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A9I6Y3

- FPG_BORPD

UniProt

A9I6Y3 - FPG_BORPD

Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      Previous versions | rss
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    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 sitei58 – 581Proton donor; for beta-elimination activityUniRule annotation
    Binding sitei91 – 911DNAUniRule annotation
    Binding sitei109 – 1091DNAUniRule annotation
    Binding sitei154 – 1541DNAUniRule annotation
    Active sitei264 – 2641Proton donor; for delta-elimination activityUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri240 – 27435FPG-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

    Enzyme and pathway databases

    BioCyciBPET340100:GJBO-4069-MONOMER.

    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:Bpet4006
    OrganismiBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448)
    Taxonomic identifieri340100 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
    ProteomesiUP000001225: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 275274Formamidopyrimidine-DNA glycosylasePRO_1000094031Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi340100.Bpet4006.

    Structurei

    3D structure databases

    ProteinModelPortaliA9I6Y3.
    ModBaseiSearch...
    MobiDBiSearch...

    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 fingeri240 – 27435FPG-typeUniRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0266.
    HOGENOMiHOG000020881.
    KOiK10563.
    OMAiKIVATDH.
    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.

    A9I6Y3-1 [UniParc]FASTAAdd to Basket

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    MPELPEVETT RRGIDAVITG KTLRRLLVRE SRMRWPIPAD LPGLLSGRAV    50
    LECARRGKYL LLRFEHGTQI VHLGMSGSLR SVPAGEAPRK HDHVDWIFDH 100
    ATLRLHDPRR FGAVLWHPDT AGPIAAHPLL ARLGIEPFDP RFDGAWLHSQ 150
    FRNRAIAVKQ ALLAGDAVVG VGNIYASESL FRAGIDPRTP ARRISRARCA 200
    RLADMVRATL ADALASGGST LRDYVGASGQ PGSYFEIHAA VYERAGLPCR 250
    VCGTPIRRLV QGQRATYYCP SCQKR 275
    Length:275
    Mass (Da):30,349
    Last modified:February 5, 2008 - v1
    Checksum:iC168ED7037DECD22
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM902716 Genomic DNA. Translation: CAP44354.1.
    RefSeqiWP_012250895.1. NC_010170.1.
    YP_001632622.1. NC_010170.1.

    Genome annotation databases

    EnsemblBacteriaiCAP44354; CAP44354; Bpet4006.
    GeneIDi5819635.
    KEGGibpt:Bpet4006.
    PATRICi21169637. VBIBorPet31633_4048.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM902716 Genomic DNA. Translation: CAP44354.1 .
    RefSeqi WP_012250895.1. NC_010170.1.
    YP_001632622.1. NC_010170.1.

    3D structure databases

    ProteinModelPortali A9I6Y3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 340100.Bpet4006.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAP44354 ; CAP44354 ; Bpet4006 .
    GeneIDi 5819635.
    KEGGi bpt:Bpet4006.
    PATRICi 21169637. VBIBorPet31633_4048.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BPET340100:GJBO-4069-MONOMER.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-461 / DSM 12804 / CCUG 43448.

    Entry informationi

    Entry nameiFPG_BORPD
    AccessioniPrimary (citable) accession number: A9I6Y3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 51 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, Multifunctional enzyme, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3