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A3PXU1

- FPG_MYCSJ

UniProt

A3PXU1 - FPG_MYCSJ

Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Mycobacterium sp. (strain JLS)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (03 Apr 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 sitei61 – 611Proton donor; for beta-elimination activityUniRule annotation
    Binding sitei104 – 1041DNAUniRule annotation
    Binding sitei123 – 1231DNAUniRule annotation
    Binding sitei169 – 1691DNAUniRule annotation
    Active sitei279 – 2791Proton donor; for delta-elimination activityUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri255 – 28935FPG-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

    BioCyciMSP164757:GHV3-1941-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:Mjls_1930
    OrganismiMycobacterium sp. (strain JLS)
    Taxonomic identifieri164757 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000002152: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 296295Formamidopyrimidine-DNA glycosylasePRO_1000008720Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi164757.Mjls_1930.

    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 fingeri255 – 28935FPG-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.

    A3PXU1-1 [UniParc]FASTAAdd to Basket

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    MPELPEVEVV RRGLDAHVTG KAITAVRVHH PRAVRRHEAG PADLTARLLG    50
    MRITGTGRRG KYLWLTLDGG DEPLARRAES SVALVVHLGM SGQMLLGPIP 100
    KEDHLRIAAL LDDGTALSFV DQRTFGGWLL ADLVTVDGTD VPVPVAHVAR 150
    DPLDPRFDRD AVVKVLRGKH SEIKRQLLDQ TVVSGIGNIY ADEALWRAKV 200
    NGARLAESLT KPKLAEILDH AADVMRDALG QGGTSFDSLY VNVNGESGYF 250
    DRSLDAYGRE GEPCRRCGAI MRREKFMNRS SFYCPRCQPR PRVRRA 296
    Length:296
    Mass (Da):32,641
    Last modified:April 3, 2007 - v1
    Checksum:i44C32DEF00398F3B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000580 Genomic DNA. Translation: ABN97718.1.
    RefSeqiWP_011855322.1. NC_009077.1.
    YP_001070209.1. NC_009077.1.

    Genome annotation databases

    EnsemblBacteriaiABN97718; ABN97718; Mjls_1930.
    GeneIDi4877652.
    KEGGimjl:Mjls_1930.
    PATRICi18089982. VBIMycSp51234_1931.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000580 Genomic DNA. Translation: ABN97718.1 .
    RefSeqi WP_011855322.1. NC_009077.1.
    YP_001070209.1. NC_009077.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 164757.Mjls_1930.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABN97718 ; ABN97718 ; Mjls_1930 .
    GeneIDi 4877652.
    KEGGi mjl:Mjls_1930.
    PATRICi 18089982. VBIMycSp51234_1931.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci MSP164757:GHV3-1941-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: JLS.

    Entry informationi

    Entry nameiFPG_MYCSJ
    AccessioniPrimary (citable) accession number: A3PXU1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 56 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3