Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q826Q0

- DEF2_STRAW

UniProt

Q826Q0 - DEF2_STRAW

Protein

Peptide deformylase 2

Gene

def2

Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • 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 bindingi104 – 1041IronUniRule annotation
    Metal bindingi146 – 1461IronUniRule annotation
    Active sitei147 – 1471UniRule annotation
    Metal bindingi150 – 1501IronUniRule 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

    BioCyciSAVE227882:GJU1-7222-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptide deformylase 2UniRule annotation (EC:3.5.1.88UniRule annotation)
    Short name:
    PDF 2UniRule annotation
    Alternative name(s):
    Polypeptide deformylase 2UniRule annotation
    Gene namesi
    Name:def2UniRule annotation
    Ordered Locus Names:SAV_7126
    OrganismiStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
    Taxonomic identifieri227882 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces
    ProteomesiUP000000428: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 186186Peptide deformylase 2PRO_0000082850Add
    BLAST

    Proteomic databases

    PRIDEiQ826Q0.

    Interactioni

    Protein-protein interaction databases

    STRINGi227882.SAV_7126.

    Structurei

    3D structure databases

    ProteinModelPortaliQ826Q0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polypeptide deformylase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0242.
    HOGENOMiHOG000243508.
    KOiK01462.
    OMAiPRAVFVY.
    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.

    Q826Q0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRHGSIPGTR GHVRPLALLG DPVLHAPCEE VTDHGPELAR LVEDMFATMY    50
    AANGVGLAAN QIGVPLRVFV YDCPDDEDVR HVGHVVNPRL IEADGVVLRG 100
    PEGCLSLPGL EAGTERYDRA VVEGFTTDGE PVRVLGTGWF ARCLQHECDH 150
    LDGGVYVDRV SGWRHRRVMR QAARAPWNRQ RAPEPR 186
    Length:186
    Mass (Da):20,511
    Last modified:June 1, 2003 - v1
    Checksum:i6B0E069BC3331CC9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000030 Genomic DNA. Translation: BAC74837.1.
    RefSeqiNP_828302.1. NC_003155.4.

    Genome annotation databases

    EnsemblBacteriaiBAC74837; BAC74837; SAV_7126.
    GeneIDi1211671.
    KEGGisma:SAV_7126.
    PATRICi23728412. VBIStrAve112782_7545.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000030 Genomic DNA. Translation: BAC74837.1 .
    RefSeqi NP_828302.1. NC_003155.4.

    3D structure databases

    ProteinModelPortali Q826Q0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 227882.SAV_7126.

    Proteomic databases

    PRIDEi Q826Q0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC74837 ; BAC74837 ; SAV_7126 .
    GeneIDi 1211671.
    KEGGi sma:SAV_7126.
    PATRICi 23728412. VBIStrAve112782_7545.

    Phylogenomic databases

    eggNOGi COG0242.
    HOGENOMi HOG000243508.
    KOi K01462.
    OMAi PRAVFVY.
    OrthoDBi EOG664CMF.

    Enzyme and pathway databases

    BioCyci SAVE227882:GJU1-7222-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. "Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
      Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
      Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
    2. "Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
      Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
      Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

    Entry informationi

    Entry nameiDEF2_STRAW
    AccessioniPrimary (citable) accession number: Q826Q0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 68 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