Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q7W4K0

- DEF2_BORPA

UniProt

Q7W4K0 - DEF2_BORPA

Protein

Peptide deformylase 2

Gene

def2

Organism
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 bindingi99 – 991IronUniRule annotation
    Metal bindingi141 – 1411IronUniRule annotation
    Active sitei142 – 1421UniRule annotation
    Metal bindingi145 – 1451IronUniRule 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

    BioCyciBPAR257311:BPP3660-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptide deformylase 2UniRule annotation (EC:3.5.1.88UniRule annotation)
    Short name:
    PDF 2UniRule annotation
    Alternative name(s):
    Polypeptide deformylase 2UniRule annotation
    Gene namesi
    Name:def2UniRule annotation
    Ordered Locus Names:BPP3660
    OrganismiBordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
    Taxonomic identifieri257311 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
    ProteomesiUP000001421: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 176176Peptide deformylase 2PRO_0000082748Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi257311.BPP3660.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7W4K0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polypeptide deformylase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0242.
    HOGENOMiHOG000243508.
    KOiK01462.
    OMAiHECDHLA.
    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.

    Q7W4K0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIHAILKMGD PRLLRVAAPV ERYDTPELRA LIDDMFETMA HAQGVGLAAP    50
    QIGVDLQLVI FGFERNDRYP DAPAVPRTIL CNPVIEPLSD EMEDGWEGCL 100
    SVPGLRGLVP RYRHIRYSGY DPAGQRIERE AEGFHARVVQ HECDHLIGRL 150
    YPTRIRDLTK FGYTEVLFPE MDPNAD 176
    Length:176
    Mass (Da):19,939
    Last modified:October 1, 2003 - v1
    Checksum:i17508C9D66721AFE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX640434 Genomic DNA. Translation: CAE38944.1.
    RefSeqiNP_885818.1. NC_002928.3.

    Genome annotation databases

    EnsemblBacteriaiCAE38944; CAE38944; BPP3660.
    GeneIDi1668312.
    KEGGibpa:BPP3660.
    PATRICi21151345. VBIBorPar43418_3841.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX640434 Genomic DNA. Translation: CAE38944.1 .
    RefSeqi NP_885818.1. NC_002928.3.

    3D structure databases

    ProteinModelPortali Q7W4K0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 257311.BPP3660.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAE38944 ; CAE38944 ; BPP3660 .
    GeneIDi 1668312.
    KEGGi bpa:BPP3660.
    PATRICi 21151345. VBIBorPar43418_3841.

    Phylogenomic databases

    eggNOGi COG0242.
    HOGENOMi HOG000243508.
    KOi K01462.
    OMAi HECDHLA.
    OrthoDBi EOG664CMF.

    Enzyme and pathway databases

    BioCyci BPAR257311:BPP3660-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. "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
      Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S.
      , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
      Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 12822 / ATCC BAA-587 / NCTC 13253.

    Entry informationi

    Entry nameiDEF2_BORPA
    AccessioniPrimary (citable) accession number: Q7W4K0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 64 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