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B5YIL7

- DEF_THEYD

UniProt

B5YIL7 - DEF_THEYD

Protein

Peptide deformylase

Gene

def

Organism
Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (25 Nov 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 bindingi93 – 931IronUniRule annotation
    Metal bindingi135 – 1351IronUniRule annotation
    Active sitei136 – 1361UniRule annotation
    Metal bindingi139 – 1391IronUniRule 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

    BioCyciTYEL289376:GH9L-329-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:THEYE_A0329
    OrganismiThermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87)
    Taxonomic identifieri289376 [NCBI]
    Taxonomic lineageiBacteriaNitrospiraeNitrospiralesNitrospiraceaeThermodesulfovibrio
    ProteomesiUP000000718: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 165165Peptide deformylasePRO_1000097356Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi289376.THEYE_A0329.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polypeptide deformylase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0242.
    HOGENOMiHOG000243509.
    KOiK01462.
    OMAiDMYDTMD.
    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.

    B5YIL7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAILEIKKYP DEVLKKKAET ISEINGDLQK LIDNMIETMY NANGIGLAAP    50
    QVGVLKRLIV VDTSPREQNQ SLIVLINPEI TDSEGEILSE EGCLSLPGFT 100
    TRLKRKERVI VKGLDRNGKE IEIEATGLLA RALQHEIDHL DGILLIDKIS 150
    PLKRELFRKK FKTKK 165
    Length:165
    Mass (Da):18,570
    Last modified:November 25, 2008 - v1
    Checksum:i396EA10220E4A59B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001147 Genomic DNA. Translation: ACI20745.1.
    RefSeqiWP_012545479.1. NC_011296.1.
    YP_002248176.1. NC_011296.1.

    Genome annotation databases

    EnsemblBacteriaiACI20745; ACI20745; THEYE_A0329.
    GeneIDi6943012.
    KEGGitye:THEYE_A0329.
    PATRICi23907675. VBITheYel104483_0322.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001147 Genomic DNA. Translation: ACI20745.1 .
    RefSeqi WP_012545479.1. NC_011296.1.
    YP_002248176.1. NC_011296.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 289376.THEYE_A0329.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACI20745 ; ACI20745 ; THEYE_A0329 .
    GeneIDi 6943012.
    KEGGi tye:THEYE_A0329.
    PATRICi 23907675. VBITheYel104483_0322.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci TYEL289376:GH9L-329-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. "The complete genome sequence of Thermodesulfovibrio yellowstonii strain ATCC 51303 / DSM 11347 / YP87."
      Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.
      Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51303 / DSM 11347 / YP87.

    Entry informationi

    Entry nameiDEF_THEYD
    AccessioniPrimary (citable) accession number: B5YIL7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 40 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