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Q9A131

- FPG_STRP1

UniProt

Q9A131 - FPG_STRP1

Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Streptococcus pyogenes serotype M1
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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 sitei110 – 1101DNAUniRule annotation
    Active sitei262 – 2621Proton donor; for delta-elimination activityUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri238 – 27235FPG-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

    BioCyciSPYO160490:GJ81-412-MONOMER.
    SPYO293653:GHFC-463-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:SPy_0497, M5005_Spy0408
    OrganismiStreptococcus pyogenes serotype M1
    Taxonomic identifieri301447 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000000750: Chromosome, UP000002702: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 275274Formamidopyrimidine-DNA glycosylasePRO_0000170871Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi160490.SPy_0497.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9A131.
    SMRiQ9A131. Positions 2-273.
    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 fingeri238 – 27235FPG-typeUniRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0266.
    HOGENOMiHOG000020885.
    KOiK10563.
    OMAiQNTLGMN.
    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.

    Q9A131-1 [UniParc]FASTAAdd to Basket

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    MPELPEVETV RRGLETLVLG QEIVAVTLKV PKMVKTDLET FALTLPGQII    50
    QSVGRRGKYL LIDLGQLVLV SHLRMEGKYL LFPDEVPDNK HFHVFFELKN 100
    GSTLVYQDVR KFGTFDLIAK SQLSAFFAKR KLGPEPKKET FKLKTFEAAL 150
    LSSQKPIKPH LLDQTLVAGL GNIYVDEVLW AAKVHPETAS SRLNKAEIKR 200
    LHDETIRILA LGIEKGGSTV RTYRNALGAD GTMQDYLQVY GQTGKPCPRC 250
    GQAIVKLKVG GRGTHICPKC QKKRL 275
    Length:275
    Mass (Da):30,702
    Last modified:January 23, 2007 - v3
    Checksum:i11DF7D4CE2EE6D9E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004092 Genomic DNA. Translation: AAK33498.1.
    CP000017 Genomic DNA. Translation: AAZ51026.1.
    RefSeqiNP_268777.1. NC_002737.1.
    YP_281771.1. NC_007297.1.

    Genome annotation databases

    EnsemblBacteriaiAAK33498; AAK33498; SPy_0497.
    AAZ51026; AAZ51026; M5005_Spy0408.
    GeneIDi3572502.
    900727.
    KEGGispy:SPy_0497.
    spz:M5005_Spy_0408.
    PATRICi19714709. VBIStrPyo79812_0423.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004092 Genomic DNA. Translation: AAK33498.1 .
    CP000017 Genomic DNA. Translation: AAZ51026.1 .
    RefSeqi NP_268777.1. NC_002737.1.
    YP_281771.1. NC_007297.1.

    3D structure databases

    ProteinModelPortali Q9A131.
    SMRi Q9A131. Positions 2-273.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 160490.SPy_0497.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK33498 ; AAK33498 ; SPy_0497 .
    AAZ51026 ; AAZ51026 ; M5005_Spy0408 .
    GeneIDi 3572502.
    900727.
    KEGGi spy:SPy_0497.
    spz:M5005_Spy_0408.
    PATRICi 19714709. VBIStrPyo79812_0423.

    Phylogenomic databases

    eggNOGi COG0266.
    HOGENOMi HOG000020885.
    KOi K10563.
    OMAi QNTLGMN.
    OrthoDBi EOG6QP131.

    Enzyme and pathway databases

    BioCyci SPYO160490:GJ81-412-MONOMER.
    SPYO293653:GHFC-463-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 700294 / SF370 / Serotype M1.
    2. "Evolutionary origin and emergence of a highly successful clone of serotype M1 group A Streptococcus involved multiple horizontal gene transfer events."
      Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K., Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P., Musser J.M.
      J. Infect. Dis. 192:771-782(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-947 / MGAS5005 / Serotype M1.

    Entry informationi

    Entry nameiFPG_STRP1
    AccessioniPrimary (citable) accession number: Q9A131
    Secondary accession number(s): Q490E2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2002
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 94 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