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B1LB14

- DEF_THESQ

UniProt

B1LB14 - DEF_THESQ

Protein

Peptide deformylase

Gene

def

Organism
Thermotoga sp. (strain RQ2)
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.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 bindingi87 – 871IronUniRule annotation
    Metal bindingi129 – 1291IronUniRule annotation
    Active sitei130 – 1301UniRule annotation
    Metal bindingi133 – 1331IronUniRule 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

    BioCyciTSP126740:GH49-1204-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:TRQ2_1168
    OrganismiThermotoga sp. (strain RQ2)
    Taxonomic identifieri126740 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000001687: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 164164Peptide deformylasePRO_1000097355Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi126740.TRQ2_1168.

    Structurei

    3D structure databases

    ProteinModelPortaliB1LB14.
    SMRiB1LB14. Positions 1-145.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polypeptide deformylase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0242.
    HOGENOMiHOG000243509.
    KOiK01462.
    OMAiEETGEEW.
    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.

    B1LB14-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYRIRVFGDP VLRKRAKPVT KFDDNLKKTI ERMIETMYHY DGVGLAAPQV    50
    GISQRFFVMD VGNGPVAVIN PEILEIDPET EVAEEGCLSF PEIFVEIERS 100
    KRIKVKYQNT RGEYVEEELE GYAARVFQHE FDHLNGVLII DRISPAKRLL 150
    LRKKLMDIAR TVKR 164
    Length:164
    Mass (Da):19,010
    Last modified:April 29, 2008 - v1
    Checksum:i9FE94BFB1D7B7907
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000969 Genomic DNA. Translation: ACB09512.1.
    RefSeqiYP_001739195.1. NC_010483.1.

    Genome annotation databases

    EnsemblBacteriaiACB09512; ACB09512; TRQ2_1168.
    GeneIDi6092603.
    KEGGitrq:TRQ2_1168.
    PATRICi23948938. VBITheSp108950_1189.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000969 Genomic DNA. Translation: ACB09512.1 .
    RefSeqi YP_001739195.1. NC_010483.1.

    3D structure databases

    ProteinModelPortali B1LB14.
    SMRi B1LB14. Positions 1-145.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 126740.TRQ2_1168.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACB09512 ; ACB09512 ; TRQ2_1168 .
    GeneIDi 6092603.
    KEGGi trq:TRQ2_1168.
    PATRICi 23948938. VBITheSp108950_1189.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci TSP126740:GH49-1204-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: RQ2.

    Entry informationi

    Entry nameiDEF_THESQ
    AccessioniPrimary (citable) accession number: B1LB14
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 45 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