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B5XIL1

- DEF_STRPZ

UniProt

B5XIL1 - DEF_STRPZ

Protein

Peptide deformylase

Gene

def

Organism
Streptococcus pyogenes serotype M49 (strain NZ131)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (25 Nov 2008)
      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 bindingi131 – 1311IronUniRule annotation
    Metal bindingi174 – 1741IronUniRule annotation
    Active sitei175 – 1751UniRule annotation
    Metal bindingi178 – 1781IronUniRule 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

    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:Spy49_1615
    OrganismiStreptococcus pyogenes serotype M49 (strain NZ131)
    Taxonomic identifieri471876 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000001039: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 204204Peptide deformylasePRO_1000097351Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi471876.Spy49_1615.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polypeptide deformylase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0242.
    HOGENOMiHOG000243507.
    KOiK01462.
    OMAiHIDKENP.
    OrthoDBiEOG6PZXGQ.

    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.

    B5XIL1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAQDKLIKP SHLITMDDII REGNPTLRAV AKEVSLPLCD EDILLGEKMM    50
    QFLKHSQNPV MAEKLGLRAG VGLAAPQIDV SKRIIAVLVP NLPDKEGNPP 100
    KEAYSWQEVL YNPKIVSHSV QDAALSDGEG CLSVDRVVEG YVVRHARVTV 150
    DYYDKEGQQH RIKLKGYNAI VVQHEIDHIN GVLFYDRINA KNPFETKEEL 200
    LILD 204
    Length:204
    Mass (Da):22,861
    Last modified:November 25, 2008 - v1
    Checksum:i835840248AF9BC05
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000829 Genomic DNA. Translation: ACI61873.1.
    RefSeqiWP_009880416.1. NC_011375.1.
    YP_002286568.1. NC_011375.1.

    Genome annotation databases

    EnsemblBacteriaiACI61873; ACI61873; Spy49_1615.
    GeneIDi6985225.
    KEGGisoz:Spy49_1615.
    PATRICi19758364. VBIStrPyo129711_1670.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000829 Genomic DNA. Translation: ACI61873.1 .
    RefSeqi WP_009880416.1. NC_011375.1.
    YP_002286568.1. NC_011375.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 471876.Spy49_1615.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACI61873 ; ACI61873 ; Spy49_1615 .
    GeneIDi 6985225.
    KEGGi soz:Spy49_1615.
    PATRICi 19758364. VBIStrPyo129711_1670.

    Phylogenomic databases

    eggNOGi COG0242.
    HOGENOMi HOG000243507.
    KOi K01462.
    OMAi HIDKENP.
    OrthoDBi EOG6PZXGQ.

    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. "Genome sequence of a nephritogenic and highly transformable M49 strain of Streptococcus pyogenes."
      McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B., Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.
      J. Bacteriol. 190:7773-7785(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NZ131.

    Entry informationi

    Entry nameiDEF_STRPZ
    AccessioniPrimary (citable) accession number: B5XIL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 43 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