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Q9RX22

- FPG_DEIRA

UniProt

Q9RX22 - FPG_DEIRA

Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 4 (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 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 sitei53 – 531Proton donor; for beta-elimination activityBy similarity
    Binding sitei91 – 911DNABy similarity
    Binding sitei110 – 1101DNABy similarity
    Binding sitei152 – 1521DNABy similarity
    Active sitei263 – 2631Proton donor; for delta-elimination activityBy similarity

    Regions

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

    Enzyme and pathway databases

    BioCyciDRAD243230:GH46-504-MONOMER.

    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:DR_0493
    OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
    Taxonomic identifieri243230 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
    ProteomesiUP000002524: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 280279Formamidopyrimidine-DNA glycosylasePRO_0000170821Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi243230.DR_0493.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9RX22.
    SMRiQ9RX22. Positions 2-274.
    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 fingeri239 – 27335FPG-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0266.
    HOGENOMiHOG000020884.
    KOiK10563.
    OMAiDHVDLKL.
    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.

    Q9RX22-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPELPEVETT RRKIEPLLRG KTIERIVHDA PHRYRNTERA HGRQVRGLTR    50
    RGKYLLLHLA AADAAEDEPH DLELIVHLGM TGGFRLEEGP HTRVTFELGS 100
    GEKLYFNDPR RFGKVVAVAP GDYASMPTLA AMGPEPLSDD FTEAEFVALA 150
    ARCGPVKPWL LSQKPVSGVG NIYADESLWH ARLHPAQTRL NADEAGRLYR 200
    AIREVMAAAV DKGGSSLGNG VGNYRQHDGE GGGFQHSHHV YGRAGQPCDR 250
    CGTPIEKIVL GQRGTHFCPV CQPLRTDRSA 280
    Length:280
    Mass (Da):30,819
    Last modified:January 23, 2007 - v4
    Checksum:i9785ECBDF0CB3A44
    GO

    Sequence cautioni

    The sequence AAF10070.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000513 Genomic DNA. Translation: AAF10070.1. Different initiation.
    PIRiH75512.
    RefSeqiNP_294216.1. NC_001263.1.

    Genome annotation databases

    EnsemblBacteriaiAAF10070; AAF10070; DR_0493.
    GeneIDi1799429.
    KEGGidra:DR_0493.
    PATRICi21628510. VBIDeiRad64572_0671.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000513 Genomic DNA. Translation: AAF10070.1 . Different initiation.
    PIRi H75512.
    RefSeqi NP_294216.1. NC_001263.1.

    3D structure databases

    ProteinModelPortali Q9RX22.
    SMRi Q9RX22. Positions 2-274.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243230.DR_0493.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF10070 ; AAF10070 ; DR_0493 .
    GeneIDi 1799429.
    KEGGi dra:DR_0493.
    PATRICi 21628510. VBIDeiRad64572_0671.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci DRAD243230:GH46-504-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 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

    Entry informationi

    Entry nameiFPG_DEIRA
    AccessioniPrimary (citable) accession number: Q9RX22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 19, 2002
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 96 of the entry and version 4 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