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B0SHH1

- DEF_LEPBA

UniProt

B0SHH1 - DEF_LEPBA

Protein

Peptide deformylase

Gene

def

Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (08 Apr 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 bindingi103 – 1031IronUniRule annotation
    Metal bindingi145 – 1451IronUniRule annotation
    Active sitei146 – 1461UniRule annotation
    Metal bindingi149 – 1491IronUniRule 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

    BioCyciLBIF355278:GHTJ-1519-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:LBF_1521
    OrganismiLeptospira biflexa serovar Patoc (strain Patoc 1 / Ames)
    Taxonomic identifieri355278 [NCBI]
    Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
    ProteomesiUP000001846: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 179179Peptide deformylasePRO_1000097321Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi355278.LBF_1521.

    Structurei

    3D structure databases

    ProteinModelPortaliB0SHH1.
    SMRiB0SHH1. Positions 2-179.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polypeptide deformylase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0242.
    HOGENOMiHOG000243508.
    KOiK01462.
    OMAiALEYPSE.
    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.

    B0SHH1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVRKILKIG NPILRQTSED VSESEIQTKD FKKLIRDMFE TMRHADGVGL    50
    AAPQIGVLKK LVVVGQEDDN ERYPGTPEVP NQIILNPEIT PLSPPRDGFW 100
    EGCLSVPGMR GYVERPNKIR MKWRDENYVE HDEIIEGYRA IVLQHECDHL 150
    FGVLYVDRLK STKLFGYNED IDTAGKLLD 179
    Length:179
    Mass (Da):20,479
    Last modified:April 8, 2008 - v1
    Checksum:i50A5293F6C91CCE5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000777 Genomic DNA. Translation: ABZ94032.1.
    RefSeqiYP_001962610.1. NC_010842.1.

    Genome annotation databases

    EnsemblBacteriaiABZ94032; ABZ94032; LBF_1521.
    GeneIDi6388120.
    KEGGilbf:LBF_1521.
    PATRICi22342115. VBILepBif95142_1617.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000777 Genomic DNA. Translation: ABZ94032.1 .
    RefSeqi YP_001962610.1. NC_010842.1.

    3D structure databases

    ProteinModelPortali B0SHH1.
    SMRi B0SHH1. Positions 2-179.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 355278.LBF_1521.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABZ94032 ; ABZ94032 ; LBF_1521 .
    GeneIDi 6388120.
    KEGGi lbf:LBF_1521.
    PATRICi 22342115. VBILepBif95142_1617.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci LBIF355278:GHTJ-1519-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. "Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis."
      Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A.
      , Davies J.K., Medigue C., Adler B.
      PLoS ONE 3:E1607-E1607(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Patoc 1 / Ames.

    Entry informationi

    Entry nameiDEF_LEPBA
    AccessioniPrimary (citable) accession number: B0SHH1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 42 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