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Q67R59

- FPG_SYMTH

UniProt

Q67R59 - FPG_SYMTH

Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Symbiobacterium thermophilum (strain T / IAM 14863)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (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 sitei92 – 921DNAUniRule annotation
    Binding sitei111 – 1111DNAUniRule annotation
    Binding sitei154 – 1541DNAUniRule annotation
    Active sitei263 – 2631Proton donor; for delta-elimination activityUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri239 – 27335FPG-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

    BioCyciSTHE292459:GJMM-909-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:STH849
    OrganismiSymbiobacterium thermophilum (strain T / IAM 14863)
    Taxonomic identifieri292459 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiales Family XVIII. Incertae SedisSymbiobacterium
    ProteomesiUP000000417: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 305304Formamidopyrimidine-DNA glycosylasePRO_0000228477Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi292459.STH849.

    Structurei

    3D structure databases

    ProteinModelPortaliQ67R59.
    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 fingeri239 – 27335FPG-typeUniRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0266.
    HOGENOMiHOG000020884.
    KOiK10563.
    OMAiIYCSESL.
    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.

    Q67R59-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPELPEVETV RRTLCPRVVG RRIRRVEILT PRQIYHPDPA TFAADLEGAV    50
    FDDIERRGKY LLFRLGPRIL VAHLRMSGHL YVCGPEAPRP RHLHVVFHLD 100
    DGGELRYADQ RKFGGFHLLG PGGEGMPPGL ANLGPEPLSP EFTPQVLAER 150
    LAGRHTSIKA ALLNQALVAG LGNIYADEAL FCARIHPARE AGSLTPAEVE 200
    RLHGCIRRVL LRAVERRGTT FSLYRDGEGN EGDMYDELQV FDRAGEPCPV 250
    CGTPIRKVAV AQRGTHFCPR CQPVPEGVAL SPRRARPGRR GNSVRVAAEP 300
    PGTYE 305
    Length:305
    Mass (Da):33,684
    Last modified:January 23, 2007 - v3
    Checksum:iB47EDEC0828DB164
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP006840 Genomic DNA. Translation: BAD39834.1.
    RefSeqiWP_011194981.1. NC_006177.1.
    YP_074678.1. NC_006177.1.

    Genome annotation databases

    EnsemblBacteriaiBAD39834; BAD39834; STH849.
    GeneIDi2981069.
    KEGGisth:STH849.
    PATRICi23779816. VBISymThe116959_0838.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP006840 Genomic DNA. Translation: BAD39834.1 .
    RefSeqi WP_011194981.1. NC_006177.1.
    YP_074678.1. NC_006177.1.

    3D structure databases

    ProteinModelPortali Q67R59.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 292459.STH849.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD39834 ; BAD39834 ; STH849 .
    GeneIDi 2981069.
    KEGGi sth:STH849.
    PATRICi 23779816. VBISymThe116959_0838.

    Phylogenomic databases

    eggNOGi COG0266.
    HOGENOMi HOG000020884.
    KOi K10563.
    OMAi IYCSESL.
    OrthoDBi EOG6QP131.

    Enzyme and pathway databases

    BioCyci STHE292459:GJMM-909-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. "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism."
      Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.
      Nucleic Acids Res. 32:4937-4944(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: T / IAM 14863.

    Entry informationi

    Entry nameiFPG_SYMTH
    AccessioniPrimary (citable) accession number: Q67R59
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 77 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