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Q6ML45

- FPG_BDEBA

UniProt

Q6ML45 - FPG_BDEBA

Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    • Comment

    Functioni

    Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.UniRule annotation

    Catalytic activityi

    Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.UniRule annotation
    The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.UniRule annotation

    Cofactori

    Binds 1 zinc ion per subunit.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei2 – 21Schiff-base intermediate with DNAUniRule annotation
    Active sitei3 – 31Proton donorUniRule annotation
    Active sitei59 – 591Proton donor; for beta-elimination activityUniRule annotation
    Binding sitei91 – 911DNAUniRule annotation
    Binding sitei110 – 1101DNAUniRule annotation
    Binding sitei151 – 1511DNAUniRule annotation
    Active sitei260 – 2601Proton donor; for delta-elimination activityUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri236 – 27035FPG-typeUniRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. damaged DNA binding Source: InterPro
    2. oxidized purine nucleobase lesion DNA N-glycosylase activity Source: UniProtKB-HAMAP
    3. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. base-excision repair Source: InterPro
    2. nucleotide-excision repair Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase, Lyase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Formamidopyrimidine-DNA glycosylaseUniRule annotation (EC:3.2.2.23UniRule annotation)
    Short name:
    Fapy-DNA glycosylaseUniRule annotation
    Alternative name(s):
    DNA-(apurinic or apyrimidinic site) lyase MutMUniRule annotation (EC:4.2.99.18UniRule annotation)
    Short name:
    AP lyase MutMUniRule annotation
    Gene namesi
    Name:mutMUniRule annotation
    Synonyms:fpgUniRule annotation
    Ordered Locus Names:Bd2176
    OrganismiBdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100)
    Taxonomic identifieri264462 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaBdellovibrionalesBdellovibrionaceaeBdellovibrio
    ProteomesiUP000008080: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 270269Formamidopyrimidine-DNA glycosylasePRO_0000228418Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi264462.Bd2176.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FPG family.UniRule annotation
    Contains 1 FPG-type zinc finger.UniRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri236 – 27035FPG-typeUniRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0266.
    HOGENOMiHOG000020881.
    KOiK10563.
    OMAiDHVDLKL.
    OrthoDBiEOG6QP131.

    Family and domain databases

    HAMAPiMF_00103. Fapy_DNA_glycosyl.
    InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
    IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
    IPR000191. DNA_glycosylase/AP_lyase.
    IPR012319. DNA_glycosylase/AP_lyase_cat.
    IPR020629. Formamido-pyr_DNA_Glyclase.
    IPR010979. Ribosomal_S13-like_H2TH.
    IPR000214. Znf_DNA_glyclase/AP_lyase.
    IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
    [Graphical view]
    PfamiPF01149. Fapy_DNA_glyco. 1 hit.
    PF06831. H2TH. 1 hit.
    PF06827. zf-FPG_IleRS. 1 hit.
    [Graphical view]
    SMARTiSM00898. Fapy_DNA_glyco. 1 hit.
    [Graphical view]
    SUPFAMiSSF46946. SSF46946. 1 hit.
    SSF81624. SSF81624. 1 hit.
    TIGRFAMsiTIGR00577. fpg. 1 hit.
    PROSITEiPS51068. FPG_CAT. 1 hit.
    PS01242. ZF_FPG_1. 1 hit.
    PS51066. ZF_FPG_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q6ML45-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPELPEVEVV RRGLETILKD QPILEKVELM RKDLREPIPA KKISTLVGQP    50
    LTSIERRAKY LLLWTPKGAM LSHLGMTGTW RVAVPGDERL HDHIYLHFSG 100
    DLRLAYRDPR RFGCFDFVQD PLKHPKLADL GPEPLEAEFN GPLLWEKLRG 150
    KDVALKVALM DQKVVVGVGN IYASEALFAA GIKPTLPARK LSLERASLLV 200
    GEIKKILSQS IKAGGSSISD FAQASGESGY FQTSFRVYGR DKEPCVTCGQ 250
    QVKSKVLGGR NTFWCSRCQK 270
    Length:270
    Mass (Da):30,125
    Last modified:January 23, 2007 - v3
    Checksum:iA577EE10A7617600
    GO

    Sequence cautioni

    The sequence CAE80012.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX842651 Genomic DNA. Translation: CAE80012.1. Different initiation.
    RefSeqiNP_969019.1. NC_005363.1.
    WP_011164614.1. NC_005363.1.

    Genome annotation databases

    EnsemblBacteriaiCAE80012; CAE80012; Bd2176.
    GeneIDi2734536.
    KEGGibba:Bd2176.
    PATRICi21078844. VBIBdeBac73187_1987.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX842651 Genomic DNA. Translation: CAE80012.1 . Different initiation.
    RefSeqi NP_969019.1. NC_005363.1.
    WP_011164614.1. NC_005363.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 264462.Bd2176.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAE80012 ; CAE80012 ; Bd2176 .
    GeneIDi 2734536.
    KEGGi bba:Bd2176.
    PATRICi 21078844. VBIBdeBac73187_1987.

    Phylogenomic databases

    eggNOGi COG0266.
    HOGENOMi HOG000020881.
    KOi K10563.
    OMAi DHVDLKL.
    OrthoDBi EOG6QP131.

    Family and domain databases

    HAMAPi MF_00103. Fapy_DNA_glycosyl.
    InterProi IPR015886. DNA_glyclase/AP_lyase_DNA-bd.
    IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
    IPR000191. DNA_glycosylase/AP_lyase.
    IPR012319. DNA_glycosylase/AP_lyase_cat.
    IPR020629. Formamido-pyr_DNA_Glyclase.
    IPR010979. Ribosomal_S13-like_H2TH.
    IPR000214. Znf_DNA_glyclase/AP_lyase.
    IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
    [Graphical view ]
    Pfami PF01149. Fapy_DNA_glyco. 1 hit.
    PF06831. H2TH. 1 hit.
    PF06827. zf-FPG_IleRS. 1 hit.
    [Graphical view ]
    SMARTi SM00898. Fapy_DNA_glyco. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46946. SSF46946. 1 hit.
    SSF81624. SSF81624. 1 hit.
    TIGRFAMsi TIGR00577. fpg. 1 hit.
    PROSITEi PS51068. FPG_CAT. 1 hit.
    PS01242. ZF_FPG_1. 1 hit.
    PS51066. ZF_FPG_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective."
      Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C.
      Science 303:689-692(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 15356 / DSM 50701 / NCIB 9529 / HD100.

    Entry informationi

    Entry nameiFPG_BDEBA
    AccessioniPrimary (citable) accession number: Q6ML45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 79 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3