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A1BAN2

- FPG_PARDP

UniProt

A1BAN2 - FPG_PARDP

Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Paracoccus denitrificans (strain Pd 1222)
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 (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 sitei58 – 581Proton donor; for beta-elimination activityUniRule annotation
    Binding sitei100 – 1001DNAUniRule annotation
    Binding sitei119 – 1191DNAUniRule annotation
    Binding sitei160 – 1601DNAUniRule annotation
    Active sitei271 – 2711Proton donor; for delta-elimination activityUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri245 – 28137FPG-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

    BioCyciPDEN318586:GCVQ-4555-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:Pden_4512
    OrganismiParacoccus denitrificans (strain Pd 1222)
    Taxonomic identifieri318586 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus
    ProteomesiUP000000361: Chromosome 2

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 281280Formamidopyrimidine-DNA glycosylasePRO_1000008730Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi318586.Pden_4512.

    Structurei

    3D structure databases

    ProteinModelPortaliA1BAN2.
    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 fingeri245 – 28137FPG-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.
    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.
    PS51066. ZF_FPG_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    A1BAN2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPELPEVETV RRGLQPHLEG RVIARAEARR PDLRWPLPPD LVQVLTGARV    50
    VALRRRSKYI LAELEDRGSL LLHLGMSGRM LIEGESQGDF HRDPAILPRH 100
    DHVVLWNDQG TRITFNDARR FGMVDLVPPG AEHPLLAHLG PEPLSDAFTA 150
    EALAAAFAGR RMPVKAALLD QRIVAGLGNI YVSEALYRAG IDPRRLAGAV 200
    TAPEVAALVG HVRAVLEEAI AAGGSSLRDH RQATGELGYF QHSFRVYGRE 250
    GAPCPTPGCT GTVQRIVQSG RSSFFCPLCQ Q 281
    Length:281
    Mass (Da):30,669
    Last modified:January 23, 2007 - v1
    Checksum:i11C161FC68CF6D44
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000490 Genomic DNA. Translation: ABL72576.1.
    RefSeqiWP_011750737.1. NC_008687.1.
    YP_918272.1. NC_008687.1.

    Genome annotation databases

    EnsemblBacteriaiABL72576; ABL72576; Pden_4512.
    GeneIDi4583062.
    KEGGipde:Pden_4512.
    PATRICi22860246. VBIParDen97112_4475.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000490 Genomic DNA. Translation: ABL72576.1 .
    RefSeqi WP_011750737.1. NC_008687.1.
    YP_918272.1. NC_008687.1.

    3D structure databases

    ProteinModelPortali A1BAN2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 318586.Pden_4512.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABL72576 ; ABL72576 ; Pden_4512 .
    GeneIDi 4583062.
    KEGGi pde:Pden_4512.
    PATRICi 22860246. VBIParDen97112_4475.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PDEN318586:GCVQ-4555-MONOMER.

    Family and domain databases

    HAMAPi MF_00103. Fapy_DNA_glycosyl.
    InterProi IPR015886. DNA_glyclase/AP_lyase_DNA-bd.
    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.
    PS51066. ZF_FPG_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Pd 1222.

    Entry informationi

    Entry nameiFPG_PARDP
    AccessioniPrimary (citable) accession number: A1BAN2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 23, 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3