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P59065

- FPG_THEEB

UniProt

P59065 - FPG_THEEB

Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Thermosynechococcus elongatus (strain BP-1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 87 (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 By similarity.By similarity

    Catalytic activityi

    Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
    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.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei2 – 21Schiff-base intermediate with DNABy similarity
    Active sitei3 – 31Proton donorBy similarity
    Active sitei60 – 601Proton donor; for beta-elimination activityBy similarity
    Binding sitei94 – 941DNABy similarity
    Binding sitei113 – 1131DNABy similarity
    Active sitei267 – 2671Proton donor; for delta-elimination activityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri243 – 27735FPG-typeAdd
    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 glycosylase (EC:3.2.2.23)
    Short name:
    Fapy-DNA glycosylase
    Alternative name(s):
    DNA-(apurinic or apyrimidinic site) lyase MutM (EC:4.2.99.18)
    Short name:
    AP lyase MutM
    Gene namesi
    Name:mutM
    Synonyms:fpg
    Ordered Locus Names:tll1566
    OrganismiThermosynechococcus elongatus (strain BP-1)
    Taxonomic identifieri197221 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
    ProteomesiUP000000440: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 284283Formamidopyrimidine-DNA glycosylasePRO_0000170875Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi197221.tll1566.

    Structurei

    3D structure databases

    ProteinModelPortaliP59065.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri243 – 27735FPG-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0266.
    HOGENOMiHOG000020884.
    KOiK10563.
    OMAiAKIHPEK.
    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.

    P59065-1 [UniParc]FASTAAdd to Basket

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    MPELPEVETV RRGLELVTLK QPIVDVEVLL ARSIALPKEP QAFIEHLRDR    50
    AIEQWQRRGK YLLATLDDGS RLVIHLRMSG QLLWLTTPQP PCPHTRVRWF 100
    FPTRAELRFV DQRTFGRCWW LPPDCRVAEA IPALATLAPE PLSEAFTVAF 150
    LAARLAHCRR SIKTALLDQS IVAGMGNIYA DESLFLSGLH PTQSAHTLTP 200
    EQVQRLHGVI CQVLREGIAA GGTTIRTFMS PAGVNGHYGG QAWVYGRKGE 250
    ACRVCGTTIE RLRLAGRSSH YCPQCQPLSS AIGK 284
    Length:284
    Mass (Da):31,631
    Last modified:January 23, 2007 - v3
    Checksum:iE8C1351D8858DC08
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000039 Genomic DNA. Translation: BAC09118.1.
    RefSeqiNP_682356.1. NC_004113.1.
    WP_011057406.1. NC_004113.1.

    Genome annotation databases

    EnsemblBacteriaiBAC09118; BAC09118; BAC09118.
    GeneIDi1010930.
    KEGGitel:tll1566.
    PATRICi23928498. VBITheElo119873_1642.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000039 Genomic DNA. Translation: BAC09118.1 .
    RefSeqi NP_682356.1. NC_004113.1.
    WP_011057406.1. NC_004113.1.

    3D structure databases

    ProteinModelPortali P59065.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 197221.tll1566.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC09118 ; BAC09118 ; BAC09118 .
    GeneIDi 1010930.
    KEGGi tel:tll1566.
    PATRICi 23928498. VBITheElo119873_1642.

    Phylogenomic databases

    eggNOGi COG0266.
    HOGENOMi HOG000020884.
    KOi K10563.
    OMAi AKIHPEK.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: BP-1.

    Entry informationi

    Entry nameiFPG_THEEB
    AccessioniPrimary (citable) accession number: P59065
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 2002
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 87 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