(data stored in ACNUC7421 zone)

SWISSPROT: A8FPF7_SHESH

ID   A8FPF7_SHESH            Unreviewed;       273 AA.
AC   A8FPF7;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   05-JUL-2017, entry version 79.
DE   RecName: Full=Formamidopyrimidine-DNA glycosylase {ECO:0000256|HAMAP-Rule:MF_00103};
DE            Short=Fapy-DNA glycosylase {ECO:0000256|HAMAP-Rule:MF_00103};
DE            EC=3.2.2.23 {ECO:0000256|HAMAP-Rule:MF_00103};
DE   AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM {ECO:0000256|HAMAP-Rule:MF_00103};
DE            Short=AP lyase MutM {ECO:0000256|HAMAP-Rule:MF_00103};
DE            EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_00103};
GN   Name=mutM {ECO:0000256|HAMAP-Rule:MF_00103};
GN   Synonyms=fpg {ECO:0000256|HAMAP-Rule:MF_00103};
GN   OrderedLocusNames=Ssed_0117 {ECO:0000313|EMBL:ABV34730.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34730.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34730.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34730.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in base excision repair of DNA damaged by
CC       oxidation or by mutagenic agents. Acts as DNA glycosylase that
CC       recognizes and removes damaged bases. Has a preference for
CC       oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has
CC       AP (apurinic/apyrimidinic) lyase activity and introduces nicks in
CC       the DNA strand. Cleaves the DNA backbone by beta-delta elimination
CC       to generate a single-strand break at the site of the removed base
CC       with both 3'- and 5'-phosphates. {ECO:0000256|HAMAP-Rule:MF_00103,
CC       ECO:0000256|SAAS:SAAS00635477}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of DNA containing ring-opened 7-
CC       methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC       methyl)formamidopyrimidine. {ECO:0000256|HAMAP-Rule:MF_00103,
CC       ECO:0000256|SAAS:SAAS00635490}.
CC   -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
CC       apyrimidinic site in DNA is broken by a beta-elimination reaction,
CC       leaving a 3'-terminal unsaturated sugar and a product with a
CC       terminal 5'-phosphate. {ECO:0000256|HAMAP-Rule:MF_00103,
CC       ECO:0000256|SAAS:SAAS00643435}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00103};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00103};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00103,
CC       ECO:0000256|SAAS:SAAS00635466}.
CC   -!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|HAMAP-
CC       Rule:MF_00103, ECO:0000256|SAAS:SAAS00643420}.
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DR   EMBL; CP000821; ABV34730.1; -; Genomic_DNA.
DR   ProteinModelPortal; A8FPF7; -.
DR   STRING; 425104.Ssed_0117; -.
DR   EnsemblBacteria; ABV34730; ABV34730; Ssed_0117.
DR   KEGG; sse:Ssed_0117; -.
DR   eggNOG; ENOG4105ERD; Bacteria.
DR   eggNOG; COG0266; LUCA.
DR   HOGENOM; HOG000020881; -.
DR   KO; K10563; -.
DR   OMA; GVHLRMT; -.
DR   OrthoDB; POG091H01RH; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   HAMAP; MF_00103; Fapy_DNA_glycosyl; 1.
DR   InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR   InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
DR   InterPro; IPR020629; Formamido-pyr_DNA_Glyclase.
DR   InterPro; IPR012319; FPG_cat.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR   InterPro; IPR010663; Znf_FPG/IleRS.
DR   Pfam; PF01149; Fapy_DNA_glyco; 1.
DR   Pfam; PF06831; H2TH; 1.
DR   Pfam; PF06827; zf-FPG_IleRS; 1.
DR   SMART; SM00898; Fapy_DNA_glyco; 1.
DR   SMART; SM01232; H2TH; 1.
DR   SUPFAM; SSF46946; SSF46946; 1.
DR   SUPFAM; SSF81624; SSF81624; 1.
DR   TIGRFAMs; TIGR00577; fpg; 1.
DR   PROSITE; PS51068; FPG_CAT; 1.
DR   PROSITE; PS01242; ZF_FPG_1; 1.
DR   PROSITE; PS51066; ZF_FPG_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FPF7.
DR   SWISS-2DPAGE; A8FPF7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS00643418};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS00643382};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS00643405};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS00643419, ECO:0000313|EMBL:ABV34730.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS00643430, ECO:0000313|EMBL:ABV34730.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS00643421};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS00640292};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS00643397};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00103, ECO:0000256|SAAS:SAAS00640325};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00103, ECO:0000256|PROSITE-
KW   ProRule:PRU00391, ECO:0000256|SAAS:SAAS00640308}.
FT   DOMAIN        4    114       FPG_CAT. {ECO:0000259|PROSITE:PS51068}.
FT   DOMAIN      238    272       FPG-type. {ECO:0000259|PROSITE:PS51066}.
FT   ACT_SITE      4      4       Schiff-base intermediate with DNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00103}.
FT   ACT_SITE      5      5       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00103}.
FT   ACT_SITE     59     59       Proton donor; for beta-elimination
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_00103}.
FT   ACT_SITE    262    262       Proton donor; for delta-elimination
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_00103}.
FT   BINDING      92     92       DNA. {ECO:0000256|HAMAP-Rule:MF_00103}.
FT   BINDING     111    111       DNA. {ECO:0000256|HAMAP-Rule:MF_00103}.
FT   BINDING     153    153       DNA. {ECO:0000256|HAMAP-Rule:MF_00103}.
SQ   SEQUENCE   273 AA;  30194 MW;  35F807CC6ADAA14D CRC64;
     MNMPELPEVE VTRQGITPHL VDQQATALTV RNASLRWPVP DIAQQIVGET IRNVRRRAKY
     LLIDTDAGTT IVHLGMSGSL RIVSRNTPVE KHDHIDLELA SGKILRFNDP RRFGAWLWCE
     LPEEAHPLLS KLGPEPLKDG FNPTYLEQIL KNKKKAIKLC LMDNHIVVGV GNIYANEALF
     AAGIHPETQA GNVDTERLTI LVTEVKQILA NAIKQGGTTL KDFTNAEGKP GYFAQKLHVY
     GRGGETCTQC GNLLSEIKLG QRATVFCGLC QTK
//

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