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A8YWE6

- FPG_LACH4

UniProt

A8YWE6 - FPG_LACH4

Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Lactobacillus helveticus (strain DPC 4571)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (15 Jan 2008)
      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 sitei92 – 921DNAUniRule annotation
    Binding sitei111 – 1111DNAUniRule annotation
    Binding sitei154 – 1541DNAUniRule annotation
    Active sitei263 – 2631Proton donor; for delta-elimination activityUniRule annotation

    Regions

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

    BioCyciLHEL405566:GJEN-1428-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:lhv_1616
    OrganismiLactobacillus helveticus (strain DPC 4571)
    Taxonomic identifieri405566 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus
    ProteomesiUP000000790: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 276275Formamidopyrimidine-DNA glycosylasePRO_1000071309Add
    BLAST

    Proteomic databases

    PRIDEiA8YWE6.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi405566.lhv_1616.

    Structurei

    3D structure databases

    ProteinModelPortaliA8YWE6.
    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 fingeri239 – 27335FPG-typeUniRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0266.
    HOGENOMiHOG000020885.
    KOiK10563.
    OMAiKIVATDH.
    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.

    A8YWE6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPEMPEVETV RRTLIPLIKG KTIEKVILWY PKIVATDHEK FLSELPGKKI    50
    IDIDRYAKYL LIRLSDNLTI VSHLRMEGKY HLTTSDAPKD KHDHVEFIFT 100
    DGTALRYNDV RKFGRMQLIL TGTERQTTGI GKLGYEPNSS EFTSEYLVNG 150
    LKRKKKNIKN TLLDQSVVAG LGNIYVDEVL WRTKIHPLSQ ANKIPAEKVM 200
    ELHDQINQII TEAIKLQGTT VHSFLNANGQ VGGFQSKLQV YGHVGEPCPV 250
    CGTKFEKIKV NGRGTTFCPH CQVIYK 276
    Length:276
    Mass (Da):31,318
    Last modified:January 15, 2008 - v1
    Checksum:i2EF245570D7CB7A6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000517 Genomic DNA. Translation: ABX27532.1.
    RefSeqiYP_001577833.1. NC_010080.1.

    Genome annotation databases

    EnsemblBacteriaiABX27532; ABX27532; lhv_1616.
    GeneIDi5771333.
    KEGGilhe:lhv_1616.
    PATRICi22235504. VBILacHel91643_1701.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000517 Genomic DNA. Translation: ABX27532.1 .
    RefSeqi YP_001577833.1. NC_010080.1.

    3D structure databases

    ProteinModelPortali A8YWE6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 405566.lhv_1616.

    Proteomic databases

    PRIDEi A8YWE6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABX27532 ; ABX27532 ; lhv_1616 .
    GeneIDi 5771333.
    KEGGi lhe:lhv_1616.
    PATRICi 22235504. VBILacHel91643_1701.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci LHEL405566:GJEN-1428-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. "Genome sequence of Lactobacillus helveticus: an organism distinguished by selective gene loss and IS element expansion."
      Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K., McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F., Beresford T., Ross R.P.
      J. Bacteriol. 190:727-735(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DPC 4571.

    Entry informationi

    Entry nameiFPG_LACH4
    AccessioniPrimary (citable) accession number: A8YWE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 47 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