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B0T1S9

- DEF_CAUSK

UniProt

B0T1S9 - DEF_CAUSK

Protein

Peptide deformylase

Gene

def

Organism
Caulobacter sp. (strain K31)
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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    • 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 bindingi98 – 981IronUniRule annotation
    Metal bindingi140 – 1401IronUniRule annotation
    Active sitei141 – 1411UniRule annotation
    Metal bindingi144 – 1441IronUniRule 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

    BioCyciCSP366602:GH0Y-4621-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:Caul_4570
    OrganismiCaulobacter sp. (strain K31)
    Taxonomic identifieri366602 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter
    ProteomesiUP000001316: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 173173Peptide deformylasePRO_1000076940Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi366602.Caul_4570.

    Structurei

    3D structure databases

    ProteinModelPortaliB0T1S9.
    SMRiB0T1S9. Positions 2-172.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polypeptide deformylase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0242.
    HOGENOMiHOG000243509.
    KOiK01462.
    OMAiWATCAQH.
    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.

    B0T1S9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAIRRILTVD NAADLAVLKQ VSKDVPAVDD ALRGLMDDML ETMYDAPGIG    50
    LAAVQVGELV NVIVMDLARE GEEPAPRYFV NPKITWASEE LFEYEEGCLS 100
    VPEVYDAVER PAKVKISYLN YQGEAVEEDA EELFAVCIQH EMDHLKGVLF 150
    IDHLSRLKRD RAISKVKKAR RAA 173
    Length:173
    Mass (Da):19,361
    Last modified:April 8, 2008 - v1
    Checksum:iEF44762AA0D180CE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000927 Genomic DNA. Translation: ABZ73690.1.
    RefSeqiWP_012288566.1. NC_010338.1.
    YP_001686188.1. NC_010338.1.

    Genome annotation databases

    EnsemblBacteriaiABZ73690; ABZ73690; Caul_4570.
    GeneIDi5902031.
    KEGGicak:Caul_4570.
    PATRICi21322320. VBICauSp18104_4983.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000927 Genomic DNA. Translation: ABZ73690.1 .
    RefSeqi WP_012288566.1. NC_010338.1.
    YP_001686188.1. NC_010338.1.

    3D structure databases

    ProteinModelPortali B0T1S9.
    SMRi B0T1S9. Positions 2-172.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 366602.Caul_4570.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABZ73690 ; ABZ73690 ; Caul_4570 .
    GeneIDi 5902031.
    KEGGi cak:Caul_4570.
    PATRICi 21322320. VBICauSp18104_4983.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci CSP366602:GH0Y-4621-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K31.

    Entry informationi

    Entry nameiDEF_CAUSK
    AccessioniPrimary (citable) accession number: B0T1S9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3