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Q9K855

- FPG_BACHD

UniProt

Q9K855 - FPG_BACHD

Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 100 (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 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 sitei60 – 601Proton donor; for beta-elimination activityBy similarity
    Binding sitei93 – 931DNABy similarity
    Binding sitei112 – 1121DNABy similarity
    Active sitei264 – 2641Proton donor; for delta-elimination activityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri240 – 27435FPG-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

    BioCyciBHAL272558:GJC5-3251-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:BH3152
    OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
    Taxonomic identifieri272558 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001258: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 274273Formamidopyrimidine-DNA glycosylasePRO_0000170810Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi272558.BH3152.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9K855.
    SMRiQ9K855. 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 fingeri240 – 27435FPG-typeAdd
    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.

    Q9K855-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPELPEVETV RRTLAELVIG KTIEQVDVGW AKMIKRPDDV DQFKWLLKGQ    50
    TIRSMGRRGK FLLFHLDDYT LVSHLRMEGR YGLYQQNESV AKHTHVRFVF 100
    GDGTELRYQD VRKFGTMHLF QSGREQMEPP LAKLGVEPFS DQFSAKLLTE 150
    RLSKTSRKIK SALLDQGIIV GLGNIYVDEA LFRARIHPER LAKDVTVAEV 200
    KILHQAILNT LTEAVNLGGS SIKSYVNGQG EMGMFQQRLD VYGRKGETCR 250
    QCGTPITKTV VGGRGTHFCS VCQK 274
    Length:274
    Mass (Da):30,999
    Last modified:January 23, 2007 - v3
    Checksum:iB8ED6EAFFAFC38E1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000004 Genomic DNA. Translation: BAB06871.1.
    PIRiH84043.
    RefSeqiNP_244018.1. NC_002570.2.
    WP_010899295.1. NC_002570.2.

    Genome annotation databases

    EnsemblBacteriaiBAB06871; BAB06871; BAB06871.
    GeneIDi890627.
    KEGGibha:BH3152.
    PATRICi18943560. VBIBacHal18977_3279.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000004 Genomic DNA. Translation: BAB06871.1 .
    PIRi H84043.
    RefSeqi NP_244018.1. NC_002570.2.
    WP_010899295.1. NC_002570.2.

    3D structure databases

    ProteinModelPortali Q9K855.
    SMRi Q9K855. Positions 2-274.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272558.BH3152.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB06871 ; BAB06871 ; BAB06871 .
    GeneIDi 890627.
    KEGGi bha:BH3152.
    PATRICi 18943560. VBIBacHal18977_3279.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BHAL272558:GJC5-3251-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. "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
      Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
      Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

    Entry informationi

    Entry nameiFPG_BACHD
    AccessioniPrimary (citable) accession number: Q9K855
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 100 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