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O08450

- DEF_CLOB8

UniProt

O08450 - DEF_CLOB8

Protein

Peptide deformylase

Gene

def

Organism
Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium acetobutylicum)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
  1. 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 bindingi85 – 851IronBy similarity
    Metal bindingi126 – 1261IronBy similarity
    Active sitei127 – 1271By similarity
    Metal bindingi130 – 1301IronBy 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

    BioCyciCBEI290402:GHL5-3610-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
    Synonyms:fms
    Ordered Locus Names:Cbei_3511
    OrganismiClostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium acetobutylicum)
    Taxonomic identifieri290402 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    ProteomesiUP000000565: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 136136Peptide deformylasePRO_0000082768Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi290402.Cbei_3511.

    Structurei

    3D structure databases

    ProteinModelPortaliO08450.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polypeptide deformylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0242.
    HOGENOMiHOG000243509.
    KOiK01462.
    OMAiHEMDHFE.
    OrthoDBiEOG6FNHTX.

    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.

    Sequencei

    Sequence statusi: Complete.

    O08450-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIKPIVKDIL FLGQKSEEAT KNDMVVIDDL IDTLRANLEH CVGLAANMIG    50
    VKKRILVFTV GNLIVPMINP VILKKEKPYE TEESCLSLIG FRKTKRYETI 100
    EVTYLDRNFN KKKQVFNGFT AQIIQHEMDH FEGIII 136
    Length:136
    Mass (Da):15,623
    Last modified:July 1, 1997 - v1
    Checksum:i7E9CE063FFDE9BE6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z96934 Genomic DNA. Translation: CAB09662.1.
    CP000721 Genomic DNA. Translation: ABR35634.1.
    RefSeqiWP_012059684.1. NC_009617.1.
    YP_001310590.1. NC_009617.1.

    Genome annotation databases

    EnsemblBacteriaiABR35634; ABR35634; Cbei_3511.
    GeneIDi5294680.
    KEGGicbe:Cbei_3511.
    PATRICi19351248. VBICloBei69853_3642.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z96934 Genomic DNA. Translation: CAB09662.1 .
    CP000721 Genomic DNA. Translation: ABR35634.1 .
    RefSeqi WP_012059684.1. NC_009617.1.
    YP_001310590.1. NC_009617.1.

    3D structure databases

    ProteinModelPortali O08450.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 290402.Cbei_3511.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABR35634 ; ABR35634 ; Cbei_3511 .
    GeneIDi 5294680.
    KEGGi cbe:Cbei_3511.
    PATRICi 19351248. VBICloBei69853_3642.

    Phylogenomic databases

    eggNOGi COG0242.
    HOGENOMi HOG000243509.
    KOi K01462.
    OMAi HEMDHFE.
    OrthoDBi EOG6FNHTX.

    Enzyme and pathway databases

    BioCyci CBEI290402:GHL5-3610-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.
    ProtoNeti Search...

    Publicationsi

    1. "Truncation of peptide deformylase reduces the growth rate and stabilizes solvent production in Clostridium beijerinckii NCIMB 8052."
      Evans V.J., Liyanage H., Ravagnani A., Young M., Kashket E.R.
      Appl. Environ. Microbiol. 64:1780-1785(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51743 / NCIMB 8052.

    Entry informationi

    Entry nameiDEF_CLOB8
    AccessioniPrimary (citable) accession number: O08450
    Secondary accession number(s): A6LZ54
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 86 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