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P57948

- DEF_PASMU

UniProt

P57948 - DEF_PASMU

Protein

Peptide deformylase

Gene

def

Organism
Pasteurella multocida (strain Pm70)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (27 Apr 2001)
      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 By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 1 Fe2+ ion.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi91 – 911IronBy similarity
    Metal bindingi133 – 1331IronBy similarity
    Active sitei134 – 1341By similarity
    Metal bindingi137 – 1371IronBy similarity

    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

    BioCyciPMUL272843:GC8W-1621-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptide deformylase (EC:3.5.1.88)
    Short name:
    PDF
    Alternative name(s):
    Polypeptide deformylase
    Gene namesi
    Name:def
    Ordered Locus Names:PM1559
    OrganismiPasteurella multocida (strain Pm70)
    Taxonomic identifieri272843 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
    ProteomesiUP000000809: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 170170Peptide deformylasePRO_0000082812Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi272843.PM1559.

    Structurei

    3D structure databases

    ProteinModelPortaliP57948.
    SMRiP57948. Positions 4-168.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polypeptide deformylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0242.
    HOGENOMiHOG000243509.
    KOiK01462.
    OMAiREENSEH.
    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.

    P57948-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARLNVLVYP DERLKIIAKP VVEVNDEIRE IVDNMFETMY LEEGIGLAAT    50
    QVNIHQRIIT IDVEGTKENQ YVLINPEIID SCGETGIEEG CLSLPGFRGF 100
    VPRKEKVTIK ALDRHGEEYT LSAEGLLAIC IQHEIDHLNG IVFADYLSPL 150
    KRQRMKEKLL KLQKQLARQK 170
    Length:170
    Mass (Da):19,386
    Last modified:April 27, 2001 - v1
    Checksum:i2A65407534AD5A94
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004439 Genomic DNA. Translation: AAK03643.1.
    RefSeqiNP_246498.1. NC_002663.1.

    Genome annotation databases

    EnsemblBacteriaiAAK03643; AAK03643; PM1559.
    GeneIDi1244906.
    KEGGipmu:PM1559.
    PATRICi22872405. VBIPasMul88067_1576.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004439 Genomic DNA. Translation: AAK03643.1 .
    RefSeqi NP_246498.1. NC_002663.1.

    3D structure databases

    ProteinModelPortali P57948.
    SMRi P57948. Positions 4-168.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272843.PM1559.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK03643 ; AAK03643 ; PM1559 .
    GeneIDi 1244906.
    KEGGi pmu:PM1559.
    PATRICi 22872405. VBIPasMul88067_1576.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PMUL272843:GC8W-1621-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: Pm70.

    Entry informationi

    Entry nameiDEF_PASMU
    AccessioniPrimary (citable) accession number: P57948
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: April 27, 2001
    Last modified: October 1, 2014
    This is version 81 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