECOL595496:GI18-3101-MONOMER.

    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. "Genomic sequencing reveals regulatory mutations and recombinational events in the widely used MC4100 lineage of Escherichia coli K-12."
      Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R., Wang L.
      J. Bacteriol. 191:4025-4029(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MC4100 / BW2952.

    Entry informationi

    Entry nameiDEF_ECOBW
    AccessioniPrimary (citable) accession number: C4ZUE1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 36 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